YBR170C
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| Systematic name | YBR170C |
| Gene name | NPL4 |
| Aliases | HRD4 |
| Feature type | ORF, Verified |
| Coordinates | Chr II:578086..576344 |
| Primary SGDID | S000000374 |
Description of YBR170C: Substrate-recruiting cofactor of the Cdc48p-Npl4p-Ufd1p segregase; assists Cdc48p in the dislocation of misfolded, polyubiquitinated ERAD substrates that are subsequently delivered to the proteasome for degradation; also involved in the regulated destruction of resident ER membrane proteins, such as HMG-CoA reductase (Hmg1/2p) and cytoplasmic proteins (Fbp1p); role in mobilizing membrane bound transcription factors by regulated ubiquitin/proteasome-dependent processing (RUP)[1][2][3][4][5][6]
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References
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- ↑ Barbin L, et al. (2010) The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase. Biochem Biophys Res Commun 394(2):335-41 SGD PMID 20206597
- ↑ Bays NW, et al. (2001) HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol Biol Cell 12(12):4114-28 SGD PMID 11739805
- ↑ Heo JM, et al. (2010) A stress-responsive system for mitochondrial protein degradation. Mol Cell 40(3):465-80 SGD PMID 21070972
- ↑ Hitchcock AL, et al. (2001) The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol Biol Cell 12(10):3226-41 SGD PMID 11598205
- ↑ Rape M, et al. (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107(5):667-77 SGD PMID 11733065
- ↑ Ye Y, et al. (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162(1):71-84 SGD PMID 12847084
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