Difference between revisions of "YDR057W"
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| − | '''Description of YDR057W:''' ER quality-control lectin; integral subunit of the HRD ligase; | + | '''Description of YDR057W:''' ER quality-control lectin; integral subunit of the HRD ligase; binds to glycans with terminal alpha-1,6 linked mannose on misfolded N-glycosylated proteins and participates in targeting proteins to ERAD; member of the OS-9 protein family<ref name='S000079716'>Buschhorn BA, et al. (2004) A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. FEBS Lett 577(3):422-6 {{SGDpaper|S000079716}} PMID 15556621</ref><ref name='S000113700'>Kim W, et al. (2005) Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell 19(6):753-64 {{SGDpaper|S000113700}} PMID 16168371</ref><ref name='S000086775'>Bhamidipati A, et al. (2005) Exploration of the Topological Requirements of ERAD Identifies Yos9p as a Lectin Sensor of Misfolded Glycoproteins in the ER Lumen. Mol Cell 19(6):741-51 {{SGDpaper|S000086775}} PMID 16168370</ref><ref name='S000086711'>Szathmary R, et al. (2005) Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell 19(6):765-75 {{SGDpaper|S000086711}} PMID 16168372</ref><ref name='S000131715'>Quan EM, et al. (2008) Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol Cell 32(6):870-7 {{SGDpaper|S000131715}} PMID 19111666</ref><ref name='S000120436'>Gauss R, et al. (2006) A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Nat Cell Biol 8(8):849-54 |
{{SGDpaper|S000120436}} PMID 16845381</ref> | {{SGDpaper|S000120436}} PMID 16845381</ref> | ||
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Revision as of 13:05, 30 October 2009
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| Systematic name | YDR057W |
| Gene name | YOS9 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:565926..567554 |
| Primary SGDID | S000002464 |
Description of YDR057W: ER quality-control lectin; integral subunit of the HRD ligase; binds to glycans with terminal alpha-1,6 linked mannose on misfolded N-glycosylated proteins and participates in targeting proteins to ERAD; member of the OS-9 protein family[1][2][3][4][5][6]
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Protein Details
Protein Function/Process
The ER lumenal protein Yos9p is required for both release of DHFR and degradation of multiple ERAD substrates. Yos9p forms a complex with substrates and has a sugar binding pocket that is essential for its ERAD function. Nonetheless, substrate recognition persists even when the sugar binding site is mutated or CPY* is unglycosylated. These and other considerations suggest that Yos9p plays a critical role in the bipartite recognition of terminally misfolded glycoproteins. [3] [7]
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References
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- ↑ Buschhorn BA, et al. (2004) A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. FEBS Lett 577(3):422-6 SGD PMID 15556621
- ↑ Kim W, et al. (2005) Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell 19(6):753-64 SGD PMID 16168371
- ↑ 3.0 3.1 Bhamidipati A, et al. (2005) Exploration of the Topological Requirements of ERAD Identifies Yos9p as a Lectin Sensor of Misfolded Glycoproteins in the ER Lumen. Mol Cell 19(6):741-51 SGD PMID 16168370
- ↑ Szathmary R, et al. (2005) Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell 19(6):765-75 SGD PMID 16168372
- ↑ Quan EM, et al. (2008) Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol Cell 32(6):870-7 SGD PMID 19111666
- ↑ Gauss R, et al. (2006) A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Nat Cell Biol 8(8):849-54 SGD PMID 16845381
- ↑ submitted by Maya Schuldiner on 2005-12-09
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