Publication Date:
1994-10-21
Description:
The endoplasmic reticulum (ER) contains molecular chaperones that facilitate the folding of proteins in mammalian cells. Biosynthetic labeling was used to study the interactions of two chaperones, BiP and calnexin, with vesicular stomatitis virus (VSV) glycoprotein (G protein). Coimmunoprecipitation of G protein with the chaperones showed that BiP bound maximally to early folding intermediates of G protein, whereas calnexin bound after a short lag to more folded molecules. Castanospermine, an inhibitor of ER glucosidases, blocked the binding of proteins to calnexin and inhibited G protein folding. Interaction with calnexin was necessary for efficient folding of G protein and for retention of partially folded forms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammond, C -- Helenius, A -- P01 CA46128/CA/NCI NIH HHS/ -- R01 GM38346/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):456-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939687" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
CHO Cells
;
Calcium-Binding Proteins/chemistry/*metabolism
;
Calnexin
;
Carrier Proteins/chemistry/*metabolism
;
Cell Membrane/metabolism
;
Cricetinae
;
Cytoplasm/metabolism
;
Glycoproteins/*chemistry/metabolism
;
Heat-Shock Proteins/chemistry/metabolism
;
Indolizines/pharmacology
;
*Membrane Glycoproteins
;
*Molecular Chaperones
;
Protein Folding
;
Vesicular stomatitis Indiana virus/*chemistry/physiology
;
Viral Envelope Proteins/*chemistry/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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