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Results show that silencing LIMK1 leads to defective spindle organization and centrosome integrity. Dynein light intermediate chains were identified as the downstream mediators of LIMK1 in the maintenance of centrosome integrity.
Results indicated that LIM kinase 1 was a potential target molecule for the inhibitory effect of diallyl disulfide on colon cancer cell migration and invasion.
Once activated, c-Abl kinase regulated the activity of Vav1, which further affected Rac1/PAK1/LIMK1/cofilin signaling pathway.
findings suggest that miR-519d-3p regulates the LIMK1/CFL1 pathway in breast cancer
The present study demonstrates that miR-145 plays an important role in inhibiting cell migration by directly targeting PAK4, and identifies miR-145-PAK4-LIMK1-cofilin as a novel regulatory pathway that contributed to colorectal cancer metastasis.
In turn, LIMK1 and LIMK2 are required for MT1-MMP-dependent matrix degradation and cell invasion in a three-dimensional type I collagen environment.
increased BMPR2 signal transduction is linked to fragile X syndrome (FXS) and that the BMPR2-LIMK1 pathway is a putative therapeutic target in patients with FXS and possibly other forms of autism
Report structural basis for noncanonical substrate recognition of cofilin-1/LIMK1 to regulation actin cytoskeleton dynamics.
LIMK1 expression is negatively regulated in granular layers-negative psoriatic epidermis or IL-22/IL-24-treated hyperproliferative reconstituted epidermis. These findings suggest a novel regulatory mechanism and a potent role of LIMK1 in psoriatic epidermis.
Therefore, miR-138/LIMK1/cofilin may be considered a potential therapeutic target for the treatment of non-small cell lung cancer
This study showed that LIMK1 messenger RNA levels was significantly upregulated in subjects with schizophrenia in laminar and cellular samples.
Gene knockdown/rescue experiments reveal that LIMK1 palmitoylation is essential for normal spine actin polymerization, for spine-specific structural plasticity and for long-term spine stability.
LIMK1 is overexpressed in endometrial stromal cells.
Data show that the downregulation of miR-138 induced the upregulation of Limk1 in ovarian cancer (OC) cells suggesting that these 2 genes may play a key role in the migration and invasion of OC cells.
LIMK1 is overexpressed in gastric cancer.
Results show that in addition to a potential role in promoting metastasis, changes in LIMK1 and LIMK2 expression and/or activity might contribute to AR function in prostate cancer via regulation of microtubule cytoskeletal dynamics.
CXCL12/CXCR4 signaling has a role in docetaxel-induced microtubule stabilization via p21-activated kinase 4-dependent activation of LIMK1
LIMK1 has a role in regulating human trophoblast invasion/differentiation and is down-regulated in preeclampsia
miR-20a is involved in the tumor inhibition of cutaneous squamous cell carcinoma by directly targeting LIMK1 gene.
miR-20a plays a role as a tumor suppressor in thyroid cancer cells and targets LIMK1
bone morphogenetic protein receptor II (BMPRII) is a major regulator of LIMK1 in extending RGC axons, as expression of a BMPRII lacking the LIMK1 binding region caused a dramatic shortening of the axons
results demonstrate an important role for LIMKs in central sensitization and the development of chronic pain
The spontaneous autosomal recessive mouse 'peroneal muscular atrophy' mutant (PMA) is a faithful morphological model of human clubfoot. The pma mutation was mapped and a candidate gene encoding LIM-domain kinase 1 (Limk1) identified, which is upregulated in mutant lateral motor neurons.
High LIMK1 expression is associated with aberrant synaptic development in mouse and Drosophila models of Fragile X syndrome.
we define how ROCK/LIMK pathway regulates mast cell development and functions
LIMK1 negatively regulated neuronal migration by affecting the neuronal cytoskeleton and that its effects were partly mediated by cofilin phosphorylation
Social isolation resulted in up-regulation of Limk-1 mRNA expression in the cerebral cortex.
The data emphasize the importance of the PLCeta2 EF-hand domain and articulation of PLCeta2 with LIMK-1 in regulating neuritogenesis.
Our study indicates that there is a connection between LIMK1 and AD in the mouse model of AD.
Neuroligin 1 regulates spines and synaptic plasticity via LIMK1/cofilin-mediated actin reorganization.
LIMK1 and Cofilin phosphorylation depends on PKA and is essential for mouse sperm acrosomal exocytosis
These results provide strong evidence that LIMK1 deletion is sufficient to lead to a long-term memory deficit and that this deficit is attributable to CREB hypofunction.
the conserved region in the LIMK1 3' UTR is involved in regulating LIMK1 expression at the post-transcriptional level
LIMK1 plays a novel role in selectively mediating GPIb-IX-dependent TXA2 synthesis and thrombosis.
data support the hypothesis that LIMK1 is required for normal osteoblast differentiation. In addition, its absence leads to increased cytoskeletal remodeling and bone resorption in osteoclasts
LIMK1 has a dual role in regulating lamellipodium extension by decelerating actin retrograde flow and polymerization.
LIMK1 expression is more dynamic than previously reported, in particular at sites of tissue-tissue interactions guiding multiple developmental processes
By activating the cofilin regulator Lim domain kinase 1 (Limk1), bone morphogenetic proteins control the rate of commissural axonal growth.
Results suggest that constitutive activation of the Rho-ROCK-LIM kinase pathway by extracellular production of lysophosphatidic acid by the action of autotaxin is required to maintain the large size of lysosomes in visceral endoderm cells.
role in actin cytoskeletal regulation
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.
LIM domain kinase 1
, LIM motif-containing protein kinase
, LIM motif-containing protein kinase 1
, LIM-domain containing protein kinase 1
, LIM-domain containing, protein kinase 1