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Keywords: ubiquitin
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Articles
Biochem Soc Trans (2024) 52 (5): 2023–2034.
Published: 26 September 2024
... for preserving organelle integrity and maintaining cellular health. In this mini-review, we will focus on how selective membrane protein quality control at the Golgi apparatus, particularly through the defective for SREBP cleavage (Dsc) ubiquitin ligase complex, detects orphaned proteins and prevents their mis...
Articles
Biochem Soc Trans (2024) 52 (3): 1085–1098.
Published: 08 May 2024
... process that maintains a delicate balance of protein homeostasis. The ubiquitin-proteasome system (UPS) is a key regulator of proteostasis. A dysfunctional UPS is a hallmark of muscle ageing and is often impacted in neuromuscular disorders (NMDs). Malfunction of the UPS often results in aberrant protein...
Articles
Biochem Soc Trans (2024) 52 (1): 241–267.
Published: 28 February 2024
...Derek L. Bolhuis; Michael J. Emanuele; Nicholas G. Brown Protein ubiquitination is a post-translational modification that entails the covalent attachment of the small protein ubiquitin (Ub), which acts as a signal to direct protein stability, localization, or interactions. The Ub code is written...
Articles
Biochem Soc Trans (2024) 52 (1): 291–299.
Published: 04 January 2024
... the ubiquitin molecules from ubiquitylated proteins, DUBs control ubiquitin-dependent selective protein degradation pathways such as the proteasomal-, autophagic-, and endocytic degradation pathways. In the endocytic degradation pathway, DUBs can modulate the endocytic trafficking and thus the stability...
Articles
Biochem Soc Trans (2023) 51 (3): 959–969.
Published: 15 June 2023
... on behalf of the Biochemical Society 2023 elongation control integrated stress response ribosomes stress response translation ubiquitin Eukaryotic cells are constantly exposed to a range of challenging conditions, such as starvation or heat, osmotic, oxidative, UV radiation...
Articles
Biochem Soc Trans (2023) 51 (1): 353–362.
Published: 16 January 2023
...Adam J. Middleton; Catherine L. Day Modification of proteins by ubiquitin is a highly regulated process that plays a critical role in eukaryotes, from the construction of signalling platforms to the control of cell division. Aberrations in ubiquitin transfer are associated with many diseases...
Articles
Biochem Soc Trans (2022) 50 (5): 1457–1469.
Published: 05 October 2022
... of substrates and novel pathways and substrates that utilize its activity. Valosin-containing protein (VCP, also p97, or Cdc48p in yeast) is an evolutionarily conserved, homo-hexameric, ubiquitin-selective, AAA-ATPase that functions in numerous ubiquitin-dependent protein quality control pathways. VCP...
Articles
Biochem Soc Trans (2022) 50 (2): 783–797.
Published: 21 March 2022
... putative kinase 1 ubiquitin Parkinson's disease (PD) is a neurodegenerative disorder that leads to chronic and progressive deficits in body movement that impact the life and lifestyle of affected individuals. Clinical features of PD include tremors, slowness of movement (bradykinesia), involuntary...
Articles
Biochem Soc Trans (2021) 49 (1): 365–377.
Published: 26 February 2021
... and defective proteins from the cell. The ubiquitin-proteasome system is a key pathway for the molecular control of misfolded cytosolic proteins, co-opting a cascade of ubiquitin ligases to direct terminally damaged proteins to the proteasome via modification with chains of the small protein, ubiquitin. Despite...
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Articles
Biochem Soc Trans (2020) 48 (5): 2159–2171.
Published: 23 September 2020
... proteins and complexes through ubiquitin-like modifiers. Nse2 codes for a C-terminal SP-RING domain with SUMO ligase activity, assisting Smc5/6 functions in chromosome segregation through sumoylation of several chromosome-associated proteins. Nse1 codes for a C-terminal NH-RING domain and, although it has...
Articles
Biochem Soc Trans (2020) 48 (2): 463–478.
Published: 20 April 2020
... of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) . development SUMO ubiquitin SUMO belongs to the Ubiquitin-like modifier (UbL) family of proteins and attaches covalently to target proteins in a transient and reversible process termed...
Articles
Biochem Soc Trans (2020) 48 (2): 479–497.
Published: 20 March 2020
.... The ubiquitin system is absolutely central to this process and perturbation of its function contributes directly to the onset and progression of a wide variety of diseases, including cancer, metabolic syndromes, neurodegenerative diseases, autoimmunity, inflammatory disorders, infectious diseases, and muscle...
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Articles
Biochem Soc Trans (2018) 46 (6): 1551–1558.
Published: 31 October 2018
... cerevisiae has been used to discover and define many mechanisms that regulate conserved features of endosomal trafficking. Internalised surface membrane proteins first localise to endosomes before sorting to other compartments. Ubiquitination of endosomal membrane proteins is a signal for their degradation...
Articles
Biochem Soc Trans (2018) 46 (2): 423–436.
Published: 27 March 2018
...Huib Ovaa; Alfred C.O. Vertegaal Ubiquitin (Ub) and ubiquitin-like (Ubl) proteins including small Ubl modifier (SUMO) are small proteins which are covalently linked to target proteins to regulate their functions. In this review, we discuss the current state of the art and point out what we feel...
Articles
Biochem Soc Trans (2018) 46 (2): 453–466.
Published: 22 February 2018
...Miriam Walden; Safi Kani Masandi; Krzysztof Pawłowski; Elton Zeqiraj The ubiquitin (Ub) proteasome system and Ub signalling networks are crucial to cell biology and disease development. Deubiquitylases (DUBs) control cell signalling by removing mono-Ub and polyubiquitin chains from substrates. DUBs...
Includes: Supplementary data
Articles
Biochem Soc Trans (2016) 44 (5): 1265–1271.
Published: 19 October 2016
... demonstrated by numerous disorders (known as ciliopathies) associated with disrupted cilia formation (ciliogenesis). Recent advances describing functional regulators of the primary cilium highlight an emerging role for the ubiquitin–proteasome system (UPS) as a key regulator of ciliogenesis. Although...
Articles
Biochem Soc Trans (2016) 44 (1): 212–227.
Published: 09 February 2016
...Viduth K. Chaugule; Helen Walden Post-translational modification (PTM) of proteins by ubiquitination is an essential cellular regulatory process. Such regulation drives the cell cycle and cell division, signalling and secretory pathways, DNA replication and repair processes and protein quality...
Articles
Biochem Soc Trans (2016) 44 (1): 273–278.
Published: 09 February 2016
... in our understanding of its localization and regulation by ubiquitination and SUMOylation. 1 To whom correspondence should be addressed (email [email protected] ). 26 11 2015 © 2016 Authors; published by Portland Press Limited 2016 Research in the NRL laboratory is supported...
Articles
Biochem Soc Trans (2015) 43 (5): 1049–1050.
Published: 09 October 2015
...Endre Kiss-Toth; Guillermo Velasco; Warren S. Pear 1 To whom correspondence should be addressed (email [email protected] ) . 2 6 2015 © 2015 Authors; published by Portland Press Limited 2015 cancer lipids metabolism signalling tribbles ubiquitin...
Articles
Biochem Soc Trans (2015) 43 (3): 471–475.
Published: 01 June 2015
... at the plasma membrane have emerged as important regulators of IC and their de-regulation has been associated with various diseases. Although Cx-mediated IC can be modulated by different mechanisms, ubiquitination has been described as one of the major post-translational modifications involved in Cx regulation...
Articles
Biochem Soc Trans (2013) 41 (2): 463–473.
Published: 21 March 2013
...Ronald T. Hay SUMO (small ubiquitin-like modifier) emerged from the shadow of the well-established ubiquitin some 15 years ago when it was shown that a distinct conjugation pathway was responsible for SUMO modification. Since then it has been established that SUMO modifies over a thousand...
Articles
Biochem Soc Trans (2010) 38 (6): 1621–1626.
Published: 24 November 2010
... linked mRNA metabolism with ubiquitination. Ubiquitin is well recognized for its role in protein regulation/degradation. In the present paper, we describe a new group of RNA-binding E3 ubiquitin ligases which are predicted to bind and regulate RNA stability. Although much effort has been focused...
Articles
Biochem Soc Trans (2010) 38 (2): 598–603.
Published: 22 March 2010
... of paternal effects. However, as more is known about molecular expression of chromatin-modifying proteins, ubiquitin pathway proteins and transcription factors in sperm cells, as well as their ability to achieve effect by intaglio expression, passing transcripts directly into translation, the role of the male...
Articles
Biochem Soc Trans (2010) 38 (1): 116–131.
Published: 19 January 2010
... a particular pathway is followed. Prominent among these modifications are the addition of phosphate or ubiquitin (and ubiquitin-like) moieties that confer new binding surfaces and conformational states on the modified proteins. The present review summarizes some of consequences of ubiquitin and ubiquitin-like...
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Articles
Biochem Soc Trans (2009) 37 (1): 161–166.
Published: 20 January 2009
...). For the Vps27–Hse1 complex, a coarse-grained Monte Carlo simulation of the 1:1 heterodimer bound to a membrane and ubiquitinated cargo suggests that the complex is open and dynamic, facilitating its interactions with cargo of a wide range of sizes and conformations [ 2 ]. This study has the limitation...
Articles
Biochem Soc Trans (2009) 37 (1): 137–142.
Published: 20 January 2009
...Lina M. Rodahl; Susanne Stuffers; Viola H. Lobert; Harald Stenmark The ESCRT (endosomal sorting complex required for transport) machinery consists of four protein complexes that mediate sorting of ubiquitinated membrane proteins into the intraluminal vesicles of multivesicular endosomes, thereby...
Articles
Biochem Soc Trans (2008) 36 (5): 781–785.
Published: 19 September 2008
... conditions the action of many critical cellular factors. The third intracellular proteolysis meeting held by the University La Laguna, Canary Islands, Spain, included speakers working with some of the most important proteolytic systems present in higher eukaryotes, such as the UPS (ubiquitin–proteasome...
Articles
Biochem Soc Trans (2008) 36 (5): 843–847.
Published: 19 September 2008
.... A major proteolytic pathway involves the ubiquitination of target proteins and subsequent targeting to the 26S proteasome for degradation. Many F-box proteins play a determining role in the substrate specificity of this degradation pathway. In most cases, selective recognition of the target proteins...
Articles
Biochem Soc Trans (2008) 36 (5): 802–806.
Published: 19 September 2008
...Dimitris P. Xirodimas Genetic experiments have established an important role for the ubiquitin-like molecule NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8) in the regulation of cell growth, viability and development. It is therefore essential to identify the molecular...
Articles
Biochem Soc Trans (2008) 36 (5): 858–863.
Published: 19 September 2008
... by the proteasome after polyubiquitination, we showed that the bulk of c-Fos and Fra-1 can be broken down independently of any prior ubiquitination. Certain conserved structural domains suggest that similar mechanisms may also apply to Fra-2 and FosB. Computer search indicates that certain motifs shared by the Fos...
Articles
Biochem Soc Trans (2008) 36 (5): 833–838.
Published: 19 September 2008
...Gemma Marfany; Amanda Denuc Ub (ubiquitin) and Ubls (Ub-like molecules) are peptide modifiers that change the fate and function of their substrates. A plethora of enzyme activities and protein cofactors are required for either the conjugation (mainly E3 ligases) or deconjugation of Ub and Ubls...
Articles
Biochem Soc Trans (2008) 36 (5): 807–812.
Published: 19 September 2008
... results in a latent 20S core particle that can serve further as a platform for 19S regulatory particle attachment and formation of the biologically active 26S proteasome for ubiquitin-dependent proteolysis. Both general and dedicated proteasome assembly chaperones regulate the efficiency and outcome...
Articles
Biochem Soc Trans (2008) 36 (3): 469–471.
Published: 21 May 2008
...Robert Layfield; Mark S. Searle A role for ubiquitin in the pathogenesis of human diseases was first suggested some two decades ago, from studies that localized the protein to intracellular protein aggregates, which are a feature of the major human neurodegenerative disorders. Although several...
Articles
Biochem Soc Trans (2008) 36 (3): 459–463.
Published: 21 May 2008
...Mair Thomas; Mark Wills; Paul J. Lehner Viruses exploit the ubiquitin system by targeting cell-surface receptors recognized by immune cells for internalization, thereby evading recognition. We have characterized the KSHV (Kaposi's sarcoma-associated herpesvirus)-encoded E3 ubiquitin ligases, K3...
Articles
Biochem Soc Trans (2007) 35 (5): 1334–1337.
Published: 25 October 2007
...H.D. Ulrich Damage tolerance mechanisms, which allow the bypass of DNA lesions during replication, are controlled in eukaryotic cells by mono- and poly-ubiquitination of the DNA polymerase cofactor PCNA (proliferating-cell nuclear antigen). In the present review, I will summarize our current...
Articles
Biochem Soc Trans (2006) 34 (5): 746–748.
Published: 25 October 2006
... S regulator of the 26 S proteasome. Gankyrin is also the first liver oncogene. Gankyrin is found in other complexes that contain Rb (retinoblastoma protein) and the ubiquitin protein ligase Mdm2 (murine double minute 2). Gankyrin increases the hyperphosphorylation of Rb and therefore activates E2F...
Articles
Biochem Soc Trans (2006) 34 (5): 735–737.
Published: 25 October 2006
... the disease mechanism in this skeletal disorder, but also the critical determinants of ubiquitin recognition by an ubiquitin-binding protein. The 11 separate PDB mutations identified to date all affect the C-terminal region of p62 containing the UBA domain (ubiquitin-associated domain), a ubiquitin-binding...
Articles
Biochem Soc Trans (2006) 34 (5): 738–742.
Published: 25 October 2006
... by the lysosomes. We focused on the UPS (ubiquitin–proteasome system). As a result of molecular misreading, misframed UBB (ubiquitin B) (UBB +1 ) is generated. UBB +1 accumulates in the neuritic plaques and neurofibrillary tangles in all patients with AD (Alzheimer's disease) and in the neuronal and glial...
Articles
Biochem Soc Trans (2006) 34 (5): 757–760.
Published: 25 October 2006
... (tumour-necrosis-factor-receptor-associated factor 6) complex bridging the two receptors. The atypical protein kinase C is activated and recruited to the receptor complex as well. TrkA is Lys 63 -polyubiquitinated on Lys 485 by the E3 (ubiquitin ligase), TRAF-6, and E2 (ubiquitin-conjugating enzyme...
Articles
Biochem Soc Trans (2004) 32 (5): 724–727.
Published: 26 October 2004
...L.A. Passmore The APC (anaphase-promoting complex) is a multisubunit E3 ubiquitin ligase that targets cell-cycle-related proteins for degradation by the 26 S proteasome. The APC contains at least 13 subunits and is regulated by the binding of co-activator proteins and by phosphorylation...
Articles
Biochem Soc Trans (2004) 32 (5): 728–730.
Published: 26 October 2004
...R. Layfield; B. Ciani; S.H. Ralston; L.J. Hocking; P.W. Sheppard; M.S. Searle; J.R. Cavey Mutations affecting the UBA (ubiquitin-associated) domain of SQSTM1 (Sequestosome 1) (p62) are a common cause of Paget's disease of bone. The missense mutations resolve into those which retain [P392L (Pro 392...
Articles
Biochem Soc Trans (2003) 31 (2): 474–481.
Published: 01 April 2003
... that this organelle is involved mostly in the degradation of extracellular proteins, and their proteases cannot be substrate-specific. The discovery of the complex cascade of the ubiquitin pathway revolutionized the field. It is clear now that degradation of cellular proteins via the ubiquitin system is a highly...