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
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DOI - Digital Object Identifier
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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
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Czech description
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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
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Result continuities
Project
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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
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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
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UT code for WoS article
000269432600007
EID of the result in the Scopus database
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