Number of the records: 1  

Plasma Membrane Domain Patterning and Self-Reinforcing Polarity in Arabidopsis

  1. 1.
    SYSNO ASEP0521442
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitlePlasma Membrane Domain Patterning and Self-Reinforcing Polarity in Arabidopsis
    Author(s) Marhava, P. (CH)
    Aliaga Fandino, A.C. (CH)
    Koh, S.W.H. (CH)
    Jelínková, Adriana (UEB-Q) RID, ORCID
    Kolb, M. (DE)
    Janacek, D. P. (DE)
    Breda, A.S. (NL)
    Cattaneo, P. (CH)
    Hammes, U. Z. (DE)
    Petrášek, Jan (UEB-Q) RID, ORCID
    Hardtke, C.S. (CH)
    Source TitleDevelopmental Cell. - : Cell Press - ISSN 1534-5807
    Roč. 52, č. 2 (2020), s. 223-235
    Number of pages13 s.
    Languageeng - English
    CountryUS - United States
    KeywordsArabidopsis ; DRP1A ; PIP5K1
    Subject RIVED - Physiology
    OECD categoryCell biology
    R&D ProjectsEF16_013/0001775 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Method of publishingOpen access
    Institutional supportUEB-Q - RVO:61389030
    UT WOS000509725500011
    EID SCOPUS85078186775
    DOI10.1016/j.devcel.2019.11.015
    AnnotationCell polarity is a key feature in the development of multicellular organisms. For instance, asymmetrically localized plasma-membrane-integral PIN-FORMED (PIN) proteins direct transcellular fluxes of the phytohormone auxin that govern plant development. Fine-tuned auxin flux is important for root protophloem sieve element differentiation and requires the interacting plasma-membrane-associated BREVIS RADIX (BRX) and PROTEIN KINASE ASSOCIATED WITH BRX (PAX) proteins. We observed donut-like polar PIN localization in developing sieve elements that depends on complementary, muffin-like polar localization of BRX and PAX. Plasma membrane association and polarity of PAX, and indirectly BRX, largely depends on phosphatidylinositol-4,5-bisphosphate. Consistently, mutants in phosphatidylinositol-4-phosphate 5-kinases (PIP5Ks) display protophloem differentiation defects similar to brx mutants. The same PIP5Ks are in complex with BRX and display muffin-like polar localization. Our data suggest that the BRX-PAX module recruits PIP5Ks to reinforce PAX polarity and thereby the polarity of all three proteins, which is required to maintain a local PIN minimum.
    WorkplaceInstitute of Experimental Botany
    ContactDavid Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469
    Year of Publishing2020
    Electronic addresshttp://dx.doi.org/10.1016/j.devcel.2019.11.015
Number of the records: 1  

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