共 36 条
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
被引:15
作者:
Koncz, G.
[1
]
Kerekes, K.
[1
]
Chakrabandhu, K.
[1
]
Hueber, A-O
[1
]
机构:
[1] Inst Signalling Dev Biol & Canc Res, CNRS, UMR 6543, F-06189 Nice, France
基金:
匈牙利科学研究基金会;
关键词:
Fas;
signaling;
Vav;
SHP-1;
D O I:
10.1038/sj.cdd.4402282
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
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.
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页码:494 / 503
页数:10
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