Plasma Membrane Domain Patterning and Self-Reinforcing Polarity in Arabidopsis. Marhava, P., Aliaga Fandino, A. C., Koh, S. W. H., Jelínková, A., Kolb, M., Janacek, D. P., Breda, A. S., Cattaneo, P., Hammes, U. Z., Petrášek, J., & Hardtke, C. S. Developmental Cell, 52(2):223–235.e5, January, 2020. ![Plasma Membrane Domain Patterning and Self-Reinforcing Polarity in Arabidopsis [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{marhava_plasma_2020,
title = {Plasma {Membrane} {Domain} {Patterning} and {Self}-{Reinforcing} {Polarity} in {Arabidopsis}},
volume = {52},
issn = {1534-5807},
url = {https://www.sciencedirect.com/science/article/pii/S1534580719309840},
doi = {10.1016/j.devcel.2019.11.015},
abstract = {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.},
language = {en},
number = {2},
urldate = {2022-05-02},
journal = {Developmental Cell},
author = {Marhava, Petra and Aliaga Fandino, Ana Cecilia and Koh, Samuel W. H. and Jelínková, Adriana and Kolb, Martina and Janacek, Dorina P. and Breda, Alice S. and Cattaneo, Pietro and Hammes, Ulrich Z. and Petrášek, Jan and Hardtke, Christian S.},
month = jan,
year = {2020},
keywords = {DRP1A, PIP5K1, PIP5K2, endocytosis, phloem, polar auxin transport, polarity, protophloem, root},
pages = {223--235.e5},
}
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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. 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