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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 ASEP 0314785 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Extracellular Signal-Regulated Kinase 2 (ERK2) Phosphorylation Sites and Docking Domain on the Nuclear Pore Complex Protein Tpr Cooperatively Regulate ERK2-Tpr Interaction Title Místa 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 Title Molecular and Cellular Biology. - : American Society for Microbiology - ISSN 0270-7306
Roč. 28, č. 22 (2008), s. 6954-6966Number of pages 13 s. Language eng - English Country US - United States Keywords erk ; docking domain ; cell growth Subject RIV EE - Microbiology, Virology R&D Projects IAA500200716 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000260367900018 DOI https://doi.org/10.1128/MCB.00925-08 Annotation The 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 Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2009
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