LIM kinase phosphorylation by ROCK

Stable Identifier
R-HSA-419087
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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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. ROCK1 and ROCK2 phosphorylate and activate LIM kinases LIMK1 and LIMK2 at Thr508 and Thr505, respectively (Ohashi et al. 2000, Sumi et al. 2001). These threonine residues lay within the activation loop of the kinase domain. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, resulting in stabilization of the actin cytoskeleton (Pandey et al. 2006).
Literature References
PubMed ID Title Journal Year
11018042 Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase

Nakamura, T, Matsumoto, K, Sumi, T

J Biol Chem 2001
16219803 Regulation of LIM-kinase 1 and cofilin in thrombin-stimulated platelets

Siess, W, Bamburg, JR, Pandey, D, Goyal, P

Blood 2006
10652353 Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop

Ohashi, K, Narumiya, S, Mizuno, K, Ishizaki, T, Nagata, K, Maekawa, M

J Biol Chem 2000
Participants
Participates
Catalyst Activity

protein serine/threonine kinase activity of Activated ROCK:RhoA/B/C:GTP [plasma membrane]

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