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The lipid code-dependent phosphoswitch PDK1–D6PK activates PIN-mediated auxin efflux in Arabidopsis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F20%3A00531204" target="_blank" >RIV/61389030:_____/20:00531204 - isvavai.cz</a>

  • Result on the web

    <a href="http://doi.org/10.1038/s41477-020-0648-9" target="_blank" >http://doi.org/10.1038/s41477-020-0648-9</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41477-020-0648-9" target="_blank" >10.1038/s41477-020-0648-9</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The lipid code-dependent phosphoswitch PDK1–D6PK activates PIN-mediated auxin efflux in Arabidopsis

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Nature Plants

  • ISSN

    2055-026X

  • e-ISSN

  • Volume of the periodical

    6

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    14

  • Pages from-to

    556-569

  • UT code for WoS article

    000531787500006

  • EID of the result in the Scopus database

    2-s2.0-85084451659