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Extracellular Signal-Regulated Kinase 2 (ERK2) Phosphorylation Sites and Docking Domain on the Nuclear Pore Complex Protein Tpr Cooperatively Regulate ERK2-Tpr Interaction

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    SYSNO ASEP0314785
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleExtracellular Signal-Regulated Kinase 2 (ERK2) Phosphorylation Sites and Docking Domain on the Nuclear Pore Complex Protein Tpr Cooperatively Regulate ERK2-Tpr Interaction
    TitleMísta fosforylovaná mimobuněčným signálem regulovanou kinázou 2 (ERK2) a „Docking“ doména v proteinu Tpr complexu jaderného póru kooperativně regulují interakci ERK2 s Tpr
    Author(s) Vomastek, Tomáš (MBU-M) RID, ORCID
    Iwanicky, M. P. (US)
    Burack, W. R. (US)
    Tiwari, D. (IN)
    Kumar, D. (IN)
    Parsons, J. T. (US)
    Weber, M. J. (US)
    Nandicoori, V. K. (IN)
    Source TitleMolecular and Cellular Biology. - : American Society for Microbiology - ISSN 0270-7306
    Roč. 28, č. 22 (2008), s. 6954-6966
    Number of pages13 s.
    Languageeng - English
    CountryUS - United States
    Keywordserk ; docking domain ; cell growth
    Subject RIVEE - Microbiology, Virology
    R&D ProjectsIAA500200716 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    CEZAV0Z50200510 - MBU-M (2005-2011)
    UT WOS000260367900018
    DOI https://doi.org/10.1128/MCB.00925-08
    AnnotationThe ERK cascade is activated in response to a broad spectrum of extracellular signals and regulates many cellular responses, including cell growth, cell differentiation and cell motility. Identifying ERK substrates and understanding how those substrates alter cellular functions is central to understanding how these ubiquitously activated enzymes generate diverse biological responses. We identified the nuclear pore complex protein Tpr as new substrate and binding partner for ERK2. We mapped sites on Tpr for ERK2 phosphorylation and binding and demonstrated their functional interaction. The data provide direct evidence that a component of the nuclear pore complex is a bona fide substrate of ERK2 in vivo and that activated ERK2 stably associates with this substrate after phosphorylation
    WorkplaceInstitute of Microbiology
    ContactEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Year of Publishing2009
Number of the records: 1  

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