Abstract
ENTRY of a cell into mitosis induces a series of structural and functional changes including arrest of intracellular transport1–4. Knowledge of how the mitotic cycle is driven progressed substantially with the identification of the p34cdc2 protein kinase as a subunit of maturation-promoting factor5–7, the universal regulating component of the mitotic cycle8. Activation of the kinase at the onset of mitosis9 is thought to trigger the important mitotic events by phosphorylating key proteins10. Small guanine nucleo-tide-binding proteins have been implicated in regulating transport pathways. For instance, two small Ras-related GTP-binding proteins, Sec4p and Yptlp, control distinct stages of the secretory pathway in budding yeast11–15. The GTP-binding proteins of the Rab family in rats and humans16,17 display strong homologies with Sec4p and Yptlp, and might therefore also be involved in regulating intracellular transport. Indeed, distinct Rab proteins are located in the exocytotic and endocytotic compartments18–21. Interruption of vesicular transport during mitosis might involve modification of these proteins. We now present biochemical evidence for a mitosis-specific p34cdc2 phosphorylation of RablAp and Rab4p. By contrast, Rab2p and Rab6p are not phosphorylated. We also show that the distribution of RablAp and Rab4p between cytosolic and membrane-bound forms is different in interphase and mitotic cells. This may provide a clue to the mechanism by which phosphorylation could affect membrane traffic during mitosis.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Rent or buy this article
Prices vary by article type
from$1.95
to$39.95
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Warren, G., Featherstone, C., Griffiths, G. & Burke, B. J. Cell Biol. 97, 1623–1628 (1983).
Featherstone, C., Griffiths, G. & Warren, G. J. Cell Biol. 101, 2036–2046 (1985).
Warren, G. Trends biochem. Sci. 10, 439–443 (1985).
Warren, G. Nature 342, 857–858 (1989).
Dunphy, W. G., Brizuela, L., Beach, D. & Newport, J. Cell 54, 423–431 (1988).
Gautier, J., Norbury, C., Lohka, M., Nurse, P. & Maller, J. Cell 54, 433–439 (1988).
Labbé, J.-C., Lee, M., Nurse, P., Picard, A. & Dorée, M. Nature 335, 251–254 (1988).
Nurse, P. Nature 344, 503–508 (1990).
Draetta, J. & Beach, D. Cell 54, 17–26 (1988).
Moreno, S. & Nurse, P. Cell 61, 549–551 (1990).
Salminen, A. & Novick, P. Cell 49, 527–538 (1987).
Goud, B., Salminen, A., Walworth, N. & Novick, P. Cell 53, 753–768 (1988).
Schmitt, H. D., Wagner, P., Pfaff, E. & Gallwitz, D. Cell 47, 401–412 (1986).
Segev, N., Mulholland, J. & Bostein, D. Cell 52, 915–924 (1988).
Bacon, R. A., Salminen, A., Ruohola, H., Novick, P. & Ferro-Novick, S. J. Cell Biol. 109, 1015–1022 (1989).
Touchot, N., Chardin, P. & Tavitian, A. Proc. natn. Acad. Sci. U.S.A. 84, 8210–8214 (1987).
Zahraoui, A., Touchot, N., Chardin, P. & Tavitian, A. J. biol. Chem. 264, 12394–12401 (1989).
Goud, B., Zahraoui, A., Tavitian, A. & Saraste, J. Nature 345, 553–556 (1990).
Chavrier, P., Parton, R. G., Hauri, H. P., Simons, K. & Zerial, M. Cell 62, 317–329 (1990).
Mollard, G. F. et al. Proc. natn. Acad. Sci. U.S.A. 87, 1988–1992 (1990).
Darchen, F. et al. Proc. natn. Acad. Sci. U.S.A. 87, 5692–5696 (1990).
Langan, T. A. J. biol. Chem. 257, 14835–14846 (1982).
Walworth, N., Goud, B., Kabcenell, A. & Novick, P. EMBO J. 8, 1685–1693 (1989).
Molenaar, C. M. T., Prange, R. & Gallwitz, D. EMBO J. 7, 1167–1177 (1988).
Willumsen, B. E., Christensen, A., Hubbert, N. L., Papageorge, A. G. & Lowy, D. R. Nature 310, 583–586 (1984).
Fischer v. Mollard, G. et al. Proc. natn. Acad. Sci. U.S.A. 87, 1988–1992 (1990).
Haubruck, H., Prange, R., Vorgias, C. & Gallwitz, D. EMBO J. 8, 1427–1432 (1989).
Baker, D., Wuestehube, L., Scheckman, R., Bostein, D. & Segev, N. Proc. natn. Acad. Sci. U.S.A. 87, 355–359 (1990).
Van der Sluijs, P. et al. Proc. natn. Acad. Sci. U.S.A. (in the press).
Tuomikoski, T., Felix, M. A., Dorée, M. & Gruenberg, J. Nature 342, 942–945 (1989).
Bourne, H. Cell 53, 669–671 (1988).
Maridonneau-Parini, I., Yang, C. Z., Bornens, M. & Goud, B. J. clin. Invest. 87, 901–907 (1991).
Bailly, E., Dorée, M., Nurse, P. & Bornens, M. EMBO J. 8, 3985–3995 (1989).
Bordier, C. J. biol. Chem. 256, 1604–1607 (1981).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Bailly, E., McCaffrey, M., Touchot, N. et al. Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2. Nature 350, 715–718 (1991). https://doi.org/10.1038/350715a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/350715a0
This article is cited by
-
Targeting small GTPases: emerging grasps on previously untamable targets, pioneered by KRAS
Signal Transduction and Targeted Therapy (2023)
-
Rab1 in cell signaling, cancer and other diseases
Oncogene (2016)
-
A Hypothetical Model of Cargo-Selective Rab Recruitment During Organelle Maturation
Cell Biochemistry and Biophysics (2012)
-
Alcohol induces Golgi fragmentation in differentiated PC12 cells by deregulating Rab1-dependent ER-to-Golgi transport
Histochemistry and Cell Biology (2012)
-
NME genes in epithelial morphogenesis
Naunyn-Schmiedeberg's Archives of Pharmacology (2011)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.