The N-terminal amphipathic alpha-helix of viperin mediates localization to the cytosolic face of the endoplasmic reticulum and inhibits protein secretion.

ABSTRACT: Viperin is an evolutionarily conserved interferon-inducible protein that localizes to the endoplasmic reticulum (ER) and inhibits a number of DNA and RNA viruses. In this study, we report that viperin specifically localizes to the cytoplasmic face of the ER and that an amphipathic alpha-helix at its N terminus is necessary for the ER localization of viperin and sufficient to promote ER localization of a reporter protein, dsRed. Overexpression of intact viperin but not the amphipathic alpha-helix fused to dsRed induced crystalloid ER. Consistent with other proteins that induce crystalloid ER, viperin self-associates, and it does so independently of the amphipathic alpha-helix. Viperin expression also affected the transport of soluble but not membrane-associated proteins. Expression of intac

SUBMITTER: Hinson ER 

PROVIDER: S-EPMC2640954 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature