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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 25 Jan 2016.

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
KIF17 regulates RhoA-dependent actin remodeling at epithelial cell-cell adhesions.
Kreitzer et al., Villejuif, France. In J Cell Sci, 12 Feb 2016
Inhibition of Rho or its effector ROCK, or expression of LIMK1 kinase-dead or activated cofilin(S3A) inhibited KIF17-induced junctional actin accumulation.
LIM kinase activity is required for microtubule organising centre positioning in mouse oocyte meiosis.
Ma et al., In Reprod Fertil Dev, 06 Feb 2016
UNASSIGNED: LIM kinase 1 (LIMK1) activity is essential for cell migration and cell cycle progression.
A novel and selective inhibitor of PKC ζ potently inhibits human breast cancer metastasis in vitro and in mice.
Yang et al., Tianjin, China. In Tumour Biol, 05 Feb 2016
also inhibited cells adhesion and actin polymerization through attenuating the phosphorylations of integrin β1, LIMK, and cofilin, which might be the downstream effectors of PKC ζ-mediated chemotaxis in MDA-MB-231 cells.
Effects of sevoflurane exposure during late pregnancy on brain development of offspring mice.
Mizobuchi et al., Kōbe, Japan. In Paediatr Anaesth, 31 Jan 2016
The mRNA expression levels of caspase-3, brain derived neurotrophic factor (BDNF), nerve growth factor (NGF), and LIM kinase-1 (LIMK-1) were measured in fetal whole brain and 8-week-old hippocampus sections.
Mitigation of arsenic-induced acquired cancer phenotype in prostate cancer stem cells by miR-143 restoration.
Tokar et al., United States. In Toxicol Appl Pharmacol, 22 Jan 2016
The anticancer effects of miR-143 overexpression appeared to be mediated by targeting and inhibiting LIMK1 protein, and the phosphorylation of cofilin, a LIMK1 substrate.
Zerumbone Suppresses Osteopontin-Induced Cell Invasion Through Inhibiting the FAK/AKT/ROCK Pathway in Human Non-Small Cell Lung Cancer A549 Cells.
Lee et al., Seoul, South Korea. In J Nat Prod, 17 Jan 2016
Compound 1 effectively inhibited OPN-induced protein expression of ROCK1, the phosphorylation of LIM kinase 1 and 2 (LIMK1/2), and cofilin.
Phospholipase C-η2 interacts with nuclear and cytoplasmic LIMK-1 during retinoic acid-stimulated neurite growth.
Stewart et al., Miami, United States. In Histochem Cell Biol, 15 Jan 2016
Furthermore in these compartments (and also in growing neurites), a proximity ligand assay revealed that PLCη2 specifically interacts with LIMK-1 in Neuro2A cells.
The stressed cytoskeleton: How actin dynamics can shape stress-related consequences on synaptic plasticity and complex behavior.
Müller et al., Mainz, Germany. In Neurosci Biobehav Rev, 12 Jan 2016
Identified stress-responsive ABPs include: tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1), ADF/cofilin, LIMK1, caldesmon and myosin VI.
LIM Kinase, a Newly Identified Regulator of Presynaptic Remodeling by Rod Photoreceptors After Injury.
Townes-Anderson et al., In Invest Ophthalmol Vis Sci, 01 Jan 2016
This study examines the role of LIM kinase (LIMK), a component of RhoA and Rac pathways, in the presynaptic structural remodeling of rod photoreceptors.
Distribution of LIM domain kinase 1 in the olfactory bulb, cerebral cortex, hippocampus, and cerebellum of the App/PS+/- mice.
Ren et al., Kaifeng, China. In Genet Mol Res, 2014
LIM domain kinase 1 (LIMK1), an actin-binding kinase, can phosphorylate and inactivate its substrates, and can regulate long-term memory and synaptic plasticity.
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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