Regulation of ER-associated degradation via p97/VCP-interacting motif


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Ballar P. , FANG S.

BIOCHEMICAL SOCIETY TRANSACTIONS, vol.36, pp.818-822, 2008 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 36
  • Publication Date: 2008
  • Doi Number: 10.1042/bst0360818
  • Title of Journal : BIOCHEMICAL SOCIETY TRANSACTIONS
  • Page Numbers: pp.818-822

Abstract

p97/VCP (valosin-containing protein) is a cytosolic AAA (ATPase associated with various cellular activities) essential for retrotiranslocation of misfolded proteins during ERAD [ER (endoplasmic reticulum)-associated degradation]. gp78, an ERAD ubiquitin ligase, is one of the p97/VCP recruitment proteins localized to the ER membrane. A newly identified VIM (p97/VCP-interacting motif) in gp78 has brought about novel insights into mechanisms of ERAD, such as the presence of a p97/VCP-dependent but Ufd1-independent retrotranslocation during gp78-mediated ERAD. Additionally, SVIP (small p97/VCP-interacting protein), which contains a VIM in its N-terminal region, negatively regulates ERAD by uncoupling p97/VCP and Derlin1 from gp78. Thus SVIP may protect cells from damage by extravagant ERAD.