Protein phosphatase 1 is essential for Greatwall inactivation at mitotic exit


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HEIM, Andreas, Anja KONIETZNY, Thomas U. MAYER, 2015. Protein phosphatase 1 is essential for Greatwall inactivation at mitotic exit. In: EMBO Reports. 16(11), pp. 1501-1510. ISSN 1469-221X. eISSN 1469-3178. Available under: doi: 10.15252/embr.201540876

@article{Heim2015Prote-32213, title={Protein phosphatase 1 is essential for Greatwall inactivation at mitotic exit}, year={2015}, doi={10.15252/embr.201540876}, number={11}, volume={16}, issn={1469-221X}, journal={EMBO Reports}, pages={1501--1510}, author={Heim, Andreas and Konietzny, Anja and Mayer, Thomas U.} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:contributor>Konietzny, Anja</dc:contributor> <dc:contributor>Mayer, Thomas U.</dc:contributor> <dc:creator>Konietzny, Anja</dc:creator> <dcterms:issued>2015</dcterms:issued> <dc:contributor>Heim, Andreas</dc:contributor> <dcterms:available rdf:datatype="">2015-11-23T12:30:18Z</dcterms:available> <dcterms:title>Protein phosphatase 1 is essential for Greatwall inactivation at mitotic exit</dcterms:title> <dcterms:hasPart rdf:resource=""/> <dc:creator>Heim, Andreas</dc:creator> <dc:date rdf:datatype="">2015-11-23T12:30:18Z</dc:date> <dspace:hasBitstream rdf:resource=""/> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:creator>Mayer, Thomas U.</dc:creator> <dcterms:isPartOf rdf:resource=""/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <bibo:uri rdf:resource=""/> <dcterms:abstract xml:lang="eng">Entry into mitosis is mediated by the phosphorylation of key cell cycle regulators by cyclin-dependent kinase 1 (Cdk1). In Xenopus embryos, the M-phase-promoting activity of Cdk1 is antagonized by protein phosphatase PP2A-B55. Hence, to ensure robust cell cycle transitions, Cdk1 and PP2A-B55 must be regulated so that their activities are mutually exclusive. The mechanism underlying PP2A-B55 inactivation at mitotic entry is well understood: Cdk1-activated Greatwall (Gwl) kinase phosphorylates Ensa/Arpp19, thereby enabling them to bind to and inhibit PP2A-B55. However, the re-activation of PP2A-B55 during mitotic exit, which is essential for cell cycle progression, is less well understood. Here, we identify protein phosphatase PP1 as an essential component of the PP2A-B55 re-activation pathway in Xenopus embryo extracts. PP1 initiates the re-activation of PP2A-B55 by dephosphorylating Gwl. We provide evidence that PP1 targets the auto-phosphorylation site of Gwl, resulting in efficient Gwl inactivation. This step is necessary to facilitate subsequent complete dephosphorylation of Gwl by PP2A-B55. Thus, by identifying PP1 as the phosphatase initiating Gwl inactivation, our study provides the molecular explanation for how Cdk1 inactivation is coupled to PP2A-B55 re-activation at mitotic exit.</dcterms:abstract> <dc:rights>terms-of-use</dc:rights> <dspace:isPartOfCollection rdf:resource=""/> <dcterms:rights rdf:resource=""/> <dc:language>eng</dc:language> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 23.11.2015 (Informationen über die Zugriffsstatistik)

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