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A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at the plasma membrane.

Concentration gradients regulate many cell biological and developmental processes. In rod-shaped fission yeast cells, polar cortical gradients of the DYRK family kinase Pom1 couple cell length with mitotic commitment by inhibiting a mitotic inducer positioned at midcell. However, how Pom1 gradients are established is unknown. Here, we show that Tea4, which is normally deposited at cell tips by microtubules, is both necessary and, upon ectopic cortical localization, sufficient to recruit Pom1 to the cell cortex. Pom1 then moves laterally at the plasma membrane, which it binds through a basic region exhibiting direct lipid interaction. Pom1 autophosphorylates in this region to lower lipid affinity and promote membrane release. Tea4 triggers Pom1 plasma membrane association by promoting its dephosphorylation through the protein phosphatase 1 Dis2. We propose that local dephosphorylation induces Pom1 membrane association and nucleates a gradient shaped by the opposing actions of lateral diffusion and autophosphorylation-dependent membrane detachment.

Pubmed ID: 21703453


  • Hachet O
  • Berthelot-Grosjean M
  • Kokkoris K
  • Vincenzetti V
  • Moosbrugger J
  • Martin SG



Publication Data

June 24, 2011

Associated Grants

  • Agency: European Research Council, Id: 260493

Mesh Terms

  • Amino Acid Sequence
  • Cell Cycle
  • Cell Membrane
  • Microtubule-Associated Proteins
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Kinases
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Sequence Alignment