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Graf, A.* ; Bassukas, A.E.L.* ; Xiao, Y.* ; Barbosa, I.C.R.* ; Mergner, J.* ; Grill, P. ; Michalke, B. ; Kuster, B.* ; Schwechheimer, C.*

D6PK plasma membrane polarity requires a repeated CXX(X)P motif and PDK1-dependent phosphorylation.

Nat. Plants 10, 300-314 (2024)
Verlagsversion DOI PMC
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
D6 PROTEIN KINASE (D6PK) is a polarly localized plasma-membrane-associated kinase from Arabidopsis thaliana that activates polarly distributed PIN-FORMED auxin transporters. D6PK moves rapidly to and from the plasma membrane, independent of its PIN-FORMED targets. The middle D6PK domain, an insertion between kinase subdomains VII and VIII, is required and sufficient for association and polarity of the D6PK plasma membrane. How D6PK polarity is established and maintained remains to be shown. Here we show that cysteines from repeated middle domain CXX(X)P motifs are S-acylated and required for D6PK membrane association. While D6PK S-acylation is not detectably regulated during intracellular transport, phosphorylation of adjacent serine residues, in part in dependence on the upstream 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE, promotes D6PK transport, controls D6PK residence time at the plasma membrane and prevents its lateral diffusion. We thus identify new mechanisms for the regulation of D6PK plasma membrane interaction and polarity.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Protein S-acylation; Auxin Transport; Palmitoylation; Arabidopsis; Kinase; Quantification; Growth
ISSN (print) / ISBN 2055-026X
e-ISSN 2055-0278
Zeitschrift Nature Plants
Quellenangaben Band: 10, Heft: 2, Seiten: 300-314 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Research Unit Analytical BioGeoChemistry (BGC)
Förderungen Deutsche Forschungsgemeinschaft
Alexander-von-Humboldt foundation
Center for Advanced Light Microscopy (CALM) of the TUM School of Life Sciences