PAK interacts with NCK and MLK2 to regulate the activation of jun N‐terminal kinase

FEBS Letters

Moss, Tom¹  Islam, Nazrul¹  Poitras, Luc¹  Jean, Steve¹ 

[1] Cancer Research Centre and Department of Medical Biology, Laval University, Hôtel-Dieu de Quebec, 9 rue McMahon, Québec, QC, Canada G1R 2J6

关键词: xPAK1;    Ste20p;    xMLK2;    JNK/SAPK1;    Stress kinase cascade;    Intracellular signalling;    PAK;    p21-GTPase activated kinase;    MLK;    mixed lineage kinase;    JNK;    jun N-terminal kinase;    SH2–SH3;    Src homology domain 2–3;    Squelching;    non-stochiometric expression causing disruption of a multi-protein complex;    MAPK;    mitogen activated protein kinase;    SAPK;    stress activated protein kinases;   

DOI  :  10.1016/S0014-5793(03)00424-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The p21-GTPase activated kinase, PAK1, and the mixed lineage kinase, MLK2, have been implicated in the activation of jun N-terminal kinase (JNK). However, the role of PAK1 in JNK activation is still not understood. Here we show that over-expression of the SH3-SH2 adapter Nck ‘squelches’ JNK activation but this squelching is relieved by over-expression of PAK1. In turn, PAK1 squelches activation of JNK by MLK2 and these kinases interact via their catalytic domains. The data suggest that PAK1 recruits MLK2 to an activated receptor via the adapter Nck, but cannot itself induce activation of the JNK cascade.

【 授权许可】

Unknown