Phospholipid composition and a polybasic motif determine D6 PROTEIN KINASE polar association with the plasma membrane and tropic responses

Inês C.R. Barbosa, Hiromasa Shikata, Melina Zourelidou, Mareike Heilmann, Ingo Heilmann, Claus Schwechheimer

Research output: Contribution to journalArticlepeer-review

80 Scopus citations

Abstract

Polar transport of the phytohormone auxin through PIN-FORMED (PIN) auxin efflux carriers is essential for the spatiotemporal control of plant development. The Arabidopsis thaliana serine/threonine kinase D6 PROTEIN KINASE (D6PK) is polarly localized at the plasma membrane of many cells where it colocalizes with PINs and activates PIN-mediated auxin efflux. Here, we show that the association of D6PK with the basal plasma membrane and PINs is dependent on the phospholipid composition of the plasma membrane as well as on the phosphatidylinositol phosphate 5-kinases PIP5K1 and PIP5K2 in epidermis cells of the primary root.We further show that D6PK directly binds polyacidic phospholipids through a polybasic lysine-rich motif in the middle domain of the kinase. The lysine-rich motif is required for proper PIN3 phosphorylation and for auxin transport-dependent tropic growth. Polybasic motifs are also present at a conserved position in other D6PK-related kinases and required for membrane and phospholipid binding. Thus, phospholipid-dependent recruitment to membranes through polybasic motifs might not only be required for D6PK-mediated auxin transport but also other processes regulated by these, as yet, functionally uncharacterized kinases.

Original languageEnglish
Pages (from-to)4687-4700
Number of pages14
JournalDevelopment (Cambridge)
Volume143
Issue number24
DOIs
StatePublished - 15 Dec 2016

Keywords

  • Auxin transport
  • D6PK
  • Lysine-rich motif
  • Phospholipid
  • Plasma membrane

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