Phosphorylation of dynamin bp ERK2 inhibits the dynamin-microtubule interaction

Svetlana Earnest, Andrei Khokhlatchev, Joseph P. Albanesi, Barbara Barylko

Research output: Contribution to journalArticlepeer-review

43 Scopus citations


In the present study we show that purified bovine brain dynamin can be phosphorylated by MAP kinase, ERK2, with a stoichiometry of 1 mol phosphate/mol dynamin. The phosphorylated serine residue is located within the C-terminal 10 kDa of dynamin. Dynamin I phosphorylated by ERK2 can be specifically dephosphorylated by calcineurin but not by protein phosphatase 2A (PP2A). Phosphorylation of dynamin by ERK2 weakens the binding of dynamin to microtubules and inhibits dynamin's microtubule-activated GTPase activity. Stimulation of GTPase activity by either Grb2 or phospholipids was not affected by ERK2 phosphorylation, suggesting that the binding sites for Grb2 and phospholipids do not overlap with that for microtubules.

Original languageEnglish (US)
Pages (from-to)62-66
Number of pages5
JournalFEBS Letters
Issue number1
StatePublished - Oct 28 1996


  • Dynamin
  • ERK2
  • GTPase activity
  • Phosphorylation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'Phosphorylation of dynamin bp ERK2 inhibits the dynamin-microtubule interaction'. Together they form a unique fingerprint.

Cite this