Discovery - University of Dundee - Online Publications

Library & Learning Centre

Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast

Standard

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 journalArticle

Harvard

Alexandru, G, Uhlmann, F, Mechtler, K, Poupart, M-A & Nasmyth, K 2001, 'Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast' Cell, vol 105, no. 4, pp. 459-472., 10.1016/S0092-8674(01)00362-2

APA

Alexandru, G., Uhlmann, F., Mechtler, K., Poupart, M-A., & Nasmyth, K. (2001). Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast. Cell, 105(4), 459-472. 10.1016/S0092-8674(01)00362-2

Vancouver

Alexandru G, Uhlmann F, Mechtler K, Poupart M-A, Nasmyth K. Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast. Cell. 2001;105(4):459-472. Available from: 10.1016/S0092-8674(01)00362-2

Author

Alexandru, Gabriela; Uhlmann, Frank; Mechtler, Karl; Poupart, Marc-André ; Nasmyth, Kim / Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast.

In: Cell, Vol. 105, No. 4, 2001, p. 459-472.

Research output: Contribution to journalArticle

Bibtex - Download

@article{08531c59fb2042f9be5012ec19a7e971,
title = "Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast",
author = "Gabriela Alexandru and Frank Uhlmann and Karl Mechtler and Marc-André Poupart and Kim Nasmyth",
year = "2001",
doi = "10.1016/S0092-8674(01)00362-2",
volume = "105",
number = "4",
pages = "459--472",
journal = "Cell",
issn = "0092-8674",

}

RIS (suitable for import to EndNote) - Download

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 -

Documents

Library & Learning Centre

Contact | Accessibility | Policy