gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Sep 2015.

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
Association of N-cadherin levels and downstream effectors of Rho GTPases with dendritic spine loss induced by chronic stress in rat hippocampal neurons.
Fiedler et al., Santiago, Chile. In J Neurosci Res, 31 Oct 2015
Via their effector LIM kinase (LIMK), RhoA and ras-related C3 botulinum toxin substrate 1 (RAC) GTPases phosphorylate and inhibit cofilin, an actin-depolymerizing molecule, favoring spine growth.
A Novel Recurrent Breakpoint Responsible for Rearrangements in the Williams-Beuren Region.
Tizzano et al., Barcelona, Spain. In Cytogenet Genome Res, 18 Oct 2015
We found 2 patients with a deletion and 1 patient with a duplication in this region sharing a common breakpoint located between the LIMK1 and EIF4H(WBSCR1) genes.
Discovery, development and SAR of aminothiazoles as LIMK inhibitors with cellular anti-invasive properties.
Olson et al., In J Med Chem, 10 Oct 2015
UNASSIGNED: As part of a program to develop a small molecule inhibitor of LIMK, a series of aminothiazole inhibitors were discovered by high throughput screening.
Thymosin β4 induces proliferation, invasion, and epithelial-to-mesenchymal transition of oral squamous cell carcinoma.
Hong et al., Seoul, South Korea. In Amino Acids, 15 Sep 2015
Tβ4 overexpression augmented in vitro invasion and MMP-2 activity and enhanced the phosphorylation of paxillin and cortactin and expression of LIMK1.
[Influence of limk1 Gene Polymorphism on Learning Acquisition and Memory Formation with pCREB Distribution and Aggregate Formation in Neuromuscular Junctions in Drosophila melanogaster].
Savateeva-Popova et al., In Genetika, Jun 2015
We have shown previously that the polymorphic structure of the limk1 gene in drosophila leads to changes in LIMK1 content and to defects in courtship behavior, sound production, and learning/memory.
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.
HIV-1 proteins join the family of LIM kinase partners. New roads open up for HIV-1 treatment.
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.
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.
share on facebooktweetadd +1mail to friends