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Gene Review

TCP1  -  t-complex 1

Homo sapiens

Synonyms: CCT-alpha, CCT1, CCTA, CCTa, Ccta, ...
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Disease relevance of TCP1

  • Human TCP1 cDNA clones from both fibrosarcoma and B cell lines confirmed that there was a single expressed gene. mRNA transcripts of different sizes were accounted for by two different polyadenylation signals [1].
  • In addition to its importance in development, T has intrigued geneticists because of its association with the mouse t-haplotype; this haplotype is a variant form of the t-complex and is characterized by transmission ratio distortion, male sterility and recombination suppression [2].
  • Hereditary sensory neuropathy is caused by a mutation in the delta subunit of the cytosolic chaperonin-containing t-complex peptide-1 (Cct4 ) gene [3].
  • Transient promoter-reporter assays in murine lung epithelial (MLE-12) cells revealed that the core CCT alpha promoter (240 bp) was observed to exhibit a 40-fold, 8-fold, and 3-fold higher level of activity compared with the simian virus 40, human cytomegalovirus, and Rous sarcoma virus promoters, respectively [4].
  • Based on the specificity of the Htt-CCT1 interaction, the CCT1 substrate-binding domain may provide a versatile scaffold for therapeutic inhibitors of neurodegenerative disease [5].

Psychiatry related information on TCP1


High impact information on TCP1

  • Rat monoclonal antibodies recognizing TCP-1 have been prepared and used to immunoprecipitate and Western blot a 57 kd protein from germ cell and tissue culture cell extracts [8].
  • The t complex polypeptide 1 (TCP-1) is associated with the cytoplasmic aspect of Golgi membranes [8].
  • The distribution in spermatids suggested that TCP-1 was localized to structures often associated with the developing acrosome [8].
  • We suggest that TCP1 may represent one of a family of molecules in the eukaryotic cytosol involved in protein folding and regulated in part by their heteromeric associations [9].
  • TCP1 complex is a molecular chaperone in tubulin biogenesis [10].

Biological context of TCP1


Anatomical context of TCP1

  • RESULTS: Using two-dimensional gel analysis, we have identified nine different subunits of TCP-1-containing chaperonin complexes from mammalian testis and seven different subunits of such complexes from mouse F9 cells [14].
  • The 900K complex purified from reticulocyte lysate contained as its major constituent a 58K protein that cross-reacted with a monoclonal antiserum against mouse TCP1 [10].
  • TCP1, the human homolog of the Tcp-1 locus in the mouse, which is part of the murine t complex and codes for an abundant testicular germ-cell protein, has been mapped within the human genome by in situ hybridization [13].
  • TRiC-P5, a novel TCP1-related protein, is localized in the cytoplasm and in the nuclear matrix [15].
  • The biological component included tumor control probability (TCP) for PTV1 (TCP1), PTV2 (TCP2), and normal tissue complication probability (NTCP) for lung, spinal cord, and heart [16].

Associations of TCP1 with chemical compounds


Physical interactions of TCP1


Other interactions of TCP1

  • Our mapping data show that human T maps to 6q27 and lies between two other genes of the t-complex, TCP1 and TCP10 [2].
  • The human T-complex protein 1 gene, TCP1, encodes a molecular chaperone of the chaperonin family [21].
  • TCP1 and PLG do not recombine with each other and are separated from TCP10 by about 15 cM, while the corresponding mouse genes are no more than 4 cM apart [12].
  • The hetero-oligomeric eukaryotic chaperonin TRiC (TCP-1-ring complex, also called CCT) interacts cotranslationally with a diverse subset of newly synthesized proteins, including actin, tubulin, and luciferase, and facilitates their correct folding [22].
  • In contrast to CCT epsilon, no significant light regulation of CCT alpha was found in the mesocotyl [23].

Analytical, diagnostic and therapeutic context of TCP1


  1. The human homologue of the mouse t-complex gene, TCP1, is located on chromosome 6 but is not near the HLA region. Willison, K., Kelly, A., Dudley, K., Goodfellow, P., Spurr, N., Groves, V., Gorman, P., Sheer, D., Trowsdale, J. EMBO J. (1987) [Pubmed]
  2. Genetic mapping of the human homologue (T) of mouse T(Brachyury) and a search for allele association between human T and spina bifida. Morrison, K., Papapetrou, C., Attwood, J., Hol, F., Lynch, S.A., Sampath, A., Hamel, B., Burn, J., Sowden, J., Stott, D., Mariman, E., Edwards, Y.H. Hum. Mol. Genet. (1996) [Pubmed]
  3. Hereditary sensory neuropathy is caused by a mutation in the delta subunit of the cytosolic chaperonin-containing t-complex peptide-1 (Cct4 ) gene. Lee, M.J., Stephenson, D.A., Groves, M.J., Sweeney, M.G., Davis, M.B., An, S.F., Houlden, H., Salih, M.A., Timmerman, V., de Jonghe, P., Auer-Grumbach, M., Di Maria, E., Scaravilli, F., Wood, N.W., Reilly, M.M. Hum. Mol. Genet. (2003) [Pubmed]
  4. The CCT promoter directs high-level transgene expression in distal lung epithelial cell lines. Zhou, J., You, Y., Zabner, J., Ryan, A.J., Mallampalli, R.K. Am. J. Respir. Cell Mol. Biol. (2004) [Pubmed]
  5. The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Tam, S., Geller, R., Spiess, C., Frydman, J. Nat. Cell Biol. (2006) [Pubmed]
  6. Brain t-complex polypeptide 1 (TCP- 1) related to its natural substrate beta1 tubulin is decreased in Alzheimer's disease. Schuller, E., Gulesserian, T., Seidl, R., Cairns, N., Lube, G. Life Sci. (2001) [Pubmed]
  7. Cloning and characterisation of the Sry-related transcription factor gene Sox8. Schepers, G.E., Bullejos, M., Hosking, B.M., Koopman, P. Nucleic Acids Res. (2000) [Pubmed]
  8. The t complex polypeptide 1 (TCP-1) is associated with the cytoplasmic aspect of Golgi membranes. Willison, K., Lewis, V., Zuckerman, K.S., Cordell, J., Dean, C., Miller, K., Lyon, M.F., Marsh, M. Cell (1989) [Pubmed]
  9. T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Lewis, V.A., Hynes, G.M., Zheng, D., Saibil, H., Willison, K. Nature (1992) [Pubmed]
  10. TCP1 complex is a molecular chaperone in tubulin biogenesis. Yaffe, M.B., Farr, G.W., Miklos, D., Horwich, A.L., Sternlicht, M.L., Sternlicht, H. Nature (1992) [Pubmed]
  11. Nucleotide and amino-acid sequence of human testis-derived TCP1. Kirchhoff, C., Willison, K. Nucleic Acids Res. (1990) [Pubmed]
  12. Genetic mapping of three human homologues of murine t-complex genes localizes TCP10 to 6q27, 15 cM distal to TCP1 and PLG. Blanché, H., Wright, L.G., Vergnaud, G., de Gouyon, B., Lauthier, V., Silver, L.M., Dausset, J., Cann, H.M., Spielman, R.S. Genomics (1992) [Pubmed]
  13. Assignment of the TCP1 locus to the long arm of human chromosome 6 by in situ hybridization. Fonatsch, C., Gradl, G., Ragoussis, J., Ziegler, A. Cytogenet. Cell Genet. (1987) [Pubmed]
  14. Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin. Kubota, H., Hynes, G., Carne, A., Ashworth, A., Willison, K. Curr. Biol. (1994) [Pubmed]
  15. TRiC-P5, a novel TCP1-related protein, is localized in the cytoplasm and in the nuclear matrix. Joly, E.C., Tremblay, E., Tanguay, R.M., Wu, Y., Bibor-Hardy, V. J. Cell. Sci. (1994) [Pubmed]
  16. Inhomogeneous target-dose distributions: a dimension more for optimization? De Gersem, W.R., Derycke, S., Colle, C.O., De Wagter, C., De Neve, W.J. Int. J. Radiat. Oncol. Biol. Phys. (1999) [Pubmed]
  17. gamma-Tubulin in mammalian cells: the centrosomal and the cytosolic forms. Moudjou, M., Bordes, N., Paintrand, M., Bornens, M. J. Cell. Sci. (1996) [Pubmed]
  18. Regulation of CTP:phosphocholine cytidylyltransferase by amphitropism and relocalization. Cornell, R.B., Northwood, I.C. Trends Biochem. Sci. (2000) [Pubmed]
  19. Caveolin-1 interacts with the chaperone complex TCP-1 and modulates its protein folding activity. Doucey, M.A., Bender, F.C., Hess, D., Hofsteenge, J., Bron, C. Cell. Mol. Life Sci. (2006) [Pubmed]
  20. Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex. Guenther, M.G., Yu, J., Kao, G.D., Yen, T.J., Lazar, M.A. Genes Dev. (2002) [Pubmed]
  21. Origin of gene overlap: the case of TCP1 and ACAT2. Shintani, S., O'hUigin, C., Toyosawa, S., Michalová, V., Klein, J. Genetics (1999) [Pubmed]
  22. The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking. Etchells, S.A., Meyer, A.S., Yam, A.Y., Roobol, A., Miao, Y., Shao, Y., Carden, M.J., Skach, W.R., Frydman, J., Johnson, A.E. J. Biol. Chem. (2005) [Pubmed]
  23. Developmental and light-dependent changes of the cytosolic chaperonin containing TCP-1 (CCT) subunits in maize seedlings, and the localization in coleoptiles. Himmelspach, R., Nick, P., Schäfer, E., Ehmann, B. Plant J. (1997) [Pubmed]
  24. Analysis of chaperonin-containing TCP-1 subunits in the human keratinocyte two-dimensional protein database: further characterisation of antibodies to individual subunits. Hynes, G., Celis, J.E., Lewis, V.A., Carne, A., U, S., Lauridsen, J.B., Willison, K.R. Electrophoresis (1996) [Pubmed]
  25. Family-based association studies of the TCP1 gene and schizophrenia in the Chinese Han population. Tang, W., Shi, Y., Feng, G., Yan, L., Xing, Y., Zhu, S., Liu, J., Zhao, X., Tang, R., Du, J., Zhang, J., He, G., Liang, P., He, L. Journal of neural transmission (Vienna, Austria : 1996) (2006) [Pubmed]
  26. Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex. Hung, L.Y., Tang, C.J., Tang, T.K. Mol. Cell. Biol. (2000) [Pubmed]
  27. T-complex polypeptide-1 interacts with the erythrocyte cytoskeleton in response to elevated temperatures. Wagner, C.T., Lu, I.Y., Hoffman, M.H., Sun, W.Q., Trent, J.D., Connor, J. J. Biol. Chem. (2004) [Pubmed]
  28. Molecular chaperones and the centrosome. A role for TCP-1 in microtubule nucleation. Brown, C.R., Doxsey, S.J., Hong-Brown, L.Q., Martin, R.L., Welch, W.J. J. Biol. Chem. (1996) [Pubmed]
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