Estradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex: The roles of heat shock protein 90 (Hsp90) and MEK2

György Sétáló, Meharvan Singh, Xiaoping Guan, C. Dominique Toran-Allerand

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

Confocal laser scanning microscopy was used to identify the cells within organotypic slice cultures of the developing mouse cerebral cortex that respond to estradiol treatment by phosphorylation of ERK1 and ERK2. Estrogen-responsive cells resembled neurons morphologically and expressed the neuronal marker microtubule-associated protein 2B. The intracellular distribution of the phospho-ERK signal was both cytoplasmic and nuclear, but inhibition of protein synthesis abolished the appearance of the nuclear signal. ERK1and ERK2 also coimmunoprecipitated with heat shock protein 90 (Hsp90) in the cerebral cortical explants. Geldanamycin effectively disrupted this association and prevented ERK phosphorylation. Surprisingly, MEK2 but not MEK1 was the principal mediator of estradiol-induced activation of ERK. Our data demonstrate the requirement for Hsp90 in estrogen-induced activation of ERK1 and ERK2 by MEK2 in the developing mouse cerebral cortex and also provide insight into alternative mechanisms by which estradiol may influence cytoplasmic and nuclear events in responsive neurons via the MAP kinase cascade.

Original languageEnglish
Pages (from-to)1-12
Number of pages12
JournalJournal of Neurobiology
Volume50
Issue number1
DOIs
StatePublished - 1 Jan 2002

Fingerprint

HSP90 Heat-Shock Proteins
Cerebral Cortex
Estradiol
Phosphorylation
Estrogens
Neurons
Microtubule-Associated Proteins
MAP Kinase Signaling System
Nuclear Proteins
Confocal Microscopy

Keywords

  • ERK
  • Estrogen
  • Geldanamycin
  • Hsp90
  • MEK

Cite this

Sétáló, György ; Singh, Meharvan ; Guan, Xiaoping ; Toran-Allerand, C. Dominique. / Estradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex : The roles of heat shock protein 90 (Hsp90) and MEK2. In: Journal of Neurobiology. 2002 ; Vol. 50, No. 1. pp. 1-12.
@article{7c495dc9c6f94dab8c535a5043e6aa01,
title = "Estradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex: The roles of heat shock protein 90 (Hsp90) and MEK2",
abstract = "Confocal laser scanning microscopy was used to identify the cells within organotypic slice cultures of the developing mouse cerebral cortex that respond to estradiol treatment by phosphorylation of ERK1 and ERK2. Estrogen-responsive cells resembled neurons morphologically and expressed the neuronal marker microtubule-associated protein 2B. The intracellular distribution of the phospho-ERK signal was both cytoplasmic and nuclear, but inhibition of protein synthesis abolished the appearance of the nuclear signal. ERK1and ERK2 also coimmunoprecipitated with heat shock protein 90 (Hsp90) in the cerebral cortical explants. Geldanamycin effectively disrupted this association and prevented ERK phosphorylation. Surprisingly, MEK2 but not MEK1 was the principal mediator of estradiol-induced activation of ERK. Our data demonstrate the requirement for Hsp90 in estrogen-induced activation of ERK1 and ERK2 by MEK2 in the developing mouse cerebral cortex and also provide insight into alternative mechanisms by which estradiol may influence cytoplasmic and nuclear events in responsive neurons via the MAP kinase cascade.",
keywords = "ERK, Estrogen, Geldanamycin, Hsp90, MEK",
author = "Gy{\"o}rgy S{\'e}t{\'a}l{\'o} and Meharvan Singh and Xiaoping Guan and Toran-Allerand, {C. Dominique}",
year = "2002",
month = "1",
day = "1",
doi = "10.1002/neu.10000",
language = "English",
volume = "50",
pages = "1--12",
journal = "Journal of Neurobiology",
issn = "0022-3034",
publisher = "John Wiley and Sons Inc.",
number = "1",

}

Estradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex : The roles of heat shock protein 90 (Hsp90) and MEK2. / Sétáló, György; Singh, Meharvan; Guan, Xiaoping; Toran-Allerand, C. Dominique.

In: Journal of Neurobiology, Vol. 50, No. 1, 01.01.2002, p. 1-12.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Estradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex

T2 - The roles of heat shock protein 90 (Hsp90) and MEK2

AU - Sétáló, György

AU - Singh, Meharvan

AU - Guan, Xiaoping

AU - Toran-Allerand, C. Dominique

PY - 2002/1/1

Y1 - 2002/1/1

N2 - Confocal laser scanning microscopy was used to identify the cells within organotypic slice cultures of the developing mouse cerebral cortex that respond to estradiol treatment by phosphorylation of ERK1 and ERK2. Estrogen-responsive cells resembled neurons morphologically and expressed the neuronal marker microtubule-associated protein 2B. The intracellular distribution of the phospho-ERK signal was both cytoplasmic and nuclear, but inhibition of protein synthesis abolished the appearance of the nuclear signal. ERK1and ERK2 also coimmunoprecipitated with heat shock protein 90 (Hsp90) in the cerebral cortical explants. Geldanamycin effectively disrupted this association and prevented ERK phosphorylation. Surprisingly, MEK2 but not MEK1 was the principal mediator of estradiol-induced activation of ERK. Our data demonstrate the requirement for Hsp90 in estrogen-induced activation of ERK1 and ERK2 by MEK2 in the developing mouse cerebral cortex and also provide insight into alternative mechanisms by which estradiol may influence cytoplasmic and nuclear events in responsive neurons via the MAP kinase cascade.

AB - Confocal laser scanning microscopy was used to identify the cells within organotypic slice cultures of the developing mouse cerebral cortex that respond to estradiol treatment by phosphorylation of ERK1 and ERK2. Estrogen-responsive cells resembled neurons morphologically and expressed the neuronal marker microtubule-associated protein 2B. The intracellular distribution of the phospho-ERK signal was both cytoplasmic and nuclear, but inhibition of protein synthesis abolished the appearance of the nuclear signal. ERK1and ERK2 also coimmunoprecipitated with heat shock protein 90 (Hsp90) in the cerebral cortical explants. Geldanamycin effectively disrupted this association and prevented ERK phosphorylation. Surprisingly, MEK2 but not MEK1 was the principal mediator of estradiol-induced activation of ERK. Our data demonstrate the requirement for Hsp90 in estrogen-induced activation of ERK1 and ERK2 by MEK2 in the developing mouse cerebral cortex and also provide insight into alternative mechanisms by which estradiol may influence cytoplasmic and nuclear events in responsive neurons via the MAP kinase cascade.

KW - ERK

KW - Estrogen

KW - Geldanamycin

KW - Hsp90

KW - MEK

UR - http://www.scopus.com/inward/record.url?scp=0036135006&partnerID=8YFLogxK

U2 - 10.1002/neu.10000

DO - 10.1002/neu.10000

M3 - Article

C2 - 11748628

AN - SCOPUS:0036135006

VL - 50

SP - 1

EP - 12

JO - Journal of Neurobiology

JF - Journal of Neurobiology

SN - 0022-3034

IS - 1

ER -