Plasma Membrane Domain Patterning and Self-Reinforcing Polarity in Arabidopsis

0521442 - ÚEB 2020 RIV US eng J - Článek v odborném periodiku
Marhava, P. - Aliaga Fandino, A.C. - Koh, S.W.H. - Jelínková, Adriana - Kolb, M. - Janacek, D. P. - Breda, A.S. - Cattaneo, P. - Hammes, U. Z. - Petrášek, Jan - Hardtke, C.S.
Plasma Membrane Domain Patterning and Self-Reinforcing Polarity in Arabidopsis.
Developmental Cell. Roč. 52, č. 2 (2020), s. 223-235. ISSN 1534-5807. E-ISSN 1878-1551
Grant CEP: GA MŠMT(CZ) EF16_013/0001775
Institucionální podpora: RVO:61389030
Klíčová slova: Arabidopsis * DRP1A * PIP5K1
Obor OECD: Cell biology
Impakt faktor: 12.270, rok: 2020
Způsob publikování: Open access
http://dx.doi.org/10.1016/j.devcel.2019.11.015

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.
Trvalý link: http://hdl.handle.net/11104/0306065