Regulating Vav1 phosphorylation by the SHP-1 tyrosine phosphatase is a fine-tuning mechanism for the negative regulation of DISC formation and Fas-mediated cell death signaling

G. Koncz, K. Kerekes, K. Chakrabandhu, A. O. Hueber

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The actin cytoskeleton association is required for caspase 8-independent Fas/CD95 receptor internalization, a critical step for an optimal death-inducing signaling complex formation along the endocytic pathway, leading to efficient activation of the caspase cascade and, ultimately, cell death. However, the way in which this initiation phase of Fas receptor signaling is regulated is still unknown. We report herein that, in B cells, upon Fas engagement, the tyrosine phosphatase SHP-1-regulated Vav dephosphorylation, by downmodulating the Fas-ezrin-actin linkage is a fine-tune switch-off mechanism that the cell uses as a way to terminate the receptor internalization, controlling therefore the time and extent of the DISC formation and cell death.

Original languageEnglish
Pages (from-to)494-503
Number of pages10
JournalCell Death and Differentiation
Volume15
Issue number3
DOIs
Publication statusPublished - Mar 2008

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Non-Receptor Type 6 Protein Tyrosine Phosphatase
CD95 Antigens
Cell Death
Death Domain Receptor Signaling Adaptor Proteins
Phosphorylation
Caspase 8
Caspases
Actin Cytoskeleton
Actins
B-Lymphocytes

ASJC Scopus subject areas

  • Cell Biology

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Regulating Vav1 phosphorylation by the SHP-1 tyrosine phosphatase is a fine-tuning mechanism for the negative regulation of DISC formation and Fas-mediated cell death signaling. / Koncz, G.; Kerekes, K.; Chakrabandhu, K.; Hueber, A. O.

In: Cell Death and Differentiation, Vol. 15, No. 3, 03.2008, p. 494-503.

Research output: Contribution to journalArticle

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