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Correction: 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson’s disease-associated mutations and regulates cytoplasmic localization

Biochem J (2025) 482 (12): 901–902.

https://doi.org/10.1042/BJ20100483_COR

Published: 18 June 2025

... disease pathogenic mutation phosphorylation ...

View articletitled, Correction: 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson’s disease-associated mutations and regulates cytoplasmic localization

Articles

Correction: Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

Biochem J (2025) 482 (07): 357–358.

https://doi.org/10.1042/BCJ20200937_COR

Published: 26 March 2025

... kinase leucine rich repeat kinase phosphorylation Rab GTPase It has come to the attention of the authors of the article “Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms” (DOI: 10.1042/BCJ20200937...

View articletitled, Correction: Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

Articles

Noncanonical RGS14 structural determinants control hormone-sensitive NPT2A-mediated phosphate transport

W. Bruce Sneddon, Suneela Ramineni, G. Emme Van Doorn, John R. Hepler, Peter A. Friedman

Biochem J (2025) 482 (03): 135–146.

https://doi.org/10.1042/BCJ20240122

Published: 30 January 2025

... action. Examination of the α-helical linker region suggested candidate serine residues that might facilitate regulatory activities. RGS14 Ser 266 and Ser 269 are phosphorylated in response to PTH and FGF23, and replacement of these residues by Ala eliminated the actions of RGS14 on hormone-sensitive...

View articletitled, Noncanonical RGS14 structural determinants control hormone-sensitive NPT2A-mediated phosphate transport

Includes: Supplementary data

Articles

Filamin A regulates platelet shape change and contractile force generation via phosphorylation of the myosin light chain

Felix Hong, Molly Y. Mollica, Kalyan Golla, Enoli De Silva, Nathan J. Sniadecki, José A. López, Hugh Kim

Biochem J (2024) 481 (20): 1395–1410.

https://doi.org/10.1042/BCJ20240114

Published: 07 October 2024

... agonists such as thrombin. Platelet shape change is driven by a dynamic remodeling of the actin cytoskeleton. Actin filaments interact with the protein myosin, which is phosphorylated on the myosin light chain (MLC) upon platelet activation. Actin-myosin interactions trigger contraction of the actin...

View articletitled, Filamin A regulates platelet shape change and contractile force generation via phosphorylation of the myosin light chain

Includes: Supplementary data

Articles

Charting the importance of filamin A posttranslational modifications

Kyle D. Shead, Veneta Salyahetdinova, George S. Baillie

Biochem J (2024) 481 (13): 865–881.

https://doi.org/10.1042/BCJ20240121

Published: 03 July 2024

... phosphorylation, irreversible cleavage, ubiquitin mediated degradation, hydroxylation and O-GlcNAcylation, with preliminary evidence of tyrosylation, carbonylation and acetylation. Each modification and its relation to filamin A function will be described here. These modifications are often aberrantly applied...

View articletitled, Charting the importance of filamin A posttranslational modifications

Articles

The role of phosphorylation in calmodulin-mediated gating of human AQP0

Stefan Kreida, Jennifer Virginia Roche, Julie Winkel Missel, Tamim Al-Jubair, Carl Johan Hagströmer, Veronika Wittenbecher, Sara Linse, Pontus Gourdon, Susanna Törnroth-Horsefield

Biochem J (2024) 481 (1): 17–32.

https://doi.org/10.1042/BCJ20230158

Published: 04 January 2024

... lens transparency. AQP0 binds the Ca 2+ -sensing protein calmodulin (CaM) and this interaction is believed to gate its water permeability by closing the water-conducting pore. Here, we express recombinant and functional human AQP0 in Pichia pastoris and investigate how phosphorylation affects...

View articletitled, The role of phosphorylation in calmodulin-mediated gating of human AQP0

Includes: Supplementary data

Articles

TOR complex 2 is a master regulator of plasma membrane homeostasis

In Collection

Awards

Jeremy Thorner

Biochem J (2022) 479 (18): 1917–1940.

https://doi.org/10.1042/BCJ20220388

Published: 23 September 2022

...-regulation of the phosphorylation and thus the activity of its essential downstream effector the AGC family protein kinase Ypk1. Through the ensuing effect on the efficiency with which Ypk1 phosphorylates multiple substrates that control diverse processes, membrane homeostasis is maintained. Thus, the major...

View articletitled, TOR complex 2 is a master regulator of plasma membrane homeostasis

Includes: Supplementary data

Articles

Divergent kinase WNG1 is regulated by phosphorylation of an atypical activation sub-domain

Pravin S. Dewangan, Tsebaot G. Beraki, E. Ariana Paiz, Delia Appiah Mensah, Zhe Chen, Michael L. Reese

Biochem J (2022) 479 (17): 1877–1889.

https://doi.org/10.1042/BCJ20220076

Published: 16 September 2022

... into the membrane after trafficking through the parasite secretory system as soluble, chaperoned complexes. A regulator of this process is an atypical protein kinase called WNG1. Phosphorylation by WNG1 appears to serve as a switch for membrane integration. However, like its substrates, WNG1 is secreted from...

View articletitled, Divergent kinase WNG1 is regulated by phosphorylation of an atypical activation sub-domain

Includes: Supplementary data

Articles

RIP1 post-translational modifications

In Collection

Cell death and survival

Eugene Varfolomeev, Domagoj Vucic

Biochem J (2022) 479 (9): 929–951.

https://doi.org/10.1042/BCJ20210725

Published: 06 May 2022

... by caspase-8, RIP1 autophosphorylation, and phosphorylation by a number of signaling kinases can greatly impact cellular fate. Disruption of the tightly regulated RIP1 modifications can lead to signaling disbalance in TNF and/or TLR controlled and other inflammatory pathways, and result in severe human...

View articletitled, RIP1 post-translational modifications

Articles

Distinct phosphorylation signals drive acceptor versus free ubiquitin chain targeting by parkin

Karen M. Dunkerley, Anne C. Rintala-Dempsey, Giulia Salzano, Roya Tadayon, Dania Hadi, Kathryn R. Barber, Helen Walden, Gary S. Shaw

Biochem J (2022) 479 (6): 751–766.

https://doi.org/10.1042/BCJ20210741

Published: 28 March 2022

.... Parkin activation involves binding of a phosphorylated ubiquitin (pUb), followed by phosphorylation of the Ubl domain in parkin, both mediated by the OMM kinase, PINK1. How an OMM protein is selected for ubiquitination is unclear. Parkin targeted OMM proteins have little structural or sequence similarity...

View articletitled, Distinct phosphorylation signals drive acceptor versus free ubiquitin chain targeting by parkin

Includes: Supplementary data

Articles

Conformational plasticity of the ULK3 kinase domain

Sebastian Mathea, Eidarus Salah, Cynthia Tallant, Deep Chatterjee, Benedict-Tilman Berger, Rebecca Konietzny, Susanne Müller, Benedikt M. Kessler, Stefan Knapp

Biochem J (2021) 478 (14): 2811–2823.

https://doi.org/10.1042/BCJ20210257

Published: 23 July 2021

...–substrate interactions phosphorylation small-molecule inhibitor ULK kinase Membrane abscission is the ultimate step in several physiologically important processes such as exosome budding and cytokinesis [ 1 ]. Any connection between two membrane substructures is cut, setting free extracellular...

View articletitled, Conformational plasticity of the ULK3 kinase domain

Includes: Supplementary data

Articles

Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

In Collection

Protein structure and function

Asad U. Malik, Athanasios Karapetsas, Raja S. Nirujogi, Sebastian Mathea, Deep Chatterjee, Prosenjit Pal, Pawel Lis, Matthew Taylor, Elena Purlyte, Robert Gourlay, Mark Dorward, Simone Weidlich, Rachel Toth, Nicole K. Polinski, Stefan Knapp, Francesca Tonelli, Dario R. Alessi

Biochem J (2021) 478 (3): 553–578.

https://doi.org/10.1042/BCJ20200937

Published: 10 February 2021

... mutations in LRRK2 that enhance kinase activity cause Parkinson's disease. LRRK2 phosphorylates a subset of Rab GTPases including Rab8A and Rab10 within its effector binding motif. Here, we explore whether LRRK1, a less studied homolog of LRRK2 that regulates growth factor receptor trafficking...

View articletitled, Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

Includes: Supplementary data

Articles

Structural insights into DNA double-strand break signaling

Rashmi Panigrahi, J. N. Mark Glover

Biochem J (2021) 478 (1): 135–156.

https://doi.org/10.1042/BCJ20200066

Published: 13 January 2021

... structural approaches to visualize and build a more complete understanding of protein dynamics at the break site. © 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2021 DNA damage signaling mediators phosphorylation sensors ubiquitylation...

View articletitled, Structural insights into DNA double-strand break signaling

Articles

PARP-1 activation after oxidative insult promotes energy stress-dependent phosphorylation of YAP1 and reduces cell viability

Sandra M. Martín-Guerrero, Pedro Casado, Maruan Hijazi, Vinothini Rajeeve, Julio Plaza-Díaz, Francisco Abadía-Molina, Julio Navascués, Miguel A. Cuadros, Pedro R. Cutillas, David Martín-Oliva

Biochem J (2020) 477 (23): 4491–4513.

https://doi.org/10.1042/BCJ20200525

Published: 03 December 2020

...-based phosphoproteomics in WRL68 cells showed that the oxidative damage induced by H 2 O 2 increased the phosphorylation of YAP1, a transcriptional co-activator involved in cell survival, and modified the phosphorylation of other proteins involved in transcription. Genetic or pharmacological inhibition...

View articletitled, PARP-1 activation after oxidative insult promotes energy stress-dependent phosphorylation of YAP1 and reduces cell viability

Includes: Supplementary data

Articles

RORα phosphorylation by casein kinase 1α as glucose signal to regulate estrogen sulfation in human liver cells

Hao Hu, Masahiko Negishi

Biochem J (2020) 477 (18): 3583–3598.

https://doi.org/10.1042/BCJ20200427

Published: 28 September 2020

... HepG2 cells cultured in high glucose (450 mg/dl) medium. Here, we have investigated this glucose signal that leads to phosphorylation of nuclear receptor RORα (NR1F1) at Ser100 and the transcription mechanism by which phosphorylated RORα transduces this signal to nuclear receptor HNF4α, activating...

View articletitled, RORα phosphorylation by casein kinase 1α as glucose signal to regulate estrogen sulfation in human liver cells

Includes: Supplementary data

Articles

AMP-activated protein kinase regulates alternative pre-mRNA splicing by phosphorylation of SRSF1

Eri Matsumoto, Kaho Akiyama, Takuya Saito, Yu Matsumoto, Ken-Ichi Kobayashi, Jun Inoue, Yuji Yamamoto, Tsukasa Suzuki

Biochem J (2020) 477 (12): 2237–2248.

https://doi.org/10.1042/BCJ20190894

Published: 24 June 2020

... substrate. AMPK directly phosphorylated SRSF1 at Ser133 in an RNA recognition motif. Ser133 phosphorylation suppressed the interaction between SRSF1 and specific RNA sequences without altering the subcellular localization of SRSF1. Moreover, AMPK regulated the SRSF1-mediated alternative pre-mRNA splicing...

View articletitled, AMP-activated protein kinase regulates alternative pre-mRNA splicing by phosphorylation of SRSF1

Articles

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

Nikolai N. Sluchanko

Biochem J (2020) 477 (7): 1219–1225.

https://doi.org/10.1042/BCJ20200084

Published: 09 April 2020

...Nikolai N. Sluchanko Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation...

View articletitled, Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

Articles

Ufd1 phosphorylation at serine 229 negatively regulates endoplasmic reticulum-associated degradation by inhibiting the interaction of Ufd1 with VCP

Quynh-Anh Thi Nguyen, Juyong Choi, Jin Kuk Yang, Sang Yoon Lee

Biochem J (2019) 476 (18): 2561–2577.

https://doi.org/10.1042/BCJ20190254

Published: 20 September 2019

... degradation protein 1 (Ufd1) with VCP via its SHP box motif ( 228 F-S-G-S-G-N-R-L 235 ) is required for ERAD. However, the mechanisms by which the VCP–Ufd1 interaction is regulated are not well understood. Here, we found that the serine 229 residue located in the Ufd1 SHP box is phosphorylated in vitro...

View articletitled, Ufd1 phosphorylation at serine 229 negatively regulates endoplasmic reticulum-associated degradation by inhibiting the interaction of Ufd1 with VCP

Articles

RhoBTB1 interacts with ROCKs and inhibits invasion

Raquel B. Haga, Ritu Garg, Francesca Collu, Bárbara Borda D'Agua, Sofia T. Menéndez, Audrey Colomba, Franca Fraternali, Anne J. Ridley

Biochem J (2019) 476 (17): 2499–2514.

https://doi.org/10.1042/BCJ20190203

Published: 13 September 2019

... with ROCK1 is via its Rho domain. The Rho domain binds to the coiled-coil region of ROCK1 close to its kinase domain. We identify two amino acids within the Rho domain that alter RhoBTB1 association with ROCK1. RhoBTB1 is a substrate for ROCK1, and mutation of putative phosphorylation sites reduces its...

View articletitled, RhoBTB1 interacts with ROCKs and inhibits invasion

Includes: Supplementary data

Articles

Nitration-induced ubiquitination and degradation control quality of ERK1

Yuanya Zhang, Xiahe Huang, Jinlong Wang, Xiaorong Wang, Xiaofei Liu, Yuhang Chen, Wu Xu, Yingchun Wang

Biochem J (2019) 476 (13): 1911–1926.

https://doi.org/10.1042/BCJ20190240

Published: 02 July 2019

... License 4.0 (CC BY) . Phosphorylation plays a critical role in regulating ERK activity and localization. It has long been established that TEY motif phosphorylation is important for ERK nuclear translocation [ 5 ]. The recent discovery of the nuclear translocation signals (NTS) on ERKs further...

View articletitled, Nitration-induced ubiquitination and degradation control quality of ERK1

Includes: Supplementary data

Articles

G protein subunit phosphorylation as a regulatory mechanism in heterotrimeric G protein signaling in mammals, yeast, and plants

David Chakravorty, Sarah M. Assmann

Biochem J (2018) 475 (21): 3331–3357.

https://doi.org/10.1042/BCJ20160819

Published: 09 November 2018

... are fundamental to human health [ Biochimica et Biophysica Acta (2007) 1768 , 994–1005] and are the target of >30% of pharmaceuticals in clinical use [ Biotechnology Advances (2013) 31 , 1676–1694; Nature Reviews Drug Discovery (2017) 16 , 829–842]. This review focuses on phosphorylation of G protein subunits...

View articletitled, G protein subunit phosphorylation as a regulatory mechanism in heterotrimeric G protein signaling in mammals, yeast, and plants

Includes: Supplementary data

Articles

PKA-site phosphorylation of importin13 regulates its subcellular localization and nuclear transport function

Xujie Liu, Wenbo Lin, Xiuyu Shi, Rebecca G. Davies, Kylie M. Wagstaff, Tao Tao, David A. Jans

Biochem J (2018) 475 (16): 2699–2712.

https://doi.org/10.1042/BCJ20180082

Published: 31 August 2018

... to undergo phosphorylation, but the impact of this on function has not been investigated. Here, we show for the first time that IPO13 is phosphorylated by cAMP-dependent protein kinase A specifically at serine 193. Results from fluorescence recovery after photobleaching and fluorescence loss...

View articletitled, PKA-site phosphorylation of importin13 regulates its subcellular localization and nuclear transport function

Articles

The Parkinson's disease VPS35[D620N] mutation enhances LRRK2-mediated Rab protein phosphorylation in mouse and human

In Collection

Editors' pick of research highlights published in the Biochemical Journal in 2018 & 2019

Rafeeq Mir, Francesca Tonelli, Pawel Lis, Thomas Macartney, Nicole K. Polinski, Terina N. Martinez, Meng-Yun Chou, Andrew J.M. Howden, Theresa König, Christoph Hotzy, Ivan Milenkovic, Thomas Brücke, Alexander Zimprich, Esther Sammler, Dario R. Alessi

Biochem J (2018) 475 (11): 1861–1883.

https://doi.org/10.1042/BCJ20180248

Published: 06 June 2018

... repeat protein kinase-2) and VPS35 genes result in autosomal dominant Parkinson's disease. The VPS35 gene encodes for the cargo-binding component of the retromer complex, while LRRK2 modulates vesicular trafficking by phosphorylating a subgroup of Rab proteins. Pathogenic mutations in LRRK2 increase its...

View articletitled, The Parkinson's disease VPS35[D620N] mutation enhances LRRK2-mediated Rab protein phosphorylation in mouse and human

Includes: Supplementary data

Articles

Biological role of site-specific O-glycosylation in cell adhesion activity and phosphorylation of osteopontin

Midori Oyama, Yoshinobu Kariya, Yukiko Kariya, Kana Matsumoto, Mayumi Kanno, Yoshiki Yamaguchi, Yasuhiro Hashimoto

Biochem J (2018) 475 (9): 1583–1595.

https://doi.org/10.1042/BCJ20170205

Published: 09 May 2018

... lacking five O-glycosylation sites (Thr 134 /Thr 138 /Thr 143 /Thr 147 /Thr 152 ) in the threonine/proline-rich region increased cell adhesion activity and phosphorylation compared with the wild type. However, the role of O-glycosylation in cell adhesion activity and phosphorylation of OPN remains...

View articletitled, Biological role of site-specific O-glycosylation in cell adhesion activity and phosphorylation of osteopontin

Includes: Supplementary data

Articles

Phosphorylation of BACH1 switches its function from transcription factor to mitotic chromosome regulator and promotes its interaction with HMMR

Jie Li, Hiroki Shima, Hironari Nishizawa, Masatoshi Ikeda, Andrey Brydun, Mitsuyo Matsumoto, Hiroki Kato, Yuriko Saiki, Liang Liu, Miki Watanabe-Matsui, Kenji Iemura, Kozo Tanaka, Takuma Shiraki, Kazuhiko Igarashi

Biochem J (2018) 475 (5): 981–1002.

https://doi.org/10.1042/BCJ20170520

Published: 15 March 2018

... interactions with proteins involved in chromatin and gene expression but retained interactions with HMMR and its known partners including CHICA. By analyzing BACH1 modification using stable isotope labeling with amino acids in cell culture, mitosis-specific phosphorylations of BACH1 were observed...

View articletitled, Phosphorylation of BACH1 switches its function from transcription factor to mitotic chromosome regulator and promotes its interaction with HMMR

Articles

Back to the future: new target-validated Rab antibodies for evaluating LRRK2 signalling in cell biology and Parkinson's disease

Patrick A. Eyers

Biochem J (2018) 475 (1): 185–189.

https://doi.org/10.1042/BCJ20170870

Published: 05 January 2018

... (LRRK2) is a Ser/Thr kinase linked to familial and sporadic cases of Parkinson's disease (PD). Recent work established that multiple Rab GTPases are physiological substrates of LRRK2, with Rab10 in particular emerging as a human substrate whose site-specific phosphorylation mirrors hyperactive LRRK2...

View articletitled, Back to the future: new target-validated Rab antibodies for evaluating LRRK2 signalling in cell biology and Parkinson's disease

Articles

Dynamic multi-site phosphorylation by Fyn and Abl drives the interaction between CRKL and the novel scaffolding receptors DCBLD1 and DCBLD2

Anna M. Schmoker, Jaye L. Weinert, Kyle J. Kellett, Hannah E. Johnson, Ryan M. Joy, Marion E. Weir, Alicia M. Ebert, Bryan A. Ballif

Biochem J (2017) 474 (23): 3963–3984.

https://doi.org/10.1042/BCJ20170615

Published: 21 November 2017

... the conserved signaling features of DCBLD family members that drive their molecular activities. We previously identified DCBLD2 tyrosine phosphorylation sites in intracellular YxxP motifs that are required for the phosphorylation-dependent binding of the signaling adaptors CRK and CRKL (CT10 regulator of kinase...

View articletitled, Dynamic multi-site phosphorylation by Fyn and Abl drives the interaction between CRKL and the novel scaffolding receptors DCBLD1 and DCBLD2

Includes: Supplementary data

Articles

Reactive sulfur species inactivate Ca 2+ /calmodulin-dependent protein kinase IV via S-polysulfidation of its active-site cysteine residue

Tsuyoshi Takata, Hideshi Ihara, Naoya Hatano, Yukihiro Tsuchiya, Takaaki Akaike, Yasuo Watanabe

Biochem J (2017) 474 (15): 2547–2562.

https://doi.org/10.1042/BCJ20170092

Published: 18 July 2017

... inactivated by RSS via polysulfidation of the active-site Cys residue. CaMKIV is phosphorylated at Thr 196 by its upstream CaMK kinase (CaMKK), resulting in the induction of its full activity. In vitro incubation of CaMKIV with the exogenous RSS donors Na 2 S n ( n = 2–4) resulted in dose-dependent inhibition...

View articletitled, Reactive sulfur species inactivate Ca 2+ /calmodulin-dependent protein kinase IV via S-polysulfidation of its active-site cysteine residue

Includes: Supplementary data

Articles

HIV-1 Tat potently stabilises Mdm2 and enhances viral replication

Rameez Raja, Larance Ronsard, Sneh Lata, Shubhendu Trivedi, Akhil C. Banerjea

Biochem J (2017) 474 (14): 2449–2464.

https://doi.org/10.1042/BCJ20160825

Published: 11 July 2017

... and its implications for viral replication have not been well studied. Here, we show that the Mdm2 protein level increases during HIV-1 infection and this effect is mediated by HIV-1 Tat protein. Tat appears to stabilise Mdm2 at the post-translational level by inducing its phosphorylation at serine-166...

View articletitled, HIV-1 Tat potently stabilises Mdm2 and enhances viral replication

Includes: Supplementary data

Articles

Structure and inhibitor specificity of the PCTAIRE-family kinase CDK16

Sarah E. Dixon-Clarke, Saifeldin N. Shehata, Tobias Krojer, Timothy D. Sharpe, Frank von Delft, Kei Sakamoto, Alex N. Bullock

Biochem J (2017) 474 (5): 699–713.

https://doi.org/10.1042/BCJ20160941

Published: 20 February 2017

... trafficking and cancer cell proliferation. CDK16 is activated through binding to cyclin Y via a phosphorylation-dependent 14-3-3 interaction and has a unique consensus substrate phosphorylation motif compared with conventional CDKs. To elucidate the structure and inhibitor-binding properties of this atypical...

View articletitled, Structure and inhibitor specificity of the PCTAIRE-family kinase CDK16

Includes: Supplementary data

Articles

A role for prolyl isomerase PIN1 in the phosphorylation-dependent modulation of PRRXL1 function

Ricardo Soares-dos-Reis, Ana Sofia Pessoa, Ana Filipa Dias, Miguel Falcão, Mariana Raimundo Matos, Rui Vitorino, Filipe Almeida Monteiro, Deolinda Lima, Carlos Reguenga

Biochem J (2017) 474 (5): 683–697.

https://doi.org/10.1042/BCJ20160560

Published: 20 February 2017

... highly conserved phosphorylation sites (T110, S119, S231, S233 and S251) in PRRXL1 primary structure. Four are phospho-S/T-P sites, which suggest a role for the prolyl isomerase PIN1 in regulating PRRXL1. Accordingly, PRRXL1 physically interacts with PIN1 and displays diminished transcriptional activity...

View articletitled, A role for prolyl isomerase PIN1 in the phosphorylation-dependent modulation of PRRXL1 function

Articles

Identification of key phosphorylation sites in PTH1R that determine arrestin3 binding and fine-tune receptor signaling

Diana Zindel, Sandra Engel, Andrew R. Bottrill, Jean-Philippe Pin, Laurent Prézeau, Andrew B. Tobin, Moritz Bünemann, Cornelius Krasel, Adrian J. Butcher

Biochem J (2016) 473 (22): 4173–4192.

https://doi.org/10.1042/BCJ20160740

Published: 10 November 2016

... and kidney where it modulates extracellular Ca 2+ homeostasis and bone turnover. It is well established that phosphorylation of GPCRs constitutes a key event in regulating receptor function by promoting arrestin recruitment and coupling to G-protein-independent signaling pathways. Mapping phosphorylation...

View articletitled, Identification of key phosphorylation sites in PTH1R that determine arrestin3 binding and fine-tune receptor signaling

Articles

The interaction between AMPKβ2 and the PP1-targeting subunit R6 is dynamically regulated by intracellular glycogen content

Yvonne Oligschlaeger, Marie Miglianico, Vivian Dahlmans, Carla Rubio-Villena, Dipanjan Chanda, Maria Adelaida Garcia-Gimeno, Will A. Coumans, Yilin Liu, J. Willem Voncken, Joost J.F.P. Luiken, Jan F.C. Glatz, Pascual Sanz, Dietbert Neumann

Biochem J (2016) 473 (7): 937–947.

https://doi.org/10.1042/BJ20151035

Published: 29 March 2016

... the glucose-induced inactivation of AMPK. In the present study, we further investigated the interaction of R6 with AMPKβ and the possible dependency on Thr-148 phosphorylation status. Yeast two-hybrid (Y2H) analyses and co-immunoprecipitation (IP) of the overexpressed proteins in human embryonic kidney (HEK...

View articletitled, The interaction between AMPKβ2 and the PP1-targeting subunit R6 is dynamically regulated by intracellular glycogen content

Articles

Protein kinase Cζ exhibits constitutive phosphorylation and phosphatidylinositol-3,4,5-triphosphate-independent regulation

Irene S. Tobias, Manuel Kaulich, Peter K. Kim, Nitya Simon, Estela Jacinto, Steven F. Dowdy, Charles C. King, Alexandra C. Newton

Biochem J (2016) 473 (4): 509–523.

https://doi.org/10.1042/BJ20151013

Published: 09 February 2016

... that aPKC is constitutively phosphorylated and, using a genetically-encoded reporter for PKC activity, basally active in cells. Specifically, we show that phosphorylation at two key regulatory sites, the activation loop and turn motif, of the aPKC PKCζ in multiple cultured cell types is constitutive...

View articletitled, Protein kinase Cζ exhibits constitutive phosphorylation and phosphatidylinositol-3,4,5-triphosphate-independent regulation

Articles

A novel phosphorylation site at Ser 130 adjacent to the pseudosubstrate domain contributes to the activation of protein kinase C-δ

Jianli Gong, Ronald J. Holewinski, Jennifer E. Van Eyk, Susan F. Steinberg

Biochem J (2016) 473 (3): 311–320.

https://doi.org/10.1042/BJ20150812

Published: 25 January 2016

... phosphorylation [Gong et al. (2015) Mol. Cell. Biol. 35 , 1727–1740]. The present study uses MS-based methods to identify PKCδ phosphorylation at Thr 50 and Ser 645 (in resting and PMA-treated cardiomyocytes) as well as Thr 37 , Thr 38 , Ser 130 , Thr 164 , Thr 211 , Thr 215 , Ser 218 , Thr 295 , Ser 299 and Thr...

View articletitled, A novel phosphorylation site at Ser 130 adjacent to the pseudosubstrate domain contributes to the activation of protein kinase C-δ

Articles

Nuclear protein kinase CLK1 uses a non-traditional docking mechanism to select physiological substrates

Malik M. Keshwani, Kendra L. Hailey, Brandon E. Aubol, Laurent Fattet, Maria L. McGlone, Patricia A. Jennings, Joseph A. Adams

Biochem J (2015) 472 (3): 329–338.

https://doi.org/10.1042/BJ20150903

Published: 27 November 2015

...Malik M. Keshwani; Kendra L. Hailey; Brandon E. Aubol; Laurent Fattet; Maria L. McGlone; Patricia A. Jennings; Joseph A. Adams Phosphorylation-dependent cell communication requires enzymes that specifically recognize key proteins in a sea of similar, competing substrates. The protein kinases...

View articletitled, Nuclear protein kinase CLK1 uses a non-traditional docking mechanism to select physiological substrates

Articles

MyelStones: the executive roles of myelin basic protein in myelin assembly and destabilization in multiple sclerosis

Kenrick A. Vassall, Vladimir V. Bamm, George Harauz

Biochem J (2015) 472 (1): 17–32.

https://doi.org/10.1042/BJ20150710

Published: 30 October 2015

... fragments (MoRFs), which thereby undergo local disorder-to-order transitions. Their conformations and associations are modulated by environment and by a dynamic barcode of post-translational modifications, particularly phosphorylation by mitogen-activated and other protein kinases and deimination...

View articletitled, MyelStones: the executive roles of myelin basic protein in myelin assembly and destabilization in multiple sclerosis

Articles

The NHERF2 sequence adjacent and upstream of the ERM-binding domain affects NHERF2–ezrin binding and dexamethasone stimulated NHE3 activity

Jianbo Yang, Rafiquel Sarker, Varsha Singh, Prateeti Sarker, Jianyi Yin, Tian-E Chen, Raghothama Chaerkady, Xuhang Li, C. Ming Tse, Mark Donowitz

Biochem J (2015) 470 (1): 77–90.

https://doi.org/10.1042/BJ20150238

Published: 06 August 2015

... exclusively to the apical domain. Furthermore, phosphorylation of Ser 303 located in the EBRS of NHERF2, decreases the binding affinity for ezrin, dislocates apical NHERF2 into the cytosol and increases the NHERF2 microvillar mobility rate. Moreover, increased phosphorylation of Ser 303 was functionally...

View articletitled, The NHERF2 sequence adjacent and upstream of the ERM-binding domain affects NHERF2–ezrin binding and dexamethasone stimulated NHE3 activity

Articles

Akt-mediated regulation of antidepressant-sensitive serotonin transporter function, cell-surface expression and phosphorylation

Jeyaganesh Rajamanickam, Balasubramaniam Annamalai, Troels Rahbek-Clemmensen, Santhanalakshmi Sundaramurthy, Ulrik Gether, Lankupalle D. Jayanthi, Sammanda Ramamoorthy

Biochem J (2015) 468 (1): 177–190.

https://doi.org/10.1042/BJ20140826

Published: 05 May 2015

... and phosphorylation. However, whether Akt/PKB (protein kinase) regulates SERT function is not known. In the present study, we made the novel observation that inhibition of Akt resulted in the down-regulation of SERT function through the regulation of SERT trafficking and phosphorylation. Akt inhibitor Akt X {10-(4...

View articletitled, Akt-mediated regulation of antidepressant-sensitive serotonin transporter function, cell-surface expression and phosphorylation

Articles

Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function

Malik M. Keshwani, Brandon E. Aubol, Laurent Fattet, Chen-Ting Ma, Jinsong Qiu, Patricia A. Jennings, Xiang-Dong Fu, Joseph A. Adams

Biochem J (2015) 466 (2): 311–322.

https://doi.org/10.1042/BJ20141373

Published: 20 February 2015

... in arginine–serine dipeptide repeats (RS domains). Although the SRPKs (SR-specific protein kinases) phosphorylate these repeats, RS domains also contain prolines with flanking serines that are phosphorylated by a second family of protein kinases known as the CLKs (Cdc2-like kinases). The role of specific...

View articletitled, Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function

Includes: Supplementary data

Articles

A protein kinase screen of Neurospora crassa mutant strains reveals that the SNF1 protein kinase promotes glycogen synthase phosphorylation

Thiago De Souza Candido, Rodrigo Duarte Gonçalves, Ana Paula Felício, Fernanda Zanolli Freitas, Fernanda Barbosa Cupertino, Ana Carolina Gomes Vieira De Carvalho, Maria Célia Bertolini

Biochem J (2014) 464 (3): 323–334.

https://doi.org/10.1042/BJ20140942

Published: 05 December 2014

.... The activities of glycogen synthase and glycogen phosphorylase, the rate-limiting enzymes of the synthesis and degradation processes, respectively, are regulated by allosteric modulation and reversible phosphorylation. To identify the protein kinases affecting glycogen metabolism in Neurospora crassa , we...

View articletitled, A protein kinase screen of Neurospora crassa mutant strains reveals that the SNF1 protein kinase promotes glycogen synthase phosphorylation

Includes: Supplementary data

Articles

PI4KIIα phosphorylation by GSK3 directs vesicular trafficking to lysosomes

James W. Robinson, Iryna Leshchyns’ka, Hovik Farghaian, William E. Hughes, Vladimir Sytnyk, Graham G. Neely, Adam R. Cole

Biochem J (2014) 464 (1): 145–156.

https://doi.org/10.1042/BJ20140497

Published: 23 October 2014

... phosphorylates two distinct sites in the N-terminus of PI4KIIα (Ser 5 and Ser 47 ), promoting binding to the adaptor protein 3 (AP-3) complex for trafficking to the lysosome to be degraded. Blocking phosphorylation reduces trafficking to the lysosome, stabilizing PI4KIIα and its cargo proteins for redistribution...

View articletitled, PI4KIIα phosphorylation by GSK3 directs vesicular trafficking to lysosomes

Articles

Priming IKKβ kinase for action

Steven C. Ley, Rudi Beyaert

Biochem J (2014) 463 (1): e1–e2.

https://doi.org/10.1042/BJ20140989

Published: 08 September 2014

..., activation of IKKβ requires phosphorylation of the activation loop of its kinase domain. Different upstream protein kinases, and IKKβ itself, have been reported to directly phosphorylate and activate IKKβ in vitro , but the exact molecular mechanism of IKKβ activation in cells has remained unclear...

View articletitled, Priming IKKβ kinase for action

Articles

Osteopontin O -glycosylation contributes to its phosphorylation and cell-adhesion properties

Yoshinobu Kariya, Mayumi Kanno, Kana Matsumoto-Morita, Midori Konno, Yoshiki Yamaguchi, Yasuhiro Hashimoto

Biochem J (2014) 463 (1): 93–102.

https://doi.org/10.1042/BJ20140060

Published: 08 September 2014

... and adhesion primarily through its association with several integrins such as αvβ3, and its phosphorylation affects these processes. However, the mechanism by which OPN O -glycosylation affects these processes is not completely understood. In the present study, we demonstrated that OPN O -glycosylation self...

View articletitled, Osteopontin O -glycosylation contributes to its phosphorylation and cell-adhesion properties

Includes: Supplementary data

Articles

Regulation of PKA activity by an autophosphorylation mechanism in Saccharomyces cerevisiae

Clara Andrea Solari, Vanesa Tudisca, Marcelo Pugliessi, Alejandro Daniel Nadra, Silvia Moreno, Paula Portela

Biochem J (2014) 462 (3): 567–579.

https://doi.org/10.1042/BJ20140577

Published: 22 August 2014

...Clara Andrea Solari; Vanesa Tudisca; Marcelo Pugliessi; Alejandro Daniel Nadra; Silvia Moreno; Paula Portela PKA (cAMP-dependent protein kinase) activity, as well as that of other AGC members, is regulated by multiple phosphorylations of its catalytic subunits. In Saccharomyces cerevisiae , the PKA...

View articletitled, Regulation of PKA activity by an autophosphorylation mechanism in Saccharomyces cerevisiae

Includes: Supplementary data

Articles

N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation

Brandon E. Aubol, Ryan M. Plocinik, Malik M. Keshwani, Maria L. McGlone, Jonathan C. Hagopian, Gourisankar Ghosh, Xiang-Dong Fu, Joseph A. Adams

Biochem J (2014) 462 (1): 143–152.

https://doi.org/10.1042/BJ20140494

Published: 24 July 2014

...Brandon E. Aubol; Ryan M. Plocinik; Malik M. Keshwani; Maria L. McGlone; Jonathan C. Hagopian; Gourisankar Ghosh; Xiang-Dong Fu; Joseph A. Adams SR proteins are essential splicing factors that are regulated through multisite phosphorylation of their RS (arginine/serine-rich) domains by two major...

View articletitled, N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation

Includes: Supplementary data

Articles

T-cell co-stimulation through the CD2 and CD28 co-receptors induces distinct signalling responses

Sigrid S. Skånland, Kristine Moltu, Torunn Berge, Einar M. Aandahl, Kjetil Taskén

Biochem J (2014) 460 (3): 399–410.

https://doi.org/10.1042/BJ20140040

Published: 29 May 2014

... that CD2 co-stimulation induces phosphorylation of the TCR-proximal signalling complex, whereas CD28 activates distal signalling molecules, including the transcription factors NF-κB (nuclear factor κB), ATF (activating transcription factor)-2, STAT3/5 (signal transducer and activator of transcription 3/5...

View articletitled, T-cell co-stimulation through the CD2 and CD28 co-receptors induces distinct signalling responses

Includes: Supplementary data

Articles

Kinase and channel activity of TRPM6 are co-ordinated by a dimerization motif and pocket interaction

Jenny van der Wijst, Maxime G. Blanchard, Helen I. Woodroof, Thomas J. Macartney, Robert Gourlay, Joost G. Hoenderop, René J. Bindels, Dario R. Alessi

Biochem J (2014) 460 (2): 165–175.

https://doi.org/10.1042/BJ20131639

Published: 13 May 2014

... phosphorylation protein kinase transient receptor potential melastatin (TRPM) TRPM6 (transient receptor potential melastatin 6) is an exceptional enzyme possessing a Mg 2+ -permeant ion channel domain and a C-terminal protein kinase moiety [ 1 – 4 ]. Autosomal recessive mutations in the TRPM6 gene...

View articletitled, Kinase and channel activity of TRPM6 are co-ordinated by a dimerization motif and pocket interaction

Includes: Supplementary data

Articles

Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser 65

Agne Kazlauskaite, Chandana Kondapalli, Robert Gourlay, David G. Campbell, Maria Stella Ritorto, Kay Hofmann, Dario R. Alessi, Axel Knebel, Matthias Trost, Miratul M. K. Muqit

Biochem J (2014) 460 (1): 127–141.

https://doi.org/10.1042/BJ20140334

Published: 25 April 2014

...) is activated by mitochondrial depolarization and stimulates the Parkin E3 ligase by phosphorylating Ser 65 within its Ubl (ubiquitin-like) domain. Using phosphoproteomic analysis, we identified a novel ubiquitin phosphopeptide phosphorylated at Ser 65 that was enriched 14-fold in HEK (human embryonic kidney...

View articletitled, Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser 65

Includes: Supplementary data

Articles

Ser 119 phosphorylation modulates the activity and conformation of PRRXL1, a homeodomain transcription factor

Ricardo Soares-dos-Reis, Ana S. Pessoa, Mariana R. Matos, Miguel Falcão, Vera M. Mendes, Bruno Manadas, Filipe A. Monteiro, Deolinda Lima, Carlos Reguenga

Biochem J (2014) 459 (3): 441–453.

https://doi.org/10.1042/BJ20131014

Published: 11 April 2014

... expressed in DRG and dSC (dorsal spinal cord) nociceptive neurons. PRRXL1 is crucial for the establishment and maintenance of nociceptive circuitry, as Prrxl1 −/− mice present neuronal loss, reduced pain sensitivity and failure to thrive. In the present study, we show that PRRXL1 is highly phosphorylated...

View articletitled, Ser 119 phosphorylation modulates the activity and conformation of PRRXL1, a homeodomain transcription factor

Includes: Supplementary data

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