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Keywords: endoplasmic reticulum
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Biochem J (2023) 480 (18): 1459–1473.
Published: 21 September 2023
... M. Buck Transmembrane proteins have unique requirements to fold and integrate into the endoplasmic reticulum (ER) membrane. Most notably, transmembrane proteins must fold in three separate environments: extracellular domains fold in the oxidizing environment of the ER lumen, transmembrane domains...
Includes: Supplementary data
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Biochem J (2022) 479 (7): 839–855.
Published: 11 April 2022
.... The AAT Z variant forms polymer within the endoplasmic reticulum (ER) of hepatocytes and results in reduction in AAT secretion and severe disease. Previous studies demonstrated a secretion defect of AAT in LMAN1 deficient cells, and mild decreases in AAT levels in male LMAN1 and MCFD2 deficient mice...
Includes: Supplementary data
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Biochem J (2019) 476 (13): 1929–1942.
Published: 09 July 2019
... are believed to be derived by a budding and scission process from the surface of the endoplasmic reticulum, and this occurs concomitantly with the accumulation of neutral lipids, most often triacylglycerols and steryl esters. Overall, the mechanisms underlying LD biogenesis are difficult to generalize, in part...
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Biochem J (2018) 475 (5): 873–886.
Published: 06 March 2018
... mutants, but impair the secretion of others. However, ectopic glycans that enhanced secretion could not functionally replace a native N -glycan in the same domain. Secretion-deficient mutants, but not mutants with elevated secretion levels, show increased association with the endoplasmic reticulum...
Includes: Supplementary data
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Biochem J (2017) 474 (18): 3179–3188.
Published: 08 September 2017
... ]. In addition, some transcripts found in mammalian pro-B-cells encode HCs that can be expressed on the cell surface in the absence of any surrogate or conventional LC [ 12 ]. These HCs contain a C H 1 domain, which folds in the absence of a LC, enabling them to escape the endoplasmic reticulum (ER) quality...
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Biochem J (2016) 473 (7): 851–858.
Published: 29 March 2016
..., with the large loop between transmembrane one and two facing the lumen of the endoplasmic reticulum (ER). We used a redox sensitive green fluorescent protein (GFP) fused to the N- or C-terminus to show that these regions face the cytosol, and introduction of glycosylation sites along with mixed disulfide...
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Biochem J (2016) 473 (3): 233–244.
Published: 25 January 2016
... that impair biogenesis of the transporter cause type I cystinuria. It has been shown that upon assembly, b 0,+ AT prevents degradation and promotes folding of rBAT; then, rBAT traffics b 0,+ AT from the endoplasmic reticulum (ER) to the plasma membrane. The role of the N-glycans of rBAT and of its C-terminal...
Includes: Supplementary data
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Biochem J (2015) 469 (2): 279–288.
Published: 06 July 2015
... formation electron transfer endoplasmic reticulum protein disulfide isomerase redox potential thiol-disulfide exchange A family of proteins, collectively termed the protein disulfide isomerases (PDIs), is responsible for formation of correct disulfides in proteins entering the secretory pathway...
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Biochem J (2015) 466 (3): 455–465.
Published: 06 March 2015
...+ probes to specifically measure Ca 2+ in the cis/cis- to -medial -Go (cGo) or the trans -Go (tGo). Ca 2+ homoeostasis in these compartments and in the endoplasmic reticulum (ER) has been studied and compared. Moreover, the relative size of each subcompartment was estimated from aequorin consumption. We...
Includes: Multimedia, Supplementary data
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Biochem J (2014) 464 (2): 241–249.
Published: 14 November 2014
...Ji Won Park; James R. Reed; Lauren M. Brignac-Huber; Wayne L. Backes Cytochrome P450 (P450) function is dependent on the ability of these enzymes to successfully interact with their redox partners, NADPH-cytochrome P450 reductase (CPR) and cytochrome b 5 , in the endoplasmic reticulum (ER). Because...
Includes: Supplementary data
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Biochem J (2014) 463 (3): 373–381.
Published: 10 October 2014
... by STIM1 is poorly understood. STIM1 is a single transmembrane protein that communicates the filling state of the endoplasmic reticulum to store-operated channels. STIM1 has been reported to regulate the activity of all of the TRPC family members, except TRPC7. TRPC6 has been predominantly associated...
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Biochem J (2014) 461 (1): 107–113.
Published: 13 June 2014
...Colin Shepherd; Ojore B. V. Oka; Neil J. Bulleid Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as PDI (protein disulfide-isomerase) and a mechanism to form disulfides de novo . In mammalian cells, the major pathway for de novo...
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Biochem J (2014) 457 (1): 99–105.
Published: 10 December 2013
...Thea Bismo Strøm; Kristian Tveten; Trond P. Leren PCSK9 (proprotein convertase subtilisin/kexin type 9) binds to the LDLR (low-density lipoprotein receptor) at the cell surface and disrupts recycling of the LDLR. However, PCSK9 also interacts with the LDLR in the ER (endoplasmic reticulum...
Includes: Supplementary data
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Biochem J (2013) 456 (2): 297–309.
Published: 08 November 2013
...Helen R. Watson; Lydia Wunderley; Tereza Andreou; Jim Warwicker; Stephen High The majority of the polytopic proteins that are synthesized at the ER (endoplasmic reticulum) are integrated co-translationally via the Sec61 translocon, which provides lateral access for their hydrophobic TMs...
Includes: Supplementary data
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Biochem J (2013) 451 (3): 345–352.
Published: 12 April 2013
... correspondence should be addressed (email freddie.theodoulou@rothamsted.ac.uk ). 14 1 2013 18 2 2013 19 2 2013 © The Authors Journal compilation © 2013 Biochemical Society 2013 biogenesis endoplasmic reticulum peroxin peroxisome peroxisome membrane protein quality control...
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Biochem J (2013) 450 (2): 321–332.
Published: 15 February 2013
...Nader T. Amin; A. Katrine Wallis; Stephen A. Wells; Michelle L. Rowe; Richard A. Williamson; Mark J. Howard; Robert B. Freedman ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted to consist...
Includes: Supplementary data
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Biochem J (2012) 441 (2): 707–717.
Published: 21 December 2011
... network). In the present study, brefeldin A treatment of tendon explant cultures showed that N-proteinase activity is present in the resulting fused ER (endoplasmic reticulum)–Golgi compartment, but that C-proteinase activity is restricted to the TGN in embryonic chick tendon fibroblasts. In late...
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Biochem J (2012) 441 (1): 105–112.
Published: 14 December 2011
...Gaëlle Tahay; Elsa Wiame; Donatienne Tyteca; Pierre J. Courtoy; Emile Van Schaftingen Aspartate N-acetyltransferase (NAT8L, N-acetyltransferase 8-like), the enzyme that synthesizes N -acetylaspartate, is membrane-bound and is at least partially associated with the ER (endoplasmic reticulum...
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Biochem J (2011) 435 (2): 509–518.
Published: 29 March 2011
... demonstrated delayed glycan maturation kinetics upon substitution of the lysine residues. Moreover, VSVG-wt EPO-R, but not VSVG-5KR EPO-R, displayed endoplasmic reticulum-associated ubiquitination. Despite similar cell-surface EPO-binding levels of both receptors and the lack of EPO-induced ubiquitination...
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Biochem J (2011) 434 (2): 181–188.
Published: 11 February 2011
...Min Ni; Yi Zhang; Amy S. Lee GRP78 (glucose-regulated protein of 78 kDa) is traditionally regarded as a major ER (endoplasmic reticulum) chaperone facilitating protein folding and assembly, protein quality control, Ca 2+ binding and regulating ER stress signalling. It is a potent anti-apoptotic...
Includes: Multimedia, Supplementary data
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Biochem J (2010) 427 (3): 513–521.
Published: 14 April 2010
...Richard S. Marshall; Lorenzo Frigerio; Lynne M. Roberts The ER (endoplasmic reticulum) has long been considered the plant cell compartment within which protein disulfide bond formation occurs. Members of the ER-located PDI (protein disulfide isomerase) family are responsible for oxidizing, reducing...
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Biochem J (2010) 426 (2): 135–145.
Published: 09 February 2010
...Josh Duffy; Bhargavi Patham; Kojo Mensa-Wilmot N-terminal signal peptides direct secretory proteins into the ER (endoplasmic reticulum) of eukaryotes or the periplasmic space of prokaryotes. A hydrophobic core (h-region) is important for signal sequence function; however, the mechanism of h-region...
Includes: Supplementary data
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Biochem J (2010) 425 (1): 195–208.
Published: 14 December 2009
...Doris Roth; Emily Lynes; Jan Riemer; Henning G. Hansen; Nils Althaus; Thomas Simmen; Lars Ellgaard The thiol-disulfide oxidoreductases of the PDI (protein disulfide isomerase) family assist in disulfide-bond formation in the ER (endoplasmic reticulum). In the present study, we have shown...
Includes: Supplementary data
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Biochem J (2009) 423 (2): 145–155.
Published: 25 September 2009
...Imogen A. Sparkes; Lorenzo Frigerio; Nicholas Tolley; Chris Hawes The ER (endoplasmic reticulum) in higher plants forms a pleomorphic web of membrane tubules and small cisternae that pervade the cytoplasm, but in particular form a polygonal network at the cortex of the cell which may be anchored...
Includes: Multimedia, Supplementary data
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Biochem J (2008) 410 (2): 409–416.
Published: 12 February 2008
.... In the present study, we addressed the role of the EPO-R intracellular domain in exit from the ER (endoplasmic reticulum) and surface expression. A fusion protein between the thermo-reversible folding mutant of VSVG (vesicular-stomatitis-virus glycoprotein) (VSVGtsO45) and the EPO-R cytosolic domain [VSVG-WT...
Includes: Multimedia, Supplementary data
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Biochem J (2008) 410 (1): 93–100.
Published: 29 January 2008
... be classified into Q-SNARE and R-SNARE based on the structural property of their motifs. Assembly of four SNARE motifs (Qa, b, c and R) is supposed to trigger membrane fusion. We have previously shown that ER (endoplasmic reticulum)-localized syntaxin 18 (Qa) forms a complex with BNIP1 (Qb), p31/Use1 (Qc...
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Biochem J (2007) 404 (3): 467–476.
Published: 29 May 2007
...Kevin Larade; Zhi-gang Jiang; Andre Dejam; Hao Zhu; H. Franklin Bunn The novel reductase NCB5OR (NADPH cytochrome b 5 oxidoreductase) resides in the ER (endoplasmic reticulum) and may protect cells against ER stress. Levels of BiP (immunoglobulin heavy-chain-binding protein), CHOP (CCAAT/enhancer...
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