SLC35A2 deficiency reduces protein levels of core 1 β-1,3-galactosyltransferase 1 (C1GalT1) and its chaperone Cosmc and affects their subcellular localization
Author:
Funder
Narodowe Centrum Nauki
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology
Reference46 articles.
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2. Cloning and expression of human Core 1 beta1,3-galactosyltransferase;Ju;J. Biol. Chem.,2002
3. A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β3-galactosyltransferase;Ju;Proc. Natl. Acad. Sci. U. S. A.,2002
4. Regulation of protein O-glycosylation by the endoplasmic reticulum-localized molecular chaperone Cosmc;Ju;J. Cell Biol.,2008
5. Glycosyltransferase-specific golgi-targeting mechanisms;Petrosyan;J. Biol. Chem.,2012
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2. The glycosylation defect in solute carrier SLC35A2/SLC35A3 double knockout cells is rescued by SLC35A2–SLC35A3 and SLC35A3–SLC35A2 hybrids;FEBS Letters;2023-08-15
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