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Myosin, light chain 2, regulatory, cardiac, slow

myosin light chain 2, MLC2v, MLC2, MYL2
Thus gene encodes the regulatory light chain associated with cardiac myosin beta (or slow) heavy chain. Ca+ triggers the phosphorylation of regulatory light chain that in turn triggers contraction. Mutations in this gene are associated with mid-left ventricular chamber type hypertrophic cardiomyopathy. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, Actin, HAD, V1a, FasT
Papers using myosin light chain 2 antibodies
Tea flavonoids and cardiovascular health.
Zhang Baohong, In PLoS ONE, 2009
... Rabbit anti-MLC2 (FL-172) antibody (against whole MRLC) was obtained from Santa Cruz Biotechnology, Inc ...
Domain analysis of alpha-actinin reveals new aspects of its association with F-actin during cytokinesis.
Hotchin Neil A., In PLoS ONE, 2009
... Polyclonal MLC2 antibody (catalog #: 3672) was purchased from Cell Signaling (Danvers, MA) ...
A role for the juxtamembrane cytoplasm in the molecular dynamics of focal adhesions.
Parsons Maddy, In PLoS ONE, 2008
... anti-β1 integrin (BD Biosciences); mouse anti-alpha tubulin, rabbit anti-calnexin and rabbit anti-fibronectin (Sigma Aldrich); rabbit anti-phospho-myosin light chain 2 (Ser19) (Cell Signaling Technology, Inc., Danvers, MA), ...
PDZRhoGEF and myosin II localize RhoA activity to the back of polarizing neutrophil-like cells
Bourne Henry R. et al., In The Journal of Cell Biology, 2004
... Mouse monoclonal antibody against myosin light chain 2 phosphorylated at S19 (p-MLC2) was from Cell Signaling Technology ...
Two-photon molecular excitation imaging of Ca2+ transients in Langendorff-perfused mouse hearts.
Rutherford Suzannah, In PLoS ONE, 2002
... MLC2v-Cre/ZEG double heterozygous transgenic mice were generated by ...
Papers on myosin light chain 2
Increase in cell motility by carbon ion irradiation via the Rho signaling pathway and its inhibition by the ROCK inhibitor Y-27632 in lung adenocarcinoma A549 cells.
Nakano et al., Maebashi, Japan. In J Radiat Res (tokyo), Jul 2014
The expression of myosin light chain 2 (MLC2) and the phosphorylation of MLC2 at Ser19 (P-MLC2-S19) were analyzed by Western blot.
Mycophenolic acid mediated disruption of the intestinal epithelial tight junctions.
Asif et al., Göttingen, Germany. In Exp Cell Res, May 2014
Phosphorylation of myosin light chain 2 (MLC2) is associated with epithelial tight junction (TJ) modulation which leads to defective epithelial barrier function, and has been implicated in GI diseases.
Phospho-GlcNAc modulation of slow MLC2 during soleus atrophy through a multienzymatic and sarcomeric complex.
Bastide et al., Villeneuve-d'Ascq, France. In Pflugers Arch, Mar 2014
Among the regulatory proteins of skeletal muscle contraction, the myosin light chain 2 (MLC2) can undergo both types of post-translational modification.
Serine carboxypeptidase SCPEP1 and Cathepsin A play complementary roles in regulation of vasoconstriction via inactivation of endothelin-1.
Pshezhetsky et al., Montréal, Canada. In Plos Genet, Feb 2014
The DD mice had a reduced degradation rate of ET-1 in the blood whereas their cultured arterial vascular smooth muscle cells showed increased ET-1-dependent phosphorylation of myosin light chain 2. Together, our results define the biological role of mammalian serine carboxypeptidase Scpep1 and suggest that Scpep1 and CathA together participate in the control of ET-1 regulation of vascular tone and hemodynamics.
A two-stage association study suggests BRAP as a susceptibility gene for schizophrenia.
Zhang et al., Wuxi, China. In Plos One, Dec 2013
Furthermore, cis-eQTL analysis indicates that rs3782886 genotypes are associated with mRNA levels of aldehyde dehydrogenase 2 family (ALDH2) (P  =  0.0039) and myosin regulatory light chain 2 (MYL2) (P < 1.0E-4).
Mechanotransduction and YAP-dependent matrix remodelling is required for the generation and maintenance of cancer-associated fibroblasts.
Sahai et al., London, United Kingdom. In Nat Cell Biol, Jun 2013
YAP regulates the expression of several cytoskeletal regulators, including ANLN and DIAPH3, and controls the protein levels of MYL9 (also known as MLC2).
Intracellular regulation of matrix metalloproteinase-2 activity: new strategies in treatment and protection of heart subjected to oxidative stress.
Sawicki, Saskatoon, Canada. In Scientifica (cairo), 2012
One such mechanism involves the proteolytic degradation of contractile proteins, such as troponin I (TnI), myosin heavy chain, titin, and the myosin light chains (MLC1 and MLC2) by matrix metalloproteinase-2 (MMP-2).
Gene duplication and conversion events shaped three homologous, differentially expressed myosin regulatory light chain (MLC2) genes.
Wansink et al., Nijmegen, Netherlands. In Eur J Cell Biol, 2012
MLC2 isoforms play a role in tumorigenesis.
AMPK regulates mitotic spindle orientation through phosphorylation of myosin regulatory light chain.
Marcus et al., Atlanta, United States. In Mol Cell Biol, 2012
AMPK mediates spindle pole-associated pMRLC(ser19) to control spindle orientation via regulation of actin cortex-astral microtubule attachments
Effect of selenium on the interaction between daunorubicin and cardiac myosin.
Wang et al., Wuhan, China. In Biol Trace Elem Res, 2012
Results show that the binding force between selenium and cardiac myosin (CM), which consists of two heavy chains (MHC) and two pairs of light chains: MLC1 and MLC2, was 100 times stronger than that of daunorubicin (DNR) and CM.
Mouse and computational models link Mlc2v dephosphorylation to altered myosin kinetics in early cardiac disease.
Chen et al., Los Angeles, United States. In J Clin Invest, 2012
Mlc2 phosphorylation regulates actin-myosin interactions in striated muscle contraction. It is important for feedback control of calcium-dependent thin-filament activation. Dephosphorylation can play a critical role in heart failure.
Smooth muscle myosin light chain kinase efficiently phosphorylates serine 15 of cardiac myosin regulatory light chain.
Ajtai et al., Rochester, United States. In Biochem Biophys Res Commun, 2012
These data demonstrate that smMLCK is a specific and efficient kinase for the in vitro phosphorylation of MYL2, cardiac, and smooth muscle myosin.
Myocardin-related transcription factors and SRF are required for cytoskeletal dynamics and experimental metastasis.
Treisman et al., London, United Kingdom. In Nat Cell Biol, 2009
Two of these, MYH9 (NMHCIIa) and MYL9 (MLC2), are also required for invasion and lung colonization.
The slow force response to stretch in atrial and ventricular myocardium from human heart: functional relevance and subcellular mechanisms.
Pieske et al., Graz, Austria. In Prog Biophys Mol Biol, 2008
Furthermore, stretch increased phosphorylation of atrial myosin light chain 2 (MLC2) and inhibition of myosin light chain kinase (MLCK) attenuated the SFR in atrium and ventricle.
Shared genetic causes of cardiac hypertrophy in children and adults.
Seidman et al., Boston, United States. In N Engl J Med, 2008
We sequenced eight genes: MYH7, MYBPC3, TNNT2, TNNI3, TPM1, MYL3, MYL2, and ACTC.
Energy-dependent regulation of cell structure by AMP-activated protein kinase.
Chung et al., Taejŏn, South Korea. In Nature, 2007
Interestingly, the regulatory site of non-muscle myosin regulatory light chain (MRLC; also known as MLC2) was directly phosphorylated by AMPK.
Evaluation of the cardiac isoform of alpha2-macroglobulin as a factor inducing cardiac hypertrophy.
Jeejabai et al., Madurai, India. In Methods Mol Med, 2004
It was accompanied by enlargement of cardiac myocytes and induction of beta-myosin heavy chain (MHC) and MLC-2 gene expression.
[Pattern of skeletal muscle differentiation in fish: molecular and biological approaches].
Zinov'eva et al., In Izv Akad Nauk Ser Biol, 2004
Synthesis of the main contractile proteins, primarily the components of myosin molecule--heavy chain (MHC) and individual isoforms of light chains (MLC1, MLC2, and MLC3)--are encoded by different genes during different ontogenetic stages.
[Familial hypertrophic cardiomyopathy: genes, mutations and animal models. A review].
Padrón et al., Caracas, Venezuela. In Invest Clin, 2004
Molecular genetic studies have identified eleven genes that code proteins of the sarcomere that are associated with the HCM; the beta-myosin heavy chain gene (MYH7), alpha-myosin heavy chain (MYH6), cardiac troponin T (TNNT2); cardiac troponin C (TNNC1), alpha-tropomyosin (TPM1), myosin binding protein-C (MYBPC3), cardiac troponin (TNNI3), essential and regulatory light chain genes (MYL3 and MYL2, respectively), cardiac alpha-actin gene (ACTC) and titin (TTN).
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