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LIM domain kinase 1

LIMK1, LIMK
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, LIMK2
Papers using LIMK1 antibodies
A role of LIM kinase 1/cofilin pathway in regulating endocytic trafficking of EGF receptor in human breast cancer cells
Supplier
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
ROCK inhibition prevents early mouse embryo development.
New
Sun et al., Nanjing, China. In Histochem Cell Biol, Aug 2014
Moreover, after ROCK inhibition with Y-27632, the phosphorylation levels of LIMK1/2, a downstream molecule of ROCK, were decreased at blastomere membranes.
Retrograde BMP signaling modulates rapid activity-dependent synaptic growth via presynaptic LIM kinase regulation of cofilin.
New
Littleton et al., Cambridge, United States. In J Neurosci, Apr 2014
In a parallel pathway, we find that the BMP type II receptor Wit signals through the effector protein LIM domain kinase 1 (Limk) to regulate bouton budding.
MeCP2 suppresses nuclear microRNA processing and dendritic growth by regulating the DGCR8/Drosha complex.
New
Qiu et al., Shanghai, China. In Dev Cell, Apr 2014
Protein targets of MeCP2-suppressed microRNAs include CREB, LIMK1, and Pumilio2, which play critical roles in neural development.
[LIM kinases and their roles in the nervous system].
New
Zhang et al., Hangzhou, China. In Zhejiang Da Xue Xue Bao Yi Xue Ban, Jan 2014
LIM kinase-1 (LIMK1) and LIM kinase-2 (LIMK2) are kinases that have serine/threonine and tyrosine dual specificity.
Multimodal effects of small molecule ROCK and LIMK inhibitors on mitosis, and their implication as anti-leukemia agents.
New
Uehara et al., Japan. In Plos One, Dec 2013
Pharmacological inhibition of LIMK also induced centrosome fragmentation similar to that by ROCK inhibitors.
β-Arrestin-kinase scaffolds: turn them on or turn them off?
Review
New
DeFea et al., Riverside, United States. In Wiley Interdiscip Rev Syst Biol Med, Mar 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.
Review
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.
GeneRIF
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.
HIV-1 proteins join the family of LIM kinase partners. New roads open up for HIV-1 treatment.
Review
Manetti, Siena, Italy. In Drug Discov Today, 2012
LIM kinases (LIMK) exert their functions by recruiting many macromolecular partners that could contribute to modulate LIMK activity in a positive or negative manner.
LIM kinase has a dual role in regulating lamellipodium extension by decelerating the rate of actin retrograde flow and the rate of actin polymerization.
GeneRIF
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.
p57(Kip2) and cancer: time for a critical appraisal.
Review
Della Ragione et al., Napoli, Italy. In Mol Cancer Res, 2011
p57(Kip2) also plays a critical role in controlling cytoskeletal organization and cell migration through its interaction with LIMK-1.
Actomyosin-mediated cellular tension drives increased tissue stiffness and β-catenin activation to induce epidermal hyperplasia and tumor growth.
Impact
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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
Cross talk between Smad, MAPK, and actin in the etiology of pulmonary arterial hypertension.
Review
West, Nashville, United States. In Adv Exp Med Biol, 2009
BMPR2 potentially signals through multiple immediate downstream pathways, including Smad, MAPK, LIM domain kinase 1 (LIMK) and dynein, light chain, Tctex-type 1 (TCTEX), v-src sarcoma viral oncogene homolog (SRC), and nuclear factor kappa-B (NFkB).
A brain-specific microRNA regulates dendritic spine development.
Impact
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.
Impact
GeneRIF
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.
Impact
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.
Impact
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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