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.
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / genetics*
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Adenosine Triphosphatases / metabolism*
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Amino Acid Sequence*
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Animals
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Cell Cycle Proteins / chemistry
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Cell Cycle Proteins / genetics*
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Cell Cycle Proteins / metabolism*
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Endoplasmic Reticulum / metabolism*
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Humans
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Molecular Sequence Data
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Nuclear Proteins / metabolism
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Protein Folding
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Receptors, Autocrine Motility Factor
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Receptors, Cytokine / genetics
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Receptors, Cytokine / metabolism
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Sequence Alignment
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Ubiquitin-Protein Ligases / genetics
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Ubiquitin-Protein Ligases / metabolism
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Valosin Containing Protein
Substances
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Cell Cycle Proteins
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Nuclear Proteins
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Receptors, Cytokine
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AMFR protein, human
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Receptors, Autocrine Motility Factor
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Ubiquitin-Protein Ligases
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Adenosine Triphosphatases
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VCP protein, human
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Valosin Containing Protein