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Title

APCste9/srw1 promotes degradation of mitotic cyclins in G1 and is inhibited by cdc2 phosphorylation

AuthorsBlanco, Miguel A.; Sánchez-Díaz, Alberto ; Prada, José M. de; Moreno, Sergio
Issue Date2000
PublisherNature Publishing Group
CitationEMBO Journal 19(15): 3945-3955 (2000)
AbstractFission yeast ste9/srw1 is a WD-repeat protein highly homologous to budding yeast Hct1/Cdh1 and Drosophila Fizzy-related that are involved in activating APC/C (anaphase-promoting complex/cyclosome). We show that ApC(ste9/srw1) specifically promotes the degradation of mitotic cyclins cdc13 and cig1 but not the S-phase cyclin cig2. APC(ste9/srw1) is not necessary for the proteolysis of cdc13 and cig1 that occurs at the metaphase-anaphase transition but it is absolutely required for their degradation in G1. Therefore, we propose that the main role of APC(ste9/srw1) is to promote degradation of mitotic cyclins when cells need to delay or arrest the cell cycle in G1. We also show that ste9/srw1 is negatively regulated by cdc2-dependent protein phosphorylation. In G1, when cdc2-cyclin kinase activity is low, unphosphorylated ste9/srw1 interacts with APC/C. In the rest of the cell cycle, phosphorylation of ste9/srw1 by cdc2-cyclin complexes both triggers proteolysis of ste9/srw1 and causes its dissociation from the APC/C. This mechanism provides a molecular switch to prevent inactivation of cdc2 in G2 and early mitosis and to allow its inactivation in G1.
URIhttp://hdl.handle.net/10261/65790
DOI10.1093/emboj/19.15.3945
Identifiersdoi: 10.1093/emboj/19.15.3945
issn: 0261-4189
e-issn: 1460-2075
Appears in Collections:(IMB) Artículos
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