par Bamps, Sophie;Hermand, Damien;Tafforeau, Lionel ;Makela, Tomi T.P.;Vandenhaute, Jean
Référence XXth international conference on yeast genetics and molecular biology(Prague, Tchéquie), yeast, Vol. 19, Ed. 3, page (282)
Publication Publié, 2002-08
Publication dans des actes
Résumé : CDK activation requires activating phosphorylation of a conserved residue in the T-loop by the CAK (CDK-activating kinase). In both fission yeast and higher eukaryotes, CAK is a trimeric complex composed of Mcs6-Mcs2-Pmh1 or its homologue [1–3]. Two hybrid assays revealed interaction of both Mcs2 and Pmh1 with Shp1, a subunit of the SCF ubiquitin ligase. This prompted us to test the stability of these CAK regulators. Although the steady-state level of Mcs2 does not seem to change during the cell cycle [4], we show that it is strongly correlated to Mcs6 kinase activity and that Mcs2 was nearly undetectable when Mcs6 was strongly overexpressed. Interestingly, this effect is reversed by a mutation in shp1. Taken together, these results suggest a putative regulation of Mcs2 by Mcs6 phosphorylation and SCF ubiquitin ligase complex. Thus, the hypothesis is under investigation. (1) Hermand D, Westerling T. Pihlak A, et al. 2001. EMBO J 20: 82–90. (2) Hermand D, Pihlak A, Westerling T, et al. 1998. EMBO J 17: 7230–7238. (3) Kaldis P. 1999. Cell Mol Life Sci 55: 284–296. (4) Molz L, Beach D. 1993. EMBO J 12: 1723–1732.