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This study investigates the autoactivation mechanism of p21-activated kinase 2 (PAK2) through autophosphorylation in the presence of small G proteins Cdc42 and Rac. The findings reveal that PAK2 undergoes a bipartite autophosphorylation mechanism, with distinct phosphorylation events occurring at multiple residues in the regulatory domain and at Thr-402 in the catalytic domain, which is essential for activation. Additionally, the binding of exogenous substrates has minimal impact on the autoactivation rate
- Author
- dasjauharolevel
- Language
- EN