Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum

Rutkevich, Lori A.; Williams, David B.

doi:10.1016/j.ceb.2010.10.011

Cited by 102 publications

(98 citation statements)

References 73 publications

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“…Calnexin is another key ER chaperone that binds to nascent glycoproteins (Rutkevich and Williams, 2011). This binding slows down client protein folding and prevents their aggregation owing to retention of folding intermediates in the ER.…”

Section: Introductionmentioning

confidence: 99%

“…All along, calnexin works in partnership with ERp57, an oxidoreductase that is a member of the protein disulfide isomerase (PDI) family (Coe and Michalak, 2010;Oliver et al, 1997;Zapun et al, 1998). Studies have shown that a certain subset of disulfide-bonded heavily glycosylated proteins such as the lowdensity lipoprotein receptor (LDLR) depend specifically on this partnership for efficient folding and subsequent trafficking through the secretory system (Jessop et al, 2007;Rutkevich and Williams, 2011). Surprisingly, our laboratory and others have determined that calnexin is not only found on the rough ER, but is often enriched on the MAM (Hayashi and Su, 2007;Myhill et al, 2008;Wieckowski et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

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Palmitoylation is the Switch that Assigns Calnexin to Quality Control or ER Calcium Signaling

Lynes

Raturi

Shenkman

et al. 2013

Journal of Cell Science

137

111

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SummaryThe palmitoylation of calnexin serves to enrich calnexin on the mitochondria-associated membrane (MAM). Given a lack of information on the significance of this finding, we have investigated how this endoplasmic reticulum (ER)-internal sorting signal affects the functions of calnexin. Our results demonstrate that palmitoylated calnexin interacts with sarcoendoplasmic reticulum (SR) Ca 2+ transport ATPase (SERCA) 2b and that this interaction determines ER Ca 2+ content and the regulation of ER-mitochondria Ca 2+ crosstalk. In contrast, non-palmitoylated calnexin interacts with the oxidoreductase ERp57 and performs its well-known function in quality control. Interestingly, our results also show that calnexin palmitoylation is an ER-stress-dependent mechanism. Following a short-term ER stress, calnexin quickly becomes less palmitoylated, which shifts its function from the regulation of Ca 2+ signaling towards chaperoning and quality control of known substrates. These changes also correlate with a preferential distribution of calnexin to the MAM under resting conditions, or the rough ER and ER quality control compartment (ERQC) following ER stress. Our results have therefore identified the switch that assigns calnexin either to Ca 2+ signaling or to protein chaperoning.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Palmitoylation is the Switch that Assigns Calnexin to Quality Control or ER Calcium Signaling

Lynes

Raturi

Shenkman

et al. 2013

Journal of Cell Science

137

111

View full text Add to dashboard Cite

show abstract

“…Correct folding of the transporter is stabilized by its four N-glycan chains, but it also requires an interaction with several ER chaperones (22). For example, calnexin (CNX) transiently binds to an intermediate hypoglycosylated transporter precursor, and it facilitates GlyT2 processing.…”

mentioning

confidence: 99%

Molecular Basis of the Dominant Negative Effect of a Glycine Transporter 2 Mutation Associated with Hyperekplexia

Arribas-González

Juan-Sanz

Aragón

et al. 2015

Journal of Biological Chemistry

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Background: Hyperekplexia is caused by defective glycinergic neurotransmission. Results: A dominant negative glycine transporter-2 mutant is trapped in a calnexin-bound state and retains wild type GlyT2 in the endoplasmic reticulum. Conclusion: Chemical chaperones rescue the folding defect of the mutant and overcome its dominant negative effect. Significance: This opens the way to revert the dominant negative effect exerted by the mutant associated with hyperekplexia in neurons.

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“…The build-up of ROS causes protein misfolding in the ER which, may result in possible immune system defects precipitating inappropriate autoimmune response against melanocytes (Figure 3). Calreticulin (CRT) is a ubiquitous protein localized predominantly in the ER and plays a major role in intracellular Ca 2+ homeostasis [213][214][215][216]. Cell surface localization of CRT has been reported on T cells, neutrophils, monocytes, macrophages and dendritic cells [217][218][219][220].…”

Section: Cross Talk Between Oxidative Stress Er Stress and Immune Symentioning

confidence: 99%

Could ER Stress Be A Major Link Between Oxidative Stress And Autoimmunity In Vitiligo?

Mansuri¹,

Singh²

2014

J Pigment Disord

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Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum

Cited by 102 publications

References 73 publications

Palmitoylation is the Switch that Assigns Calnexin to Quality Control or ER Calcium Signaling

Palmitoylation is the Switch that Assigns Calnexin to Quality Control or ER Calcium Signaling

Molecular Basis of the Dominant Negative Effect of a Glycine Transporter 2 Mutation Associated with Hyperekplexia

Could ER Stress Be A Major Link Between Oxidative Stress And Autoimmunity In Vitiligo?

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