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Myosin light chain kinase

myosin light chain kinase, MLCK
This gene, a muscle member of the immunoglobulin gene superfamily, encodes myosin light chain kinase which is a calcium/calmodulin dependent enzyme. This kinase phosphorylates myosin regulatory light chains to facilitate myosin interaction with actin filaments to produce contractile activity. This gene encodes both smooth muscle and nonmuscle isoforms. In addition, using a separate promoter in an intron in the 3' region, it encodes telokin, a small protein identical in sequence to the C-terminus of myosin light chain kinase, that is independently expressed in smooth muscle and functions to stabilize unphosphorylated myosin filaments. A pseudogene is located on the p arm of chromosome 3. Four transcript variants that produce four isoforms of the calcium/calmodulin dependent enzyme have been identified as well as two transcripts that produce two isoforms of telokin. Additional variants have been identified but lack full length transcripts. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Actin, Rhodopsin, V1a, CAN, HAD
Papers using myosin light chain kinase antibodies
Nuclear actin dynamics–from form to function.
Tyagi Anil Kumar, In PLoS ONE, 2007
... Phospho-specific and nonphospho-specific antibodies against MLCK and the catalytic subunit of MLCP (MYPT) were obtained from Santa Cruz Biotechnology.
Papers on myosin light chain kinase
Se Enhances MLCK Activation by Regulating Selenoprotein T (SelT) in the Gastric Smooth Muscle of Rats.
Guo et al., Wuhan, China. In Biol Trace Elem Res, Feb 2016
The myosin light chain kinase (MLCK) and myosin light chain (MLC) play key roles in the contraction process of smooth muscle.
Enzymatic changes in myosin regulatory proteins may explain vasoplegia in terminally ill patients with sepsis.
Ouyang et al., Binzhou, China. In Biosci Rep, Feb 2016
Down regulation of myosin light chain kinase and upregulation of myosin light chain kinase may explain the loss of tone and failure to mount contractile response in vivo during circulation.
Epithelial Nuclear Factor-x03BA;B Activation in Inflammatory Bowel Diseases and Colitis-Associated Carcinogenesis.
Watanabe et al., In Digestion, Feb 2016
Myosin light chain kinase (MLCK) is suggested to be associated with epithelial permeability via TNF signaling.
The N-terminal acetyltransferase Naa10/ARD1 does not acetylate lysine residues.
Marmorstein et al., United States. In J Biol Chem, Feb 2016
Surprisingly, recent reports claim that Naa10 may also acetylate lysine residues of diverse targets, including methionine sulfoxide reductase A (MSRA), myosin light chain kinase (MLCK), and Runt-related transcription factor 2 (Runx2).
Beyond Ussing's chambers: Contemporary thoughts on integration of transepithelial transport.
Turner et al., Chicago, United States. In Am J Physiol Cell Physiol, Jan 2016
Intermediates in this process include activation of p38 MAPK, the apical Na(+)-H(+) exchanger NHE3, and myosin light chain kinase (MLCK).
Molecular mechanisms in lipopolysaccharide-induced pulmonary endothelial barrier dysfunction.
Kou et al., Nanjing, China. In Int Immunopharmacol, Dec 2015
As for barrier-disruption, the activation of myosin light chain kinase (MLCK), RhoA and tyrosine kinases; increase of calcium influx; and apoptosis of the endothelium lead to an elevation of lung endothelial permeability.
Altered expression levels of occludin, claudin-1 and myosin light chain kinase in the common bile duct of pediatric patients with pancreaticobiliary maljunction.
Wang et al., Suzhou, China. In Bmc Gastroenterol, Dec 2015
Total protein extracts of common bile duct were analyzed by Western blotting assays to examine expression of occludin, claudin-1 and myosin light chain kinase (MLCK).
A role for the Ca(2+)-dependent tyrosine kinase Pyk2 in tonic depolarization-induced vascular smooth muscle contraction.
Walsh et al., Calgary, Canada. In J Muscle Res Cell Motil, Aug 2015
The initial phasic contractile response is due to opening of voltage-gated Ca(2+) channels and entry of extracellular Ca(2+), which binds to calmodulin, leading to activation of myosin light chain kinase, phosphorylation of the regulatory light chains of myosin II at Ser19 and cross-bridge cycling.
Immunosuppressant MPA Modulates Tight Junction through Epigenetic Activation of MLCK/MLC-2 Pathway via p38MAPK.
Asif et al., Göttingen, Germany. In Front Physiol, 2014
Recently, we reported the MPA induced tight junctions (TJs) deregulation which involves MLCK/MLC-2 pathway.
2D DIGE Does Not Reveal all: A Scotopic Report Suggests Differential Expression of a Single "Calponin Family Member" Protein for Tetany of Sphincters!
Chaudhury, Little Rock, United States. In Front Med (lausanne), 2014
Earlier studies have shown differences in expression of different proteins like Rho-associated protein kinase II, myosin light chain kinase, myosin phosphatase, and protein kinase C between IAS and RSM.
Molecular mechanism of telokin-mediated disinhibition of myosin light chain phosphatase and cAMP/cGMP-induced relaxation of gastrointestinal smooth muscle.
Somlyo et al., Charlottesville, United States. In J Biol Chem, 2012
Molecular mechanism of telokin-mediated disinhibition of myosin light chain phosphatase and cAMP/cGMP-induced relaxation of gastrointestinal smooth muscle.
Novel role for non-muscle myosin light chain kinase (MLCK) in hyperoxia-induced recruitment of cytoskeletal proteins, NADPH oxidase activation, and reactive oxygen species generation in lung endothelium.
Natarajan et al., Chicago, United States. In J Biol Chem, 2012
MLCK is essential for the translocation and association of cortactin and p47phox.
Enterocyte STAT5 promotes mucosal wound healing via suppression of myosin light chain kinase-mediated loss of barrier function and inflammation.
Han et al., Cincinnati, United States. In Embo Mol Med, 2012
Deletion of MLCK restored intestinal barrier function in STAT5 knockout mice, and facilitated mucosal wound healing(MLCK)
Hypermethylated FAM5C and MYLK in serum as diagnosis and pre-warning markers for gastric cancer.
Liu et al., Shanghai, China. In Dis Markers, 2011
Hypermethylated FAM5C and MYLK in serum are strongly associated with the development of gastric cancer and can be used as potential biomarkers for diagnosis and pre-warning.
Myosin light-chain kinase is necessary for membrane homeostasis in cochlear inner hair cells.
Zhu et al., Nanjing, China. In Plos One, 2011
Myosin light-chain kinase is necessary for maintaining the membrane stability of inner hair cells.
A family of protein-deglutamylating enzymes associated with neurodegeneration.
Janke et al., Montpellier, France. In Cell, 2010
Accordingly, we show that these enzymes convert detyrosinated tubulin into Δ2-tubulin and also modify other substrates, including myosin light chain kinase 1.
Non-muscle myosin IIA is a functional entry receptor for herpes simplex virus-1.
Kawaguchi et al., Tokyo, Japan. In Nature, 2010
A specific inhibitor of myosin light chain kinase, which regulates NM-IIA by phosphorylation, reduced the redistribution of NMHC-IIA as well as HSV-1 infection in cell culture and in a murine model for herpes stromal keratitis.
A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow.
Leung et al., Singapore, Singapore. In Cell, 2008
This binding leads to MRCK activation and its phosphorylation of MYO18A, independently of ROK and MLCK.
Periodic lamellipodial contractions correlate with rearward actin waves.
Sheetz et al., New York City, United States. In Cell, 2004
In spreading and migrating cells we find local periodic contractions of lamellipodia that depend on matrix rigidity, fibronectin binding and myosin light chain kinase (MLCK).
FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly.
Horwitz et al., Charlottesville, United States. In Nat Cell Biol, 2004
Using these assays, we show that kinases and adaptor molecules, including focal adhesion kinase (FAK), Src, p130CAS, paxillin, extracellular signal-regulated kinase (ERK) and myosin light-chain kinase (MLCK) are critical for adhesion turnover at the cell front, a process central to migration.
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