Phosphorylation of LIMK-1 by PAK

Stable Identifier
Reaction [transition]
Homo sapiens
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LIM kinases are serine protein kinases with a unique combination of two N-terminal LIM motifs, a central PDZ domain, and a C-terminal protein kinase domain. LIMK1 is one of the downstream targets of PAK1 and is activated through phosphorylation by PAK1 on T508 within its activation loop (Edwards et al. 1999, Aizawa et al. 2001). LIM-kinase is responsible for the tight regulation of the activity of cofilin (a protein that depolymerizes actin filaments) and thus maintains the balance between actin assembly and disassembly. Phosphorylated cofilin is inactive, resulting in stabilization of the actin cytoskeleton.

Literature References
PubMed ID Title Journal Year
11276226 Phosphorylation of cofilin by LIM-kinase is necessary for semaphorin 3A-induced growth cone collapse

Sekine-Aizawa, Y, Wakatsuki, S, Sehara-Fujisawa, A, Ohashi, K, Goshima, Y, Aizawa, H, Moriyama, K, Yahara, I, Ishii, A, Mizuno, K, Sasaki, Y

Nat Neurosci 2001
10559936 Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics

Sanders, LC, Edwards, DC, Bokoch, GM, Gill, GN

Nat Cell Biol 1999
Catalyst Activity

protein serine/threonine kinase activity of Sema3A:Nrp-1:PlexinA:Rac1-GTP:pPAK [plasma membrane]

Orthologous Events
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