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The phosphomimetic mutation of an evolutionarily conserved serine residue affects the signaling properties of Rho of plants (ROPs)

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    SYSNO ASEP0367374
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleThe phosphomimetic mutation of an evolutionarily conserved serine residue affects the signaling properties of Rho of plants (ROPs)
    Author(s) Fodor-Dunai, C. (HU)
    Fricke, I. (DE)
    Potocký, Martin (UEB-Q) RID, ORCID
    Dorjgotov, D. (HU)
    Domoki, M. (DE)
    Jurca, M. E. (DE)
    Oetvoes, K. (HU)
    Žárský, Viktor (UEB-Q) RID, ORCID
    Berken, A. (DE)
    Feher, A. (HU)
    Source TitlePlant Journal. - : Wiley - ISSN 0960-7412
    Roč. 66, č. 4 (2011), s. 669-679
    Number of pages11 s.
    Languageeng - English
    CountryGB - United Kingdom
    KeywordsRho GTPase ; plant-specific ROP nucleotide exchanger ; ROP guanine nucleotide exchange factor
    Subject RIVEB - Genetics ; Molecular Biology
    R&D ProjectsGP522/09/P299 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z50380511 - UEB-Q (2005-2011)
    UT WOS000290456400009
    DOI10.1111/j.1365-313X.2011.04528.x
    AnnotationPlant ROP proteins form a unique subgroup of Rho-type small G-proteins. Here we demonstrate that the phosphomimetic mutation of a serine conserved in all Rho proteins affects ROP signaling. We found that the S74E mutation prevented the binding of Medicago ROP6 to its upstream activator, PRONE-domain-containing RopGEF protein and abolished the PRONE-mediated nucleotide exchange in vitro. Structural modeling supported the hypothesis that phosphorylation of the S74 residue interferes with the binding of the PRONE-domain to the adjacent R76 residue which is critical in ROP-PRONE interaction. Moreover, we show that the capability of S74E mutant to activate the RRK1 kinase was reduced. This correlates with the morphology of tobacco pollen tubes expressing mutant forms of YFP:ROP6. The S74E mutation had no influence on pollen tube morphology. The presented data suggest that the phosphorylation of the serine corresponding to S74 in ROP6 is a general principle for regulating ROP signaling.
    WorkplaceInstitute of Experimental Botany
    ContactDavid Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469
    Year of Publishing2012
Number of the records: 1  

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