Journal
FEBS LETTERS
Volume 582, Issue 21-22, Pages 3179-3184Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.07.062
Keywords
BiP; HBV; membrane topology; translocational regulation; posttranslational translocation
Funding
- Deutsche Forschungsgemeinschaft [SFB 490-D1, PR 305/1-3]
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The hepatitis B virus L protein forms a dual topology in the endoplasmic reticulum (ER) via a process involving cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain. Here, we show that preS posttranslocation depends on the action of the ER chaperone BiP. To modulate the in vivo BiP activity, we designed an approach based on overexpressing its positive and negative regulators, ER-localized DnaJ-domain containing protein 4 (ERdj4) and BiP-associated protein ( BAP), respectively. The feasibility of this approach was confirmed by demonstrating that BAP, but not ERdj4, destabilizes the L/BiP complex. Overexpressing BAP or ERdj4 inhibits preS posttranslocation as does the reduction of ATP levels. These results hint to a new role of BiP in guiding posttranslational polypeptide import into the mammalian ER. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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