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Gene Review

PCM1  -  pericentriolar material 1

Homo sapiens

Synonyms: PCM-1, PTC4, Pericentriolar material 1 protein, hPCM-1
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Disease relevance of PCM1


High impact information on PCM1

  • Here we show that BBS4 localizes to the centriolar satellites of centrosomes and basal bodies of primary cilia, where it functions as an adaptor of the p150(glued) subunit of the dynein transport machinery to recruit PCM1 (pericentriolar material 1 protein) and its associated cargo to the satellites [6].
  • A polyclonal antibody raised against the protein was able to 'supershift' the native MeCP11 complex from HeLa cells, indicating that PCM1 is a component of mammalian MeCP1 [7].
  • Electron microscopic immunocytochemistry localized this antigen in dense pericentriolar material (PCM) surrounding the centrioles [8].
  • The centrosome consists of a pair of centrioles and a surrounding matrix of pericentriolar material that anchors microtubule nucleation sites and consequently determines the number and organization of microtubules in interphase and mitotic cells [9].
  • Here, we identify a novel centrosomal substrate of Plk1, Kizuna (Kiz), depletion of which causes fragmentation and dissociation of the pericentriolar material from centrioles at prometaphase, resulting in multipolar spindles [10].
  • PCM1 has sense Alu elements in its 3'UTR region, making it susceptible to the regulation of other protein-coding or non-coding RNAs with antisense Alu elements [11].

Biological context of PCM1


Anatomical context of PCM1

  • In cells, BBS8 localizes to centrosomes and basal bodies and interacts with PCM1, a protein probably involved in ciliogenesis [17].
  • Immunodepletion of neither pericentrin-B nor PCM-1 from cellular extracts inhibited the ability of salt-stripped centrosomes to recover microtubule nucleation potential, demonstrating that neither protein plays a key role in microtubule nucleation processes [18].
  • By 24 h, centrioles have formed inside of already well-developed PCM clouds [19].
  • Immunohistochemistry, using an antibody specific for the C-terminal portion of PCM-1 showed that the protein level is drastically decreased and its subcellular localization is altered in thyroid tumor tissue with respect to normal thyroid [20].
  • In oocytes, the PCM was found not only at the poles of the barrel-shaped metaphase II spindle but also at many discrete loci around the cytoplasm near the cell cortex [21].

Associations of PCM1 with chemical compounds

  • The breakpoints were variable in both genes, but in all cases the chimeric mRNA is predicted to encode a protein that retains several of the predicted coiled-coil domains from PCM1 and the entire tyrosine kinase domain of JAK2 [14].
  • The polysaccharide fractions also existed in conformations including random coil (as in PCM0 and PCM1) and expanded chain (as in PCM3), and differed molecular mass [22].
  • Although clouds of PCM consistently form even when microtubules are completely disassembled by nocodazole, the centrioles are not assembled under these conditions [19].
  • Conversely, cells arrested at the G1/S boundary of the cell cycle maintained PCM-1 mRNA at artificially elevated levels, providing a possible molecular mechanism for explaining the multiple rounds of centrosome replication that occurred in CHO cells during prolonged hydroxyurea-induced arrest [23].
  • Stepwise solubilization of centrosomal structures using urea showed that high urea concentrations were required to solubilize centrosomal vinculin, suggesting tight association of vinculin with the pericentriolar material [24].

Other interactions of PCM1


Analytical, diagnostic and therapeutic context of PCM1


  1. PCM1-JAK2 fusion in myeloproliferative disorders and acute erythroid leukemia with t(8;9) translocation. Murati, A., Gelsi-Boyer, V., Adélaïde, J., Perot, C., Talmant, P., Giraudier, S., Lodé, L., Letessier, A., Delaval, B., Brunel, V., Imbert, M., Garand, R., Xerri, L., Birnbaum, D., Mozziconacci, M.J., Chaffanet, M. Leukemia (2005) [Pubmed]
  2. JAK the trigger. Mahon, F.X. Oncogene (2005) [Pubmed]
  3. A t(8;9) translocation with PCM1-JAK2 fusion in a patient with T-cell lymphoma. Adélaïde, J., Pérot, C., Gelsi-Boyer, V., Pautas, C., Murati, A., Copie-Bergman, C., Imbert, M., Chaffanet, M., Birnbaum, D., Mozziconacci, M.J. Leukemia (2006) [Pubmed]
  4. Five genes from chromosomal band 8p22 are significantly down-regulated in ovarian carcinoma: N33 and EFA6R have a potential impact on overall survival. Pils, D., Horak, P., Gleiss, A., Sax, C., Fabjani, G., Moebus, V.J., Zielinski, C., Reinthaller, A., Zeillinger, R., Krainer, M. Cancer (2005) [Pubmed]
  5. Centrosome amplification and the origin of chromosomal instability in breast cancer. Salisbury, J.L., D'Assoro, A.B., Lingle, W.L. Journal of mammary gland biology and neoplasia. (2004) [Pubmed]
  6. The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression. Kim, J.C., Badano, J.L., Sibold, S., Esmail, M.A., Hill, J., Hoskins, B.E., Leitch, C.C., Venner, K., Ansley, S.J., Ross, A.J., Leroux, M.R., Katsanis, N., Beales, P.L. Nat. Genet. (2004) [Pubmed]
  7. A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins. Cross, S.H., Meehan, R.R., Nan, X., Bird, A. Nat. Genet. (1997) [Pubmed]
  8. Centrosome development in early mouse embryos as defined by an autoantibody against pericentriolar material. Calarco-Gillam, P.D., Siebert, M.C., Hubble, R., Mitchison, T., Kirschner, M. Cell (1983) [Pubmed]
  9. Centrosome size is controlled by centriolar SAS-4. Salisbury, J.L. Trends Cell Biol. (2003) [Pubmed]
  10. The Plk1 target Kizuna stabilizes mitotic centrosomes to ensure spindle bipolarity. Oshimori, N., Ohsugi, M., Yamamoto, T. Nat. Cell Biol. (2006) [Pubmed]
  11. A gene expression restriction network mediated by sense and antisense Alu sequences located on protein-coding messenger RNAs. Liang, K.H., Yeh, C.T. BMC. Genomics. (2013) [Pubmed]
  12. The t(8;9)(p22;p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene. Bousquet, M., Quelen, C., De Mas, V., Duchayne, E., Roquefeuil, B., Delsol, G., Laurent, G., Dastugue, N., Brousset, P. Oncogene (2005) [Pubmed]
  13. Mapping of the human autoantigen pericentriolar material 1 (PCM1) gene to chromosome 8p21.3-p22. Ohata, H., Fujiwara, Y., Koyama, K., Nakamura, Y. Genomics (1994) [Pubmed]
  14. The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2. Reiter, A., Walz, C., Watmore, A., Schoch, C., Blau, I., Schlegelberger, B., Berger, U., Telford, N., Aruliah, S., Yin, J.A., Vanstraelen, D., Barker, H.F., Taylor, P.C., O'Driscoll, A., Benedetti, F., Rudolph, C., Kolb, H.J., Hochhaus, A., Hehlmann, R., Chase, A., Cross, N.C. Cancer Res. (2005) [Pubmed]
  15. Population distribution in North and Central America of PGM1 and Gc subtypes as determined by isoelectric focusing (IEF). Dykes, D.D., Crawford, M.H., Polesky, H.F. Am. J. Phys. Anthropol. (1983) [Pubmed]
  16. PCM-1, A 228-kD centrosome autoantigen with a distinct cell cycle distribution. Balczon, R., Bao, L., Zimmer, W.E. J. Cell Biol. (1994) [Pubmed]
  17. Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome. Ansley, S.J., Badano, J.L., Blacque, O.E., Hill, J., Hoskins, B.E., Leitch, C.C., Kim, J.C., Ross, A.J., Eichers, E.R., Teslovich, T.M., Mah, A.K., Johnsen, R.C., Cavender, J.C., Lewis, R.A., Leroux, M.R., Beales, P.L., Katsanis, N. Nature (2003) [Pubmed]
  18. Kendrin/pericentrin-B, a centrosome protein with homology to pericentrin that complexes with PCM-1. Li, Q., Hansen, D., Killilea, A., Joshi, H.C., Palazzo, R.E., Balczon, R. J. Cell. Sci. (2001) [Pubmed]
  19. De novo formation of centrosomes in vertebrate cells arrested during S phase. Khodjakov, A., Rieder, C.L., Sluder, G., Cassels, G., Sibon, O., Wang, C.L. J. Cell Biol. (2002) [Pubmed]
  20. RET/PCM-1: a novel fusion gene in papillary thyroid carcinoma. Corvi, R., Berger, N., Balczon, R., Romeo, G. Oncogene (2000) [Pubmed]
  21. Non-spindle microtubule organizing centers in metaphase II-arrested mouse oocytes. Maro, B., Howlett, S.K., Webb, M. J. Cell Biol. (1985) [Pubmed]
  22. Effect of culture media on the chemical and physical characteristics of polysaccharides isolated from Poria cocos mycelia. Jin, Y., Zhang, L., Chen, L., Chen, Y., Cheung, P.C., Chen, L. Carbohydr. Res. (2003) [Pubmed]
  23. Dissociation of centrosome replication events from cycles of DNA synthesis and mitotic division in hydroxyurea-arrested Chinese hamster ovary cells. Balczon, R., Bao, L., Zimmer, W.E., Brown, K., Zinkowski, R.P., Brinkley, B.R. J. Cell Biol. (1995) [Pubmed]
  24. Identification of vinculin as a pericentriolar component in mammalian cells. Chevrier, V., Paintrand, M., Koteliansky, V., Block, M.R., Job, D. Exp. Cell Res. (1995) [Pubmed]
  25. Dynamic recruitment of Nek2 kinase to the centrosome involves microtubules, PCM-1, and localized proteasomal degradation. Hames, R.S., Crookes, R.E., Straatman, K.R., Merdes, A., Hayes, M.J., Faragher, A.J., Fry, A.M. Mol. Biol. Cell (2005) [Pubmed]
  26. EVI5 is a novel centrosomal protein that binds to alpha- and gamma-tubulin. Faitar, S.L., Dabbeekeh, J.T., Ranalli, T.A., Cowell, J.K. Genomics (2005) [Pubmed]
  27. PPX, a novel protein serine/threonine phosphatase localized to centrosomes. Brewis, N.D., Street, A.J., Prescott, A.R., Cohen, P.T. EMBO J. (1993) [Pubmed]
  28. Receptor for hyaluronan-mediated motility correlates with centrosome abnormalities in multiple myeloma and maintains mitotic integrity. Maxwell, C.A., Keats, J.J., Belch, A.R., Pilarski, L.M., Reiman, T. Cancer Res. (2005) [Pubmed]
  29. Heat shock causes protein aggregation and reduced protein solubility at the centrosome and other cytoplasmic locations. Vidair, C.A., Huang, R.N., Doxsey, S.J. International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group. (1996) [Pubmed]
  30. Insoluble gamma-tubulin-containing structures are anchored to the apical network of intermediate filaments in polarized CACO-2 epithelial cells. Salas, P.J. J. Cell Biol. (1999) [Pubmed]
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