Difference between revisions of "YDR212W"
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| − | '''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein<ref name=' | + | '''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein<ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40 {{SGDpaper|S000042926}} PMID 1901944</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 {{SGDpaper|S000043581}} PMID 7865875</ref><ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000118957'>Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62 {{SGDpaper|S000118957}} PMID 16980959</ref><ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 |
| − | {{SGDpaper| | + | {{SGDpaper|S000075049}} PMID 14517260</ref> |
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Revision as of 13:05, 31 March 2009
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| Systematic name | YDR212W |
| Gene name | TCP1 |
| Aliases | CCT1 |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:887230..888909 |
| Primary SGDID | S000002620 |
Description of YDR212W: Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein[1][2][3][4][5]
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References
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- ↑ Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40 SGD PMID 1901944
- ↑ Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 SGD PMID 7865875
- ↑ Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 SGD PMID 9878052
- ↑ Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62 SGD PMID 16980959
- ↑ Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 SGD PMID 14517260
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