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The lipid code-dependent phosphoswitch PDK1–D6PK activates PIN-mediated auxin efflux in Arabidopsis
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SYSNO ASEP 0531204 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The lipid code-dependent phosphoswitch PDK1–D6PK activates PIN-mediated auxin efflux in Arabidopsis Author(s) Tan, S. (US)
Zhang, X. (US)
Kong, W. (US)
Yang, X.-J. (CN)
Molnár, G. (AT)
Vondráková, Zuzana (UEB-Q) RID, ORCID
Filepová, Roberta (UEB-Q) SAI
Petrášek, Jan (UEB-Q) RID, ORCID
Friml, J. (AT)
Xue, H.W. (CN)Number of authors 10 Source Title Nature Plants - ISSN 2055-026X
Roč. 6, č. 5 (2020), s. 556-569Number of pages 14 s. Language eng - English Country GB - United Kingdom Keywords D6 PROTEIN-KINASE ; PLASMA-MEMBRANE ; PHOSPHATIDIC-ACID Subject RIV ED - Physiology OECD category Biochemistry and molecular biology Method of publishing Open access Institutional support UEB-Q - RVO:61389030 UT WOS 000531787500006 EID SCOPUS 85084451659 DOI 10.1038/s41477-020-0648-9 Annotation The PDK1 lipid-dependent kinase controls PIN1 and auxin transport through a phosphorylation cascade that includes AGC-type kinase D6PK. The double pdk1 mutant reveals auxin-related phenotypes such as reduced gravitropism and lateral roots. Directional intercellular transport of the phytohormone auxin mediated by PIN-FORMED (PIN) efflux carriers has essential roles in both coordinating patterning processes and integrating multiple external cues by rapidly redirecting auxin fluxes. PIN activity is therefore regulated by multiple internal and external cues, for which the underlying molecular mechanisms are not fully elucidated. Here, we demonstrate that 3 '-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE1 (PDK1), which is conserved in plants and mammals, functions as a molecular hub that perceives upstream lipid signalling and modulates downstream substrate activity through phosphorylation. Using genetic analysis, we show that the loss-of-function Arabidopsis pdk1.1 pdk1.2 mutant exhibits a plethora of abnormalities in organogenesis and growth due to defective polar auxin transport. Further cellular and biochemical analyses reveal that PDK1 phosphorylates D6 protein kinase, a well-known upstream activator of PIN proteins. We uncover a lipid-dependent phosphorylation cascade that connects membrane-composition-based cellular signalling with plant growth and patterning by regulating morphogenetic auxin fluxes. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2021 Electronic address http://doi.org/10.1038/s41477-020-0648-9
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