Abstract：
:The hemagglutinin of influenza virus is synthesized as a monomeric subunit that is cotranslationally translocated across the membrane of the rough endoplasmic reticulum. We show that folding and assembly of hemagglutinin monomers into trimeric structures takes approximately 7-10 min and is completed before the protein leaves the endoplasmic reticulum. Mutants of hemagglutinin that fail to be transported from the endoplasmic reticulum are blocked at different stages of the folding pathway. Unfolded molecules of hemagglutinin are associated with a cellular protein of 77 kd that has been shown previously to bind to IgG heavy chain in the endoplasmic reticulum of certain myelomas. We discuss why assembly of native structures is required for transport of proteins through the exocytotic pathway.
journal_name
Celljournal_title
Cellauthors
Gething MJ,McCammon K,Sambrook Jdoi
10.1016/0092-8674(86)90076-0subject
Has Abstractpub_date
1986-09-12 00:00:00pages
939-50issue
6eissn
0092-8674issn
1097-4172pii
0092-8674(86)90076-0journal_volume
46pub_type
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