Difference between revisions of "YBR170C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YBR170C YBR170C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000374 YBR170C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''NPL4 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''NPL4 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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|nowrap| Chr II:578081..576339
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|nowrap| Chr II:578086..576344
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000374
 
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'''Description of {{PAGENAME}}:''' Endoplasmic reticulum and nuclear membrane protein, forms a complex with Cdc48p and Ufd1p that recognizes ubiquitinated proteins in the endoplasmic reticulum and delivers them to the proteasome for degradation<ref name='S000071485'>Bays NW and Hampton RY (2002) Cdc48-Ufd1-Npl4: stuck in the middle with Ub. Curr Biol 12(10):R366-71 {{SGDpaper|S000071485}} PMID 12015140</ref><ref name='S000069870'>Bays NW, et al. (2001) HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol Biol Cell 12(12):4114-28 {{SGDpaper|S000069870}} PMID 11739805</ref><ref name='S000066133'>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
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'''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)<ref name='S000133435'>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 {{SGDpaper|S000133435}} PMID 20206597</ref><ref name='S000069870'>Bays NW, et al. (2001) HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol Biol Cell 12(12):4114-28 {{SGDpaper|S000069870}} PMID 11739805</ref><ref name='S000140158'>Heo JM, et al. (2010) A stress-responsive system for mitochondrial protein degradation. Mol Cell 40(3):465-80 {{SGDpaper|S000140158}} PMID 21070972</ref><ref name='S000066133'>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 {{SGDpaper|S000066133}} PMID 11598205</ref><ref name='S000074009'>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 {{SGDpaper|S000074009}} PMID 11733065</ref><ref name='S000073828'>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
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  {{SGDpaper|S000066133}} PMID 11598205</ref>
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  {{SGDpaper|S000073828}} PMID 12847084</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 13:05, 3 July 2012

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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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  1. ↑ 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
  2. ↑ 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
  3. ↑ Heo JM, et al. (2010) A stress-responsive system for mitochondrial protein degradation. Mol Cell 40(3):465-80 SGD PMID 21070972
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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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