Abstract：
:Secretory proteins are segregated from cytosolic proteins by their translocation into the endoplasmic reticulum (ER). A modified secretory protein trapped during translocation across the ER membrane can be crosslinked to two previously identified proteins, Sec61p and BiP (Kar2p). The dependence of this cross-linking upon proteins and small molecules was examined. Mutations in SEC62 and SEC63 decrease the ability of Sec61p to be cross-linked to the secretory polypeptide trapped in translocation. ATP is also required for interaction of Sec61p with the secretory protein. Three kar2 alleles display defective translocation in vitro. Two of these alleles also decrease the ability of Sec61p to be cross-linked to the secretory protein. The third allele, while exhibiting a severe translocation defect, does not affect the interaction of Sec61p with the secretory protein. These results suggest that Sec61p is directly involved in translocation and that BiP acts at two stages of the translocation cycle.
journal_name
Celljournal_title
Cellauthors
Sanders SL,Whitfield KM,Vogel JP,Rose MD,Schekman RWdoi
10.1016/0092-8674(92)90415-9subject
Has Abstractpub_date
1992-04-17 00:00:00pages
353-65issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(92)90415-9journal_volume
69pub_type
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