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Structure and function of the PP2A-shugoshin interaction

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985904%3A_____%2F09%3A00328951" target="_blank" >RIV/67985904:_____/09:00328951 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structure and function of the PP2A-shugoshin interaction

  • Original language description

    Accurate chromosome segregation during mitosis and meiosis depends od shugoshin proteins that prevent precocious dissociatin of cohesin from centromeres. Shugoshins associate with PP2A, which is trought to dephosphorylate cohesin and thereby prevent cleavage by separase during meiosis I. A crystal structure of a complex between a fragment of human Sgo1 and an AB.C PP1A holoenzyme reveals that Sgo1 forms a homodimerization is a prerequisite for PP2A binding. While hSgo1 interacts only with the AB.C holoenzymes, its relative, Sgo2 interacts with all PP2A forms and may thus lead to dephosphorylation of distinct substrates. Mutant shugoshin proteins defective id the binding of PP2A cannot protect centromeric cohesin from separase during meiosis I or support the spindle assembly checkpoint in yeast. Finally, we provide evidence that PP2A´s recruitment to chromosomes may be sufficied to protect cohesin from separase in mammalian oocytes.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2009

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Molecular Cell

  • ISSN

    1097-2765

  • e-ISSN

  • Volume of the periodical

    35

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    16

  • Pages from-to

  • UT code for WoS article

    000269432600007

  • EID of the result in the Scopus database