ArticleNature plants2024
D6PK plasma membrane polarity requires a repeated CXX(X)P motif and PDK1-dependent phosphorylation.
Article in Nature plants, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- PAX-regulated self-organizing polarity drives procambial strand formation.Nature plants · 2026Article
- Genome-Wide Identification of the AGC Kinase Family in Tetraploid Potato (Plants (Basel, Switzerland) · 2025Article
- The protein kinases KIPK and KIPK-LIKE1 suppress overbending during negative hypocotyl gravitropic growth in Arabidopsis.The Plant cell · 2025Article
- Genome-Wide Analysis ofInternational journal of molecular sciences · 2025Article
- Keeping D6PK polar.Nature plants · 2024Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
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.
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Registered trials
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