Phosphorylation of dynamin bp ERK2 inhibits the dynamin-microtubule interaction

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

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

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
Volume396
Issue number1
DOIs
StatePublished - Oct 28 1996

Fingerprint

Dynamins
Phosphorylation
Microtubules
GTP Phosphohydrolases
Phospholipids
Dynamin I
Protein Phosphatase 2
Calcineurin
Stoichiometry
Serine
Brain
Phosphotransferases
Phosphates
Binding Sites

Keywords

  • Dynamin
  • ERK2
  • GTPase activity
  • Phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Phosphorylation of dynamin bp ERK2 inhibits the dynamin-microtubule interaction. / Earnest, Svetlana; Khokhlatchev, Andrei; Albanesi, Joseph P.; Barylko, Barbara.

In: FEBS Letters, Vol. 396, No. 1, 28.10.1996, p. 62-66.

Research output: Contribution to journalArticle

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