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Plasma Membrane Domain Patterning and Self-Reinforcing Polarity in Arabidopsis
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SYSNO ASEP 0521442 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Plasma 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 Title Developmental Cell. - : Cell Press - ISSN 1534-5807
Roč. 52, č. 2 (2020), s. 223-235Number of pages 13 s. Language eng - English Country US - United States Keywords Arabidopsis ; DRP1A ; PIP5K1 Subject RIV ED - Physiology OECD category Cell biology R&D Projects EF16_013/0001775 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support UEB-Q - RVO:61389030 UT WOS 000509725500011 EID SCOPUS 85078186775 DOI https://doi.org/10.1016/j.devcel.2019.11.015 Annotation Cell 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. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2020 Electronic address http://dx.doi.org/10.1016/j.devcel.2019.11.015
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