|
TCP1
| TCP1 |
|---|
| Estruturas dispoñibles |
|---|
| PDB | Buscar ortólogos: PDBe, RCSB |
|---|
| Identificadores |
|---|
| Nomenclatura |
Outros nomes
- TCP1, CCT-alfa, CCT1, CCTa, D6S230E, TCP-1-alfa, complexo t 1, T-complex 1
|
|---|
| Símbolos | TCP1 (HGNC: 11655) TCP1, CCT-alfa, CCT1, CCTa, D6S230E, TCP-1-alfa |
|---|
Identificadores
externos | |
|---|
| Locus | Cr. 6 q25.3 |
|---|
|
|---|
| Padrón de expresión de ARNm |
|---|
![]() |  |  | | Máis información | |
|---|
| Ortólogos |
|---|
| Especies | |
|---|
| Entrez | |
|---|
| Ensembl | |
|---|
| UniProt | |
|---|
RefSeq
(ARNm) | |
|---|
RefSeq
(proteína) NCBI | |
|---|
| Localización (UCSC) | |
|---|
| PubMed (Busca) | |
|---|
A TCP1 ou proteína do complexo T 1, subunidade alfa ou complexo t 1[a] é unha proteína que en humanos está codificada polo xene TCP1 do cromosoma 6.[1][2][3]
Función
Este xene codifica unha chaperona molecular que é un membro do complexo TRiC. Este complexo consta de dous aneis idénticos empillados, cada un contén oito proteínas diferentes. Os polipéptidos non pregados entran na cavidade central do complexo e son pregados de maneira dependente do ATP. O complexo prega varias proteínas, incluíndo a tubulina. Caracterizáronse variantes de empalme alternativo transcricional deste xene, que codifican diferentes isoformas.[3]
Interaccións
TCP1 presenta interaccións con PPP4C[4][5] e HDAC3.[6] A CCT tamén interacciona directamente co receptor 1 de LDL oxidado de tipo lectina (LOX-1), mentres que o seu ligando a lipoproteína de baixa densidade oxidada (OxLDL) disocia CCT de LOX-1.[7]
Notas a rodapé
- ↑ O termo "TCP-1" ampliouse de forma variada como "proteína do complexo T 1" e "polipéptido do complexo sen rabo 1". O "complexo T" é o mesmo que o complexo sen rabo ou tailless, un locus CCT asociado coa lonxitude do rabo en ratos.
Notas
- ↑ Fonatsch C, Gradl G, Ragoussis J, Ziegler A (outubro de 1987). "Assignment of the TCP1 locus to the long arm of human chromosome 6 by in situ hybridization". Cytogenet Cell Genet 45 (2): 109–12. PMID 3476253. doi:10.1159/000132439.
- ↑ Willison K, Kelly A, Dudley K, Goodfellow P, Spurr N, Groves V, Gorman P, Sheer D, Trowsdale J (novembro de 1987). "The human homologue of the mouse t-complex gene, TCP1, is located on chromosome 6 but is not near the HLA region". EMBO J 6 (7): 1967–74. PMC 553584. PMID 3653076. doi:10.1002/j.1460-2075.1987.tb02459.x.
- ↑ 3,0 3,1 "Entrez Gene: TCP1 t-complex 1".
- ↑ Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault M, Gingras AC (outubro de 2008). "PP4R4/KIAA1622 Forms a Novel Stable Cytosolic Complex with Phosphoprotein Phosphatase 4". J. Biol. Chem. 283 (43): 29273–84. PMC 2662017. PMID 18715871. doi:10.1074/jbc.M803443200.
- ↑ Gingras AC, Caballero M, Zarske M, Sanchez A, Hazbun TR, Fields S, Sonenberg N, Hafen E, Raught B, Aebersold R (novembro de 2005). "A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Mol. Cell. Proteomics 4 (11): 1725–40. PMID 16085932. doi:10.1074/mcp.M500231-MCP200.
- ↑ Guenther MG, Yu J, Kao GD, Yen TJ, Lazar MA (decembro de 2002). "Assembly of the SMRT–histone deacetylase 3 repression complex requires the TCP-1 ring complex". Genes Dev. 16 (24): 3130–5. PMC 187500. PMID 12502735. doi:10.1101/gad.1037502.
- ↑ Bakthavatsalam D, Soung RH, Tweardy DJ, Chiu W, Dixon RA, Woodside DG (xuño de 2014). "Chaperonin-containing TCP-1 complex directly binds to the cytoplasmic domain of the LOX-1 receptor.". FEBS Lett 588 (13): 2133–40. PMC 4100626. PMID 24846140. doi:10.1016/j.febslet.2014.04.049.
Véxase tamén
Bibliografía
- Horwich AL, Willison KR (1993). "Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1". Philos. Trans. R. Soc. Lond. B Biol. Sci. 339 (1289): 313–25; discussion 325–6. PMID 8098536. doi:10.1098/rstb.1993.0030.
- Burston SG, Clarke AR (1997). "Molecular chaperones: physical and mechanistic properties". Essays Biochem. 29: 125–36. PMID 9189717.
- Blanché H, Wright LG, Vergnaud G, de Gouyon B, Lauthier V, Silver LM, Dausset J, Cann HM, Spielman RS (1992). "Genetic mapping of three human homologues of murine t-complex genes localizes TCP10 to 6q27, 15 cM distal to TCP1 and PLG". Genomics 12 (4): 826–8. PMID 1572657. doi:10.1016/0888-7543(92)90317-L.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. PMID 1602151. doi:10.1016/S0163-4453(05)80037-4.
- Yaffe MB, Farr GW, Miklos D, Horwich AL, Sternlicht ML, Sternlicht H (1992). "TCP1 complex is a molecular chaperone in tubulin biogenesis". Nature 358 (6383): 245–8. Bibcode:1992Natur.358..245Y. PMID 1630491. doi:10.1038/358245a0.
- Lewis VA, Hynes GM, Zheng D, Saibil H, Willison K (1992). "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol". Nature 358 (6383): 249–52. Bibcode:1992Natur.358..249L. PMID 1630492. doi:10.1038/358249a0.
- Ursic D, Culbertson MR (1991). "The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes". Mol. Cell. Biol. 11 (5): 2629–40. PMC 360032. PMID 1901944. doi:10.1128/mcb.11.5.2629.
- Kirchhoff C, Willison K (1990). "Nucleotide and amino-acid sequence of human testis-derived TCP1". Nucleic Acids Res. 18 (14): 4247. PMC 331189. PMID 2377466. doi:10.1093/nar/18.14.4247.
- Roobol A, Holmes FE, Hayes NV, Baines AJ, Carden MJ (1995). "Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in subunit composition within single cells". J. Cell Sci. 108 (4): 1477–88. PMID 7615668. doi:10.1242/jcs.108.4.1477.
- Ashworth A (1994). "Two acetyl-CoA acetyltransferase genes located in the t-complex region of mouse chromosome 17 partially overlap the Tcp-1 and Tcp-1x genes". Genomics 18 (2): 195–8. PMID 7904580. doi:10.1006/geno.1993.1454.
- Miklos D, Caplan S, Mertens D, Hynes G, Pitluk Z, Kashi Y, Harrison-Lavoie K, Stevenson S, Brown C, Barrell B (1994). "Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta". Proc. Natl. Acad. Sci. U.S.A. 91 (7): 2743–7. Bibcode:1994PNAS...91.2743M. PMC 43446. PMID 7908441. doi:10.1073/pnas.91.7.2743.
- Chen X, Sullivan DS, Huffaker TC (1994). "Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo". Proc. Natl. Acad. Sci. U.S.A. 91 (19): 9111–5. Bibcode:1994PNAS...91.9111C. PMC 44757. PMID 7916460. doi:10.1073/pnas.91.19.9111.
- Kubota H, Hynes G, Carne A, Ashworth A, Willison K (1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Curr. Biol. 4 (2): 89–99. PMID 7953530. doi:10.1016/S0960-9822(94)00024-2.
- Frydman J, Hartl FU (1996). "Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms". Science 272 (5267): 1497–502. Bibcode:1996Sci...272.1497F. PMID 8633246. doi:10.1126/science.272.5267.1497.
- Moudjou M, Bordes N, Paintrand M, Bornens M (1996). "gamma-Tubulin in mammalian cells: the centrosomal and the cytosolic forms". J. Cell Sci. 109 (4): 875–87. PMID 8718679. doi:10.1242/jcs.109.4.875.
- Morrison K, Papapetrou C, Attwood J, Hol F, Lynch SA, Sampath A, Hamel B, Burn J, Sowden J, Stott D, Mariman E, Edwards YH (1997). "Genetic mapping of the human homologue (T) of mouse T(Brachyury) and a search for allele association between human T and spina bifida". Hum. Mol. Genet. 5 (5): 669–74. PMID 8733136. doi:10.1093/hmg/5.5.669.
- Masuno M, Fukao T, Song XQ, Yamaguchi S, Orii T, Kondo N, Imaizumi K, Kuroki Y (1997). "Assignment of the human cytosolic acetoacetyl-coenzyme A thiolase (ACAT2) gene to chromosome 6q25.3-q26". Genomics 36 (1): 217–8. PMID 8812443. doi:10.1006/geno.1996.0452.
|
|
