Literature DB >> 17030123

Mitotic phosphatases: no longer silent partners.

Laura Trinkle-Mulcahy1, Angus I Lamond.   

Abstract

Recent work has highlighted the important role played by protein phosphatase complexes in the regulation of mitosis from yeast to mammals. There have been important advances in defining the roles of the protein serine/threonine phosphatases PP1 and PP2A and the dual specificity protein tyrosine phosphatases CDC25 and Cdc14. Three independent studies defined a regulatory role for PP2A in the control of sister chromatid cohesion, involving a direct interaction with shugoshin. A chromatin targeting subunit has been identified for PP1 and the complex shown to play an essential role in chromosome segregation. Key regulatory residues within CDC25 have been mapped and its activity tied both to the initial activation of cyclin-dependent kinases at the centrosome and to DNA damage checkpoints. Novel roles have been defined for Cdc14, including regulation of rDNA and telomere segregation and participation in spindle assembly. These exciting advances show that protein phosphatases are not merely silent partners to kinases in regulating the control of cell division.

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Year:  2006        PMID: 17030123     DOI: 10.1016/j.ceb.2006.09.001

Source DB:  PubMed          Journal:  Curr Opin Cell Biol        ISSN: 0955-0674            Impact factor:   8.382


  48 in total

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3.  Mitotic phosphorylation: breaking the balance of power by a tactical retreat.

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4.  Regulated activity of PP2A-B55 delta is crucial for controlling entry into and exit from mitosis in Xenopus egg extracts.

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8.  Temporal changes in Hec1 phosphorylation control kinetochore-microtubule attachment stability during mitosis.

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9.  Evolutionary radiation pattern of novel protein phosphatases revealed by analysis of protein data from the completely sequenced genomes of humans, green algae, and higher plants.

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Review 10.  Family cancer syndromes: inherited deficiencies in systems for the maintenance of genomic integrity.

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