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.
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Conference Article|
September 19 2008
Regulation of ER-associated degradation via p97/VCP-interacting motif
Petek Ballar;
Petek Ballar
1
*Ege University, School of Pharmacy, Biochemistry Department, Izmir 35100, Turkey
1To whom correspondence should be addressed (email petek.ballar@ege.edu.tr).
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Shengyun Fang
Shengyun Fang
†University of Maryland Biotechnology Institute, Medical Biotechnology Center, Baltimore, MD 21201, U.S.A.
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Publisher: Portland Press Ltd
Received:
March 11 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem Soc Trans (2008) 36 (5): 818–822.
Article history
Received:
March 11 2008
Citation
Petek Ballar, Shengyun Fang; Regulation of ER-associated degradation via p97/VCP-interacting motif. Biochem Soc Trans 1 October 2008; 36 (5): 818–822. doi: https://doi.org/10.1042/BST0360818
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