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

Alina Graf, Alkistis Eleftheria Lanassa Bassukas, Yao Xiao, Inês C.R. Barbosa, Julia Mergner, Peter Grill, Bernhard Michalke, Bernhard Kuster, Claus Schwechheimer

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)300-314
Number of pages15
JournalNature Plants
Volume10
Issue number2
DOIs
StatePublished - Feb 2024

Fingerprint

Dive into the research topics of 'D6PK plasma membrane polarity requires a repeated CXX(X)P motif and PDK1-dependent phosphorylation'. Together they form a unique fingerprint.

Cite this