ArticleThe Journal of biological chemistry2011
The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Biallelic ELOVL1 Variants Are Linked to Hypomyelinating Leukodystrophy, Movement Disorder, and Ichthyosis.Movement disorders : official journal of the Movement Disorder Society · 2025Article
- Overexpression of Tn antigen induces chronic pancreatitis in mice.Scientific reports · 2025Article
- Emerging Roles of the Unique Molecular Chaperone Cosmc in the Regulation of Health and Disease.Biomolecules · 2022Review
- Assistance for Folding of Disease-Causing Plasma Membrane Proteins.Biomolecules · 2020Review
- "Stuck on sugars - how carbohydrates regulate cell adhesion, recognition, and signaling".Glycoconjugate journal · 2019Article
- Loss of complex O-glycosylation impairs exocrine pancreatic function and induces MODY8-like diabetes in mice.Experimental & molecular medicine · 2018Article
- The Cytokinin Oxidase/Dehydrogenase CKX1 Is a Membrane-Bound Protein Requiring Homooligomerization in the Endoplasmic Reticulum for Its Cellular Activity.Plant physiology · 2018Article
- Article
- Functional Consequences of Differential O-glycosylation of MUC1, MUC4, and MUC16 (Downstream Effects on Signaling).Biomolecules · 2016Review
- Identification of a novel protein binding motif within the T-synthase for the molecular chaperone Cosmc.The Journal of biological chemistry · 2014Article
- Anchors aweigh: protein localization and transport mediated by transmembrane domains.Trends in cell biology · 2013Review
- Tight complex formation between Cosmc chaperone and its specific client non-native T-synthase leads to enzyme activity and client-driven dissociation.The Journal of biological chemistry · 2012Article
- Molecular cloning of a xylosyltransferase that transfers the second xylose to O-glucosylated epidermal growth factor repeats of notch.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The molecular basis for retention of integral membrane proteins in the endoplasmic reticulum (ER) is not well understood. We recently discovered a novel ER molecular chaperone termed Cosmc, which is essential for folding and normal activity of the Golgi enzyme T-synthase. Cosmc, a type II single-pass transmembrane protein, lacks any known ER retrieval/retention motifs. To explore specific ER localization determinants in Cosmc we generated a series of Cosmc mutants along with chimeras of Cosmc with a non-ER resident type II protein, the human transferrin receptor. Here we show that the 18 amino acid transmembrane domain (TMD) of Cosmc is essential for ER localization and confers ER retention to select chimeras. Moreover, mutations of a single Cys residue within the TMD of Cosmc prevent formation of disulfide-bonded dimers of Cosmc and eliminate ER retention. These studies reveal that Cosmc has a unique ER-retention motif within its TMD and provide new insights into the molecular mechanisms by which TMDs of resident ER proteins contribute to ER localization.
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Registered trials
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