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LIMK1 — PAK4
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind Interaction:
PAK4
—
LIMK1
Soosairajah et al., EMBO J 2005
-
IRef Bind_translation Interaction:
PAK4
—
LIMK1
(experimental interaction detection)
Soosairajah et al., EMBO J 2005
-
IRef Biogrid Interaction:
LIMK1
—
PAK4
(direct interaction, enzymatic study)
Dan et al., J Biol Chem 2001*
-
IRef Biogrid Interaction:
LIMK1
—
PAK4
(direct interaction, pull down)
Dan et al., J Biol Chem 2001*
-
IRef Hprd Interaction:
LIMK1
—
PAK4
(in vitro)
Dan et al., J Biol Chem 2001*
-
IRef Ophid Interaction:
PAK4
—
LIMK1
(aggregation, confirmational text mining)
Dan et al., J Biol Chem 2001*
-
IRef Ophid Interaction:
PAK4
—
LIMK1
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Dan et al., J Biol Chem 2001
:
Here we show that
PAK4 also
regulates the activity of the protein kinase
LIM kinase 1 (LIMK1)
Thirone et al., Am J Physiol Cell Physiol 2009
:
Hyperosmolarity provoked cofilin phosphorylation was mediated by the Rho/Rho kinase ( ROCK )
/LIM kinase ( LIMK ) but not the Rac/PAK/LIMK pathway, because 1 ) dominant negative ( DN ) Rho and DN-ROCK but not DN-Rac and DN-PAK inhibited cofilin phosphorylation ; 2 ) constitutively active ( CA ) Rho and CA-ROCK but not CA-Rac and
CA-PAK induced cofilin phosphorylation ; 3 ) hyperosmolarity induced LIMK-2 phosphorylation, and 4 ) inhibition of ROCK by Y-27632 suppressed the hypertonicity triggered LIMK-2 and cofilin phosphorylation.We thenexamined whether cofilin and its phosphorylation play a role in the hypertonicity triggered F-actin changes