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Cell

Title:		Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP
Author(s):		Lyman SK; Schekman R;
Address:		"Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley 94720, USA"
Journal Title:		Cell
Year:		1997
Volume:		88
Issue:		1
Page Number:		85 - 96
DOI:		10.1016/s0092-8674(00)81861-9
ISSN/ISBN:		0092-8674 (Print) 0092-8674 (Linking)
Abstract:		"The translocation of a secretory precursor protein across the ER membrane comprises three phases: docking of the precursor at the membrane, insertion into the translocation pore, and exit from the pore into the ER lumen. We demonstrate that Sec62p, Sec71p and Sec72p form a translocon subcomplex that engages secretory precursors at the membrane site of the ER translocation machinery. Binding of a precursor to the subcomplex depends on the presence of an intact signal sequence and occurs only in the absence of ATP. In the presence of ATP, the precursor is released from the subcomplex in a reaction mediated by the lumenal hsp70, BiP. This release reaction, which is specific to BiP and requires interaction between BiP and the DnaJ homolog Sec63p, defines a role for BiP and Sec63p early in the ER translocation process"
Keywords:		Adenosine Triphosphate/physiology Biological Transport Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/genetics/metabolism Endoplasmic Reticulum/metabolism Fungal Proteins/*metabolism HSP70 Heat-Shock Proteins/*metabolism *Heat-Shock Proteins Macromolecu;
Notes:		"MedlineLyman, S K Schekman, R eng GM26755/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1997/01/10 Cell. 1997 Jan 10; 88(1):85-96. doi: 10.1016/s0092-8674(00)81861-9"