Regulation of ER-associated degradation via p97/VCP-interacting motif. (19th September 2008)

• Record Type: Journal Article
• Authors: Ballar, Petek; Fang, Shengyun
• Is Part Of: Biochemical Society transactions. Volume 36:Number 5(2008)
• Page Start: 818
• Page End: 822
• Publication Date: 2008-09-19
• Subjects: endoplasmic reticulum (ER) -- endoplasmic-reticulum-associated degradation (ERAD) -- gp78 -- p97/VCP-interacting motif (VIM) -- small p97/VCP-interacting protein (SVIP); Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0360818
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : p97/VCP (valosin-containing protein) is a cytosolic AAA (ATPase associated with various cellular activities) essential for retrotranslocation 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.