Journal
SCIENCE
Volume 288, Issue 5464, Pages 331-333Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.288.5464.331
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A variety of molecular chaperones and folding enzymes assist the folding of newly synthesized proteins in the endoplasmic reticulum. Here we investigated why some glycoproteins interact with the molecular chaperone sip, and others with the calnexin/calreticulin pathway. The folding of Semliki forest virus glycoproteins and influenza hemagglutinin was studied in Living cells. The initial choice of chaperone depended on the Location of N-linked glycans in the growing nascent chain. Direct interaction with calnexin and calreticulin without prior interaction with BiP occurred if glycans were present within about 50 residues of the protein's NH2-terminus.
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