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LIM domain kinase 1

There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. LIMK1 is a serine/threonine kinase that regulates actin polymerization via phosphorylation and inactivation of the actin binding factor cofilin. This protein is ubiquitously expressed during development and plays a role in many cellular processes associated with cytoskeletal structure. This protein also stimulates axon growth and may play a role in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome. Alternative splicing results in multiple transcript variants encoding distinct isoforms.[provided by RefSeq, Feb 2011] (from NCBI)
Top mentioned proteins: Actin, LIM, cofilin, Rhodopsin, V1a
Papers using LIMK1 antibodies
A role of LIM kinase 1/cofilin pathway in regulating endocytic trafficking of EGF receptor in human breast cancer cells
Chakrabarti Ratna et al., In Molecular Cancer, 2005
... cells were developed by stable transfection of constitutively active (phosphomimic mutant) LIMK1 gene containing a Flag tag at the 3' end cloned in pRevTRE (Clontech, Mountain View, CA), and ...
Papers on LIMK1
Identification of para-Substituted Benzoic Acid Derivatives as Potent Inhibitors of the Protein Phosphatase Slingshot.
Sun et al., Jinan, China. In Chemmedchem, 10 Dec 2015
UNASSIGNED: Slingshot proteins form a small group of dual-specific phosphatases that modulate cytoskeleton dynamics through dephosphorylation of cofilin and Lim kinases (LIMK).
Roles of LIM kinases in central nervous system function and dysfunction.
Bénédetti et al., Orléans, France. In Febs Lett, 03 Dec 2015
UNASSIGNED: LIM kinase 1 (LIMK1) and LIM kinase 2 (LIMK2) regulate actin dynamics by phosphorylating cofilin.
LIM kinase inhibitors disrupt mitotic microtubule organization and impair tumor cell proliferation.
Olson et al., London, United Kingdom. In Oncotarget, 03 Dec 2015
A previously-described LIMK inhibitor (LIMKi) induced dose-dependent microtubule alterations that resulted in significant mitotic defects, and increased the cytotoxic potency of microtubule polymerization inhibitors.
Endothelin A receptor drives invadopodia function and cell motility through the β-arrestin/PDZ-RhoGEF pathway in ovarian carcinoma.
Rosanò et al., Roma, Italy. In Oncogene, 02 Dec 2015
Depletion of PDZ-RhoGEF, or β-arr1, or RhoC, as well as the treatment with the dual ET-1 receptor antagonist macitentan, significantly impairs invadopodia function, MMP activity and invasion, demonstrating that β-arr1/PDZ-RhoGEF interaction mediates ETAR-driven ROCK-LIMK-cofilin pathway through the control of RhoC activity.
Discovery of bis-aryl urea derivatives as potent and selective Limk inhibitors: Exploring Limk1 activity and Limk1/ROCK2 selectivity through a combined computational study.
Feng et al., Shanghai, China. In Bioorg Med Chem, 30 Nov 2015
UNASSIGNED: Lim kinase (Limk), a proline/serine-rich sequence, can regulate the polymerization of the actin filaments by phosphorylating, and it is found to be highly involved in various human diseases.
Cofilin phosphorylation is elevated after F-actin disassembly induced by Rac1 depletion.
Liu et al., Xi'an, China. In Biofactors, 10 Oct 2015
These effects were independent of the signaling pathways for p21-activated kinase/LIM kinase (Pak/LIMK), protein kinase C, or protein kinase D or generation of reactive oxygen species.
Participation of group I p21-activated kinases in neuroplasticity.
Barros et al., Rio Grande, Brazil. In J Physiol Paris, Sep 2014
Their substrates in these processes include other intracellular signaling molecules, such as Raf, Mek and LIMK, as well as other components of the cytoskeleton, such as MLC and FLNa.
[LIM kinases and their roles in the nervous system].
Zhang et al., Hangzhou, China. In Zhejiang Da Xue Xue Bao Yi Xue Ban, 2014
LIM kinase-1 (LIMK1) and LIM kinase-2 (LIMK2) are kinases that have serine/threonine and tyrosine dual specificity.
β-Arrestin-kinase scaffolds: turn them on or turn them off?
DeFea et al., Riverside, United States. In Wiley Interdiscip Rev Syst Biol Med, 2013
Subsequently a number of other kinases have been shown to undergo β-arrestin-dependent regulation, including Akt, phosphatidylinositol-3kinase (PI3K), Lim-domain-containing kinase (LIMK), calcium calmodulin kinase II (CAMKII), and calcium calmodulin kinase kinase β (CAMKKβ).
LIM kinases are attractive targets with many macromolecular partners and only a few small molecule regulators.
Manetti, Siena, Italy. In Med Res Rev, 2012
The small compounds identified as LIMK1 and LIMK2 modulators are also reported, as well as their role as possible therapeutic agents for LIMK-induced diseases.
A functional cooperativity between Aurora A kinase and LIM kinase1: implication in the mitotic process.
Chakrabarti et al., Orlando, United States. In Cell Cycle, 2012
Aur-A physically associates with LIMK1 and activates it through phosphorylation, which is important for its centrosomal and spindle pole localization.
LIM kinase has a dual role in regulating lamellipodium extension by decelerating the rate of actin retrograde flow and the rate of actin polymerization.
Mizuno et al., Sendai, Japan. In J Biol Chem, 2011
LIMK1 has a dual role in regulating lamellipodium extension by decelerating actin retrograde flow and polymerization.
Actomyosin-mediated cellular tension drives increased tissue stiffness and β-catenin activation to induce epidermal hyperplasia and tumor growth.
Olson et al., Glasgow, United Kingdom. In Cancer Cell, 2011
Inhibiting actomyosin contractility by blocking LIMK or myosin ATPase attenuated these responses, as did FAK inhibition.
Nuclear and cytoplasmic LIMK1 enhances human breast cancer progression.
Gutierrez-Hartmann et al., Aurora, United States. In Mol Cancer, 2010
LIMK1 activity in both the cytoplasmic and nuclear compartments promotes breast cancer progression.
LIM kinase 1 - dependent cofilin 1 pathway and actin dynamics mediate nuclear retinoid receptor function in T lymphocytes.
Natarajan et al., Frederick, United States. In Bmc Mol Biol, 2010
Data describe the role of LIMK1-mediated CFL1 pathway and actin dynamics in retinoid receptor mediated function and show that LIMK1-mediated phosphocycling of CFL1 plays a role in maintaining actin homeostasis and receptor activity.
Overexpression of LIMK1 promotes migration ability of multidrug-resistant osteosarcoma cells.
Gao et al., Changchun, China. In Oncol Res, 2010
demonstrated that LIMK1, a key regulator of actin cytoskeleton, was overexpressed at both mRNA and protein levels in MG63/VCR cells and the higher LIMK1 protein level was correlated with higher level of phosphorylated cofilin
A brain-specific microRNA regulates dendritic spine development.
Greenberg et al., Boston, United States. In Nature, 2006
This effect is mediated by miR-134 inhibition of the translation of an mRNA encoding a protein kinase, Limk1, that controls spine development.
LATS1 tumour suppressor affects cytokinesis by inhibiting LIMK1.
Xu et al., New Haven, United States. In Nat Cell Biol, 2004
LATS1 is a novel cytoskeleton regulator that affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1.
Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin.
Uemura et al., Kyoto, Japan. In Cell, 2002
In contrast to the mechanisms of inactivation of ADF/cofilin by kinases such as LIM-kinase 1 (LIMK1), much less is known about its reactivation through dephosphorylation.
Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization.
Mizuno et al., Fukuoka, Japan. In Nature, 1998
Here we show that LIM-kinase 1 (LIMK-1), a serine/threonine kinase containing LIM and PDZ domains, phosphorylates cofilin at Ser 3, both in vitro and in vivo.
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