Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast. / Alexandru, Gabriela; Uhlmann, Frank; Mechtler, Karl; Poupart, Marc-André ; Nasmyth, Kim.
In: Cell, Vol. 105, No. 4, 2001, p. 459-472.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast
A1 - Alexandru,Gabriela
A1 - Uhlmann,Frank
A1 - Mechtler,Karl
A1 - Poupart,Marc-André
A1 - Nasmyth,Kim
AU - Alexandru,Gabriela
AU - Uhlmann,Frank
AU - Mechtler,Karl
AU - Poupart,Marc-André
AU - Nasmyth,Kim
PY - 2001
Y1 - 2001
N2 - <p>At the onset of anaphase, a caspase-related protease (separase) destroys the link between sister chromatids by cleaving the cohesin subunit Scc1. During most of the cell cycle, separase is kept inactive by binding to an inhibitory protein called securin. Separase activation requires proteolysis of securin, which is mediated by an ubiquitin protein ligase called the anaphase-promoting complex. Cells regulate anaphase entry by delaying securin ubiquitination until all chromosomes have attached to the mitotic spindle. Though no longer regulated by this mitotic surveillance mechanism, sister separation remains tightly cell cycle regulated in yeast mutants lacking securin. We show here that the Polo/Cdc5 kinase phosphorylates serine residues adjacent to Scc1 cleavage sites and strongly enhances their cleavage. Phosphorylation of separase recognition sites may be highly conserved and regulates sister chromatid separation independently of securin.</p>
AB - <p>At the onset of anaphase, a caspase-related protease (separase) destroys the link between sister chromatids by cleaving the cohesin subunit Scc1. During most of the cell cycle, separase is kept inactive by binding to an inhibitory protein called securin. Separase activation requires proteolysis of securin, which is mediated by an ubiquitin protein ligase called the anaphase-promoting complex. Cells regulate anaphase entry by delaying securin ubiquitination until all chromosomes have attached to the mitotic spindle. Though no longer regulated by this mitotic surveillance mechanism, sister separation remains tightly cell cycle regulated in yeast mutants lacking securin. We show here that the Polo/Cdc5 kinase phosphorylates serine residues adjacent to Scc1 cleavage sites and strongly enhances their cleavage. Phosphorylation of separase recognition sites may be highly conserved and regulates sister chromatid separation independently of securin.</p>
U2 - 10.1016/S0092-8674(01)00362-2
DO - 10.1016/S0092-8674(01)00362-2
M1 - Article
JO - Cell
JF - Cell
SN - 0092-8674
IS - 4
VL - 105
SP - 459
EP - 472
ER -