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Role of Hcn1 and its phosphorylation in fission yeast anaphase-promoting complex/cyclosome function.

Yoon HJ, Feoktistova A, Chen JS, Jennings JL, Link AJ, Gould KL
J Biol Chem. 2006 281 (43): 32284-93

PMID: 16950791 · DOI:10.1074/jbc.M603867200

The anaphase-promoting complex/cyclosome (APC/C) is a conserved multisubunit ubiquitin ligase required for the degradation of key cell cycle regulators. The APC/C becomes active at the metaphase/anaphase transition and remains active during G(1) phase. One mechanism linked to activation of the APC/C is phosphorylation. Although many sites of mitotic phosphorylation have been identified in core components of the APC/C, the consequence of any individual phosphorylation event has not been elucidated in vivo. In this study, we show that Hcn1 is an essential core component of the fission yeast APC/C and is critical for maintaining complex integrity. Moreover, Hcn1 is a phosphoprotein in vivo. Phosphorylation of Hcn1 occurs at a single Cdk1 site in vitro and in vivo. Mutation of this site to alanine, but not aspartic acid, compromises APC/C function and leads to a specific defect in the completion of cell division.

MeSH Terms (13)

Alanine Amino Acid Substitution Anaphase-Promoting Complex-Cyclosome Cell Cycle Proteins Fungal Proteins G2 Phase Gene Deletion Green Fluorescent Proteins Phosphorylation Repressor Proteins Schizosaccharomyces Schizosaccharomyces pombe Proteins Ubiquitin-Protein Ligase Complexes

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