Difference between revisions of "YER125W"
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| − | '''Description of YER125W:''' E3 ubiquitin ligase of the NEDD4 family; involved in regulating many cellular processes including MVB sorting, heat shock response, transcription, endocytosis, and ribosome stability; human homolog is involved in Liddle syndrome; mutant tolerates aneuploidy<ref name='S000060760'>Dunn R and Hicke L (2001) Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol Biol Cell 12(2):421-35 {{SGDpaper|S000060760}} PMID 11179425</ref><ref name='S000074703'>Gajewska B, et al. (2003) Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast. Curr Genet 43(1):1-10 {{SGDpaper|S000074703}} PMID 12684839</ref><ref name='S000053994'>Huibregtse JM, et al. (1997) The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc Natl Acad Sci U S A 94(8):3656-61 {{SGDpaper|S000053994}} PMID 9108033</ref><ref name='S000073465'>Kaida D, et al. (2003) Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in budding yeast. Biochem Biophys Res Commun 306(4):1037-41 {{SGDpaper|S000073465}} PMID 12821147</ref><ref name='S000077431'>Katzmann DJ, et al. (2004) Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol Biol Cell 15(2):468-80 {{SGDpaper|S000077431}} PMID 14657247</ref><ref name='S000145720'>Shcherbik N and Pestov DG (2011) The ubiquitin ligase Rsp5 is required for ribosome stability in Saccharomyces cerevisiae. RNA () {{SGDpaper|S000145720}} PMID 21665996</ref><ref name='S000086109'>Somesh BP, et al. (2005) Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 121(6):913-23 {{SGDpaper|S000086109}} PMID 15960978</ref><ref name='S000136872'>Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83 | + | '''Description of YER125W:''' E3 ubiquitin ligase of the NEDD4 family; involved in regulating many cellular processes including MVB sorting, heat shock response, transcription, endocytosis, and ribosome stability; human homolog is involved in Liddle syndrome; mutant tolerates aneuploidy; ubiquitylates Sec23p<ref name='S000060760'>Dunn R and Hicke L (2001) Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol Biol Cell 12(2):421-35 {{SGDpaper|S000060760}} PMID 11179425</ref><ref name='S000074703'>Gajewska B, et al. (2003) Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast. Curr Genet 43(1):1-10 {{SGDpaper|S000074703}} PMID 12684839</ref><ref name='S000053994'>Huibregtse JM, et al. (1997) The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc Natl Acad Sci U S A 94(8):3656-61 {{SGDpaper|S000053994}} PMID 9108033</ref><ref name='S000073465'>Kaida D, et al. (2003) Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in budding yeast. Biochem Biophys Res Commun 306(4):1037-41 {{SGDpaper|S000073465}} PMID 12821147</ref><ref name='S000077431'>Katzmann DJ, et al. (2004) Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol Biol Cell 15(2):468-80 {{SGDpaper|S000077431}} PMID 14657247</ref><ref name='S000143769'>Ossareh-Nazari B, et al. (2010) The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23. Exp Cell Res 316(20):3351-7 {{SGDpaper|S000143769}} PMID 20846524</ref><ref name='S000145720'>Shcherbik N and Pestov DG (2011) The ubiquitin ligase Rsp5 is required for ribosome stability in Saccharomyces cerevisiae. RNA () {{SGDpaper|S000145720}} PMID 21665996</ref><ref name='S000086109'>Somesh BP, et al. (2005) Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 121(6):913-23 {{SGDpaper|S000086109}} PMID 15960978</ref><ref name='S000136872'>Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83 |
{{SGDpaper|S000136872}} PMID 20850176</ref> | {{SGDpaper|S000136872}} PMID 20850176</ref> | ||
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Revision as of 13:05, 13 October 2011
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| Systematic name | YER125W |
| Gene name | RSP5 |
| Aliases | MDP1, MUT2, NPI1, SMM1, UBY1 |
| Feature type | ORF, Verified |
| Coordinates | Chr V:410189..412618 |
| Primary SGDID | S000000927 |
Description of YER125W: E3 ubiquitin ligase of the NEDD4 family; involved in regulating many cellular processes including MVB sorting, heat shock response, transcription, endocytosis, and ribosome stability; human homolog is involved in Liddle syndrome; mutant tolerates aneuploidy; ubiquitylates Sec23p[1][2][3][4][5][6][7][8][9]
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Community Commentary
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References
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- ↑ Dunn R and Hicke L (2001) Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol Biol Cell 12(2):421-35 SGD PMID 11179425
- ↑ Gajewska B, et al. (2003) Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast. Curr Genet 43(1):1-10 SGD PMID 12684839
- ↑ Huibregtse JM, et al. (1997) The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc Natl Acad Sci U S A 94(8):3656-61 SGD PMID 9108033
- ↑ Kaida D, et al. (2003) Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in budding yeast. Biochem Biophys Res Commun 306(4):1037-41 SGD PMID 12821147
- ↑ Katzmann DJ, et al. (2004) Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol Biol Cell 15(2):468-80 SGD PMID 14657247
- ↑ Ossareh-Nazari B, et al. (2010) The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23. Exp Cell Res 316(20):3351-7 SGD PMID 20846524
- ↑ Shcherbik N and Pestov DG (2011) The ubiquitin ligase Rsp5 is required for ribosome stability in Saccharomyces cerevisiae. RNA () SGD PMID 21665996
- ↑ Somesh BP, et al. (2005) Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 121(6):913-23 SGD PMID 15960978
- ↑ Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83 SGD PMID 20850176
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