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Regulation of ERK2 dephosphorylation in G1-stimulated rat T lymphoblasts.

Abstract：

:Rat T lymphoblasts arrested in the G1 phase of the cell cycle by interleukin-2 (IL-2) deprivation can be forced to proceed to the S phase when they are stimulated with IL-2 or the phorbol ester phorbol 12,13-dibutyrate (PDBu). When PDBu is used as a stimulus, extracellular regulated kinase 2 (ERK2) is activated by threonine and tyrosine phosphorylation by the dual-specificity kinase MEK. Here we have studied the regulation of ERK2 dephosphorylation as a mechanism for inactivation of this kinase. In vivo inhibition of ERK2 dephosphorylation observed after preincubation with translation or transcription inhibitors (cycloheximide or actinomycin, respectively) indicates the involvement of at least one inducible phosphatase, the best candidate for which is the dual-specificity phosphatase PAC-1. Other noninducible phosphatases must act as well, however, because sodium orthovanadate is a more effective dephosphorylation blocker than cycloheximide. In addition, the okadaic acid effect in ERK2 dephosphorylation indicates that Ser/Thr phosphatases are also involved, directly and/or indirectly.

journal_name

J Clin Immunol

journal_title

Journal of clinical immunology

authors

Lisbona C,Alemany S,Fernández-Renart M

doi

10.1023/a:1027375828134

subject

Has Abstract

pub_date

1997-11-01 00:00:00

pages

494-501

issue

6

eissn

0271-9142

issn

1573-2592

journal_volume

17

pub_type

杂志文章

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