Phosphorylation of dynamin bp ERK2 inhibits the dynamin-microtubule interaction

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

doi:10.1016/0014-5793(96)01074-5

Phosphorylation of dynamin bp ERK2 inhibits the dynamin-microtubule interaction

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

Research output: Contribution to journal › Article › peer-review

43 Scopus citations

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 language	English (US)
Pages (from-to)	62-66
Number of pages	5
Journal	FEBS Letters
Volume	396
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(96)01074-5
State	Published - Oct 28 1996

Keywords

Dynamin
ERK2
GTPase activity
Phosphorylation

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(96)01074-5

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title = "Phosphorylation of dynamin bp ERK2 inhibits the dynamin-microtubule interaction",

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.",

keywords = "Dynamin, ERK2, GTPase activity, Phosphorylation",

author = "Svetlana Earnest and Andrei Khokhlatchev and Albanesi, {Joseph P.} and Barbara Barylko",

note = "Funding Information: Acknowledgements: We thank Dr. Melanie H. Cobb for encouragement and helpful discussions. This research was supported by National Institutes of Health Grant GM38567 (to J.P.A.) and the American Heart Association, Texas Affiliate Inc. Grant 94G-072 (to B.B.).",

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T1 - Phosphorylation of dynamin bp ERK2 inhibits the dynamin-microtubule interaction

AU - Earnest, Svetlana

AU - Khokhlatchev, Andrei

AU - Albanesi, Joseph P.

AU - Barylko, Barbara

N1 - Funding Information: Acknowledgements: We thank Dr. Melanie H. Cobb for encouragement and helpful discussions. This research was supported by National Institutes of Health Grant GM38567 (to J.P.A.) and the American Heart Association, Texas Affiliate Inc. Grant 94G-072 (to B.B.).

PY - 1996/10/28

Y1 - 1996/10/28

N2 - 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.

AB - 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.

KW - Dynamin

KW - ERK2

KW - GTPase activity

KW - Phosphorylation

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Phosphorylation of dynamin bp ERK2 inhibits the dynamin-microtubule interaction

Abstract

Keywords

ASJC Scopus subject areas

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