Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1994 Mar 1;124(5):783–793. doi: 10.1083/jcb.124.5.783

PCM-1, A 228-kD centrosome autoantigen with a distinct cell cycle distribution

PMCID: PMC2119948  PMID: 8120099

Abstract

We report the identification and primary sequence of PCM-1, a 228-kD centrosomal protein that exhibits a distinct cell cycle-dependent association with the centrosome complex. Immunofluorescence microscopy using antibodies against recombinant PCM-1 demonstrated that PCM-1 is tightly associated with the centrosome complex through G1, S, and a portion of G2. However, late in G2, as cells prepare for mitosis, PCM-1 dissociates from the centrosome and then remains dispersed throughout the cell during mitosis before re-associating with the centrosomes in the G1 phase progeny cells. These results demonstrate that the pericentriolar material is a dynamic substance whose composition can fluctuate during the cell cycle.

Full Text

The Full Text of this article is available as a PDF (2.8 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Balczon R. D., Brinkley B. R. Tubulin interaction with kinetochore proteins: analysis by in vitro assembly and chemical cross-linking. J Cell Biol. 1987 Aug;105(2):855–862. doi: 10.1083/jcb.105.2.855. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Balczon R., West K. The identification of mammalian centrosomal antigens using human autoimmune anticentrosome antisera. Cell Motil Cytoskeleton. 1991;20(2):121–135. doi: 10.1002/cm.970200205. [DOI] [PubMed] [Google Scholar]
  3. Baron A. T., Salisbury J. L. Identification and localization of a novel, cytoskeletal, centrosome-associated protein in PtK2 cells. J Cell Biol. 1988 Dec;107(6 Pt 2):2669–2678. doi: 10.1083/jcb.107.6.2669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brinkley B. R. Microtubule organizing centers. Annu Rev Cell Biol. 1985;1:145–172. doi: 10.1146/annurev.cb.01.110185.001045. [DOI] [PubMed] [Google Scholar]
  5. Calarco-Gillam P. D., Siebert M. C., Hubble R., Mitchison T., Kirschner M. Centrosome development in early mouse embryos as defined by an autoantibody against pericentriolar material. Cell. 1983 Dec;35(3 Pt 2):621–629. doi: 10.1016/0092-8674(83)90094-6. [DOI] [PubMed] [Google Scholar]
  6. Gould R. R., Borisy G. G. The pericentriolar material in Chinese hamster ovary cells nucleates microtubule formation. J Cell Biol. 1977 Jun;73(3):601–615. doi: 10.1083/jcb.73.3.601. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kalt A., Schliwa M. Molecular components of the centrosome. Trends Cell Biol. 1993 Apr;3(4):118–128. doi: 10.1016/0962-8924(93)90174-y. [DOI] [PubMed] [Google Scholar]
  8. Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell. 1986 Jan 31;44(2):283–292. doi: 10.1016/0092-8674(86)90762-2. [DOI] [PubMed] [Google Scholar]
  9. Osborn T. G., Patel N. J., Ross S. C., Bauer N. E. Antinuclear antibody staining only centrioles in a patient with scleroderma. N Engl J Med. 1982 Jul 22;307(4):253–254. doi: 10.1056/NEJM198207223070421. [DOI] [PubMed] [Google Scholar]
  10. Rao P. N., Zhao J. Y., Ganju R. K., Ashorn C. L. Monoclonal antibody against the centrosome. J Cell Sci. 1989 May;93(Pt 1):63–69. doi: 10.1242/jcs.93.1.63. [DOI] [PubMed] [Google Scholar]
  11. Robbins E., Jentzsch G., Micali A. The centriole cycle in synchronized HeLa cells. J Cell Biol. 1968 Feb;36(2):329–339. doi: 10.1083/jcb.36.2.329. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Rose M. D., Biggins S., Satterwhite L. L. Unravelling the tangled web at the microtubule-organizing center. Curr Opin Cell Biol. 1993 Feb;5(1):105–115. doi: 10.1016/s0955-0674(05)80015-8. [DOI] [PubMed] [Google Scholar]
  13. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Saraste M., Sibbald P. R., Wittinghofer A. The P-loop--a common motif in ATP- and GTP-binding proteins. Trends Biochem Sci. 1990 Nov;15(11):430–434. doi: 10.1016/0968-0004(90)90281-f. [DOI] [PubMed] [Google Scholar]
  15. Schatten H., Schatten G., Mazia D., Balczon R., Simerly C. Behavior of centrosomes during fertilization and cell division in mouse oocytes and in sea urchin eggs. Proc Natl Acad Sci U S A. 1986 Jan;83(1):105–109. doi: 10.1073/pnas.83.1.105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Sellitto C., Kuriyama R. Distribution of a matrix component of the midbody during the cell cycle in Chinese hamster ovary cells. J Cell Biol. 1988 Feb;106(2):431–439. doi: 10.1083/jcb.106.2.431. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Szollosi D., Calarco P., Donahue R. P. Absence of centrioles in the first and second meiotic spindles of mouse oocytes. J Cell Sci. 1972 Sep;11(2):521–541. doi: 10.1242/jcs.11.2.521. [DOI] [PubMed] [Google Scholar]
  18. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Verde F., Labbé J. C., Dorée M., Karsenti E. Regulation of microtubule dynamics by cdc2 protein kinase in cell-free extracts of Xenopus eggs. Nature. 1990 Jan 18;343(6255):233–238. doi: 10.1038/343233a0. [DOI] [PubMed] [Google Scholar]
  20. Walker J. E., Saraste M., Runswick M. J., Gay N. J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982;1(8):945–951. doi: 10.1002/j.1460-2075.1982.tb01276.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Young R. A., Davis R. W. Efficient isolation of genes by using antibody probes. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1194–1198. doi: 10.1073/pnas.80.5.1194. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Zimmer W. E., Schloss J. A., Silflow C. D., Youngblom J., Watterson D. M. Structural organization, DNA sequence, and expression of the calmodulin gene. J Biol Chem. 1988 Dec 25;263(36):19370–19383. [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES