First published online January 12, 2006
Journal of Cell Science 119, 202e (2006)
© The Company of Biologists Limited
Chaperoning yeast into mitosis
Molecular chaperones play essential roles in many aspects of cell function by ensuring that their client proteins fold properly and/or assemble into oligomeric structures. The clients of the molecular chaperone Cdc37 are generally protein kinases, and many of these are important for cell proliferation. Emma Turnbull, Ina Martin and Peter Fantes now report that Cdc2 – the pivotal cyclin-dependent kinase controlling the cell cycle – is a client of Cdc37 in fission yeast (see p. 292). They show that, at the restrictive temperature, Cdc37 function is rapidly lost in four temperature-sensitive mutants of cdc37 (cdc37ts), all of which arrest in G2 phase within one cell cycle. Cdc2 activity, which normally regulates entry into mitosis, is also rapidly reduced at the restrictive temperature in two of these mutants and the authors show that this loss of activity results from the reduced ability of Cdc2 to bind its mitotic cyclin Cdc13. They conclude that, by interacting with Cdc2, Cdc37 aids the assembly of the Cdc2-Cdc13 complexes that are needed for cell-cycle progression.
Related articles in JCS:
- Activity of Cdc2 and its interaction with the cyclin Cdc13 depend on the molecular chaperone Cdc37 in Schizosaccharomyces pombe
- Emma L. Turnbull, Ina V. Martin, and Peter A. Fantes
JCS 2006 119: 292-302.
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