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D6PK plasma membrane polarity requires a repeated CXX(X)P motif and PDK1-dependent phosphorylation.
Nat. Plants 10, 300-314 (2024)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Protein S-acylation; Auxin Transport; Palmitoylation; Arabidopsis; Kinase; Quantification; Growth
ISSN (print) / ISBN
2055-026X
e-ISSN
2055-0278
Journal
Nature Plants
Quellenangaben
Volume: 10,
Issue: 2,
Pages: 300-314
Publisher
Nature Publishing Group
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Research Unit Analytical BioGeoChemistry (BGC)
Grants
Deutsche Forschungsgemeinschaft
Alexander-von-Humboldt foundation
Center for Advanced Light Microscopy (CALM) of the TUM School of Life Sciences
Alexander-von-Humboldt foundation
Center for Advanced Light Microscopy (CALM) of the TUM School of Life Sciences