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Regulation of the microsomal proteome by salicylic acid and deficiency of phosphatidylinositol-4-kinases β1 and β2 in Arabidopsis thaliana

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F21%3A00540793" target="_blank" >RIV/61389030:_____/21:00540793 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388963:_____/21:00540793

  • Result on the web

    <a href="https://doi.org/10.1002/pmic.202000223" target="_blank" >https://doi.org/10.1002/pmic.202000223</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/pmic.202000223" target="_blank" >10.1002/pmic.202000223</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Regulation of the microsomal proteome by salicylic acid and deficiency of phosphatidylinositol-4-kinases β1 and β2 in Arabidopsis thaliana

  • Original language description

    Phosphatidylinositol-4-kinases β1 and β2 (PI4Kβ1/PI4Kβ2), which are responsible for phosphorylation of phosphatidylinositol to phosphatidylinositol-4-phosphate, have important roles in plant vesicular trafficking. Moreover, PI4Kβ1/PI4Kβ2 negatively regulates biosynthesis of phytohormone salicylic acid (SA), a key player in plant immune responses. The study focused on the effect of PI4Kβ1/PI4Kβ2 deficiency and SA level on the proteome of microsomal fraction. For that purpose we used four Arabidopsis thaliana genotypes: wild type, double mutant with impaired function of PI4Kβ1/PI4Kβ2 (pi4kβ1/pi4kβ2) exhibiting high SA level, sid2 mutant with impaired SA biosynthesis depending on the isochorismate synthase 1 and triple mutant sid2/pi4kβ1/pi4kβ2. We identified 1797 proteins whose levels were changed between genotypes. We showed that increased SA concentration affected the levels of 473 proteins. This includes typical SA pathway markers but also points to connections between SA pathway and clathrin-independent endocytosis (flotillins) and exocytosis/protein secretion (syntaxins, tetraspanin) to be investigated in future. In contrast to SA, the absence of PI4Kβ1/PI4Kβ2 itself affected only 27 proteins. Among them we identified CERK1, a receptor for chitin. Although PI4Kβ1/PI4Kβ2 deficiency itself did not have a substantial impact on the proteome of the microsomal fraction, our data clearly show that it enhances proteome changes when SA pathway is modulated in parallel.

  • 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

    10609 - Biochemical research methods

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Proteomics

  • ISSN

    1615-9853

  • e-ISSN

    1615-9861

  • Volume of the periodical

    21

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    6

  • Pages from-to

    2000223

  • UT code for WoS article

    000620571400001

  • EID of the result in the Scopus database

    2-s2.0-85101281948