Regulation of ER-associated degradation via p97/VCP-interacting motif
Articles > Article ยท 2008
Authors: Petek BALLAR KIRMIZIBAYRAK, Shengyun FANG
Biochemical Society Transactions, Journal Indexed in SCI Expanded, International, WoS, 2008, vol 36, pp 818-822
DOI: 10.1042/bst0360818
Summary
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.