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glucose increases p-cofilin by phosphorylating LIMK1 through activation of Rho/Rho kinase, probably due to diacylglycerol-sensitive PKC activation resulting from increased glucose influx.
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 (show MLXIP Proteins)-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 (show LIMK2 Proteins) expression and/or activity might contribute to AR function in prostate cancer via regulation of microtubule cytoskeletal dynamics.
CXCL12 (show CXCL12 Proteins)/CXCR4 (show CXCR4 Proteins) signaling has a role in docetaxel-induced microtubule stabilization via p21-activated kinase 4 (show PAK4 Proteins)-dependent activation of LIMK1
LIMK1 has a role in regulating human trophoblast invasion/differentiation and is down-regulated in preeclampsia
miR (show MLXIP Proteins)-20a is involved in the tumor inhibition of cutaneous squamous cell carcinoma by directly targeting LIMK1 gene.
miR (show MLXIP Proteins)-20a plays a role as a tumor suppressor in thyroid cancer cells and targets LIMK1
bone morphogenetic protein receptor II (BMPRII (show BMPR2 Proteins)) is a major regulator of LIMK1 in extending RGC axons, as expression of a BMPRII (show BMPR2 Proteins) lacking the LIMK1 binding region caused a dramatic shortening of the axons
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 (show CFL1 Proteins) 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 (show CREB1 Proteins) 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 (show CFL1 Proteins) regulator Lim domain kinase 1 (Limk1), bone morphogenetic proteins control the rate of commissural axonal growth.
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