Transphosphorylation of pLIMK1

Stable Identifier
Reaction [omitted]
Homo sapiens
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Binding of Hsp90 to the LIMK proteins protects them from degradation and promotes their dimer formation and transphosphorylation. It is estimated that LIMK1 contains at least 5 phospho-amino acids primarily phospho-serines, in its kinase domain. The positions of these serine residues are not known. Transphosphorylation of these serine residues in LIMK1 increases its stability.

Literature References
PubMed ID Title Journal Year
16641196 Hsp90 increases LIM kinase activity by promoting its homo-dimerization

Yarden, Y, Soosairajah, J, Morton, CJ, Harari, D, Li, R, Bernard, O, Parker, MW, Ng, HL, Price, J, Citri, A

FASEB J 2006
7848918 Kiz-1, a protein with LIM zinc finger and kinase domains, is expressed mainly in neurons

Kannourakis, G, Ganiatsas, S, Dringen, R, Bernard, O

Cell Growth Differ 1994
17188549 Lim kinases, regulators of actin dynamics

Bernard, O

Int J Biochem Cell Biol 2007
Catalyst Activity

protein serine/threonine kinase activity of pLIMK dimer:HSP-90 [cytosol]

Orthologous Events
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