A nanodomain-anchored scaffolding complex is required for the function and localization of phosphatidylinositol 4-kinase alpha in plants
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F22%3A00556322" target="_blank" >RIV/61389030:_____/22:00556322 - isvavai.cz</a>
Result on the web
<a href="http://doi.org/10.1093/plcell/koab135" target="_blank" >http://doi.org/10.1093/plcell/koab135</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/plcell/koab135" target="_blank" >10.1093/plcell/koab135</a>
Alternative languages
Result language
angličtina
Original language name
A nanodomain-anchored scaffolding complex is required for the function and localization of phosphatidylinositol 4-kinase alpha in plants
Original language description
Phosphoinositides are low-abundant lipids that participate in the acquisition of membrane identity through their spatiotemporal enrichment in specific compartments. Phosphatidylinositol 4-phosphate (PI4P) accumulates at the plant plasma membrane driving its high electrostatic potential, and thereby facilitating interactions with polybasic regions of proteins. PI4Ka1 has been suggested to produce PI4P at the plasma membrane, but how it is recruited to this compartment is unknown. Here, we pin-point the mechanism that tethers Arabidopsis thaliana phosphatidylinositol 4-kinase alpha1 (PI4Ka1) to the plasma membrane via a nanodomain-anchored scaffolding complex. We established that PI4Ka1 is part of a complex composed of proteins from the NO-POLLEN-GERMINATION, EFR3-OF-PLANTS, and HYCCIN-CONTAINING families. Comprehensive knockout and knockdown strategies revealed that subunits of the PI4Ka1 complex are essential for pollen, embryonic, and post-embryonic development. We further found that the PI4Ka1 complex is immobilized in plasma membrane nanodomains. Using synthetic mis-targeting strategies, we demonstrate that a combination of lipid anchoring and scaffolding localizes PI4Ka1 to the plasma membrane, which is essential for its function. Together, this work opens perspectives on the mechanisms and function of plasma membrane nanopatterning by lipid kinases.
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
10601 - Cell biology
Result continuities
Project
<a href="/en/project/GA19-21758S" target="_blank" >GA19-21758S: Good-Cop/Bad-Cop: Distinct roles of anionic phospholipids in plant endocytosis</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Plant Cell
ISSN
1040-4651
e-ISSN
1532-298X
Volume of the periodical
34
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
31
Pages from-to
302-332
UT code for WoS article
000745840600018
EID of the result in the Scopus database
2-s2.0-85123363753