The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Mylk  -  myosin, light polypeptide kinase

Mus musculus

Synonyms: 9530072E15Rik, A930019C19Rik, AW489456, KRP, Kinase-related protein, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Mylk

  • The data also indicate that inhibition of epithelial MLCK may be an effective non-immunosuppressive therapy for treatment of immune-mediated intestinal disease [1].
  • The effects of giardiasis on epithelial permeability in vivo remain unknown, and the role of T cells and myosin light chain kinase (MLCK) in altered intestinal barrier function is unclear [2].
  • When added to contracting solution at the peak of a contracture, anti-MLCK Fab elicited a relaxation that was complete in about 120 minutes despite the presence of Ca2+ [3].
  • Rapid response of cardiac obscurin gene cluster to aortic stenosis: differential activation of Rho-GEF and MLCK and involvement in hypertrophic growth [4].

Psychiatry related information on Mylk


High impact information on Mylk

  • 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) [6].
  • A specific precipitating antibody against chicken gizzard myosin light chain kinase (MLCK) has been produced in rabbits [7].
  • Indirect immunofluorescent microscopy of non-muscle tissue culture cells revealed MLCK to be localized in the spindle apparatus and midbody of mitotic cells and on the stress fibers and in the nucleolus of interphase cells [7].
  • In myofibrils isolated from skeletal and cardiac muscle, anti-MLCK decorated the actin-containing I bands of the sarcomere [7].
  • These results are consistent with the suggestion that MLCK and calmodulin are intermediates in the regulation of cell motility by calcium [7].

Biological context of Mylk


Anatomical context of Mylk


Associations of Mylk with chemical compounds


Physical interactions of Mylk

  • HFH-1 does not disrupt serum response factor binding to an adjacent CArG box within the telokin promoter, implying that HFH-1 must compete with other unidentified trans-activators to mediate repression [11].
  • Results from gel mobility shift assays demonstrated that Hoxa10-1, Hoxa10-2, and Hoxb8 bind directly to multiple sites in the telokin promoter [16].
  • Gel mobility shift assays demonstrate that GATA-6 binds to a consensus site adjacent to the CArG box in the telokin promoter [17].

Enzymatic interactions of Mylk

  • 208-kDa MLCK phosphorylates 20-kDa myosin light chains in a Ca2+/calmodulin-dependent manner, consistent with it being a member of the MLCK family [18].

Regulatory relationships of Mylk


Other interactions of Mylk


Analytical, diagnostic and therapeutic context of Mylk

  • Using a complementary chemical biology approach, we developed a new class of small-molecule MLCK inhibitor based on the pharmacologically privileged aminopyridazine and found that a single i.p. injection of the inhibitor protected WT mice against ALI and death from mechanical ventilation complications [13].
  • Gel mobility shift and chromatin immunoprecipitation assays revealed that Elk-1 binds to a nonconsensus binding site in the telokin promoter and Elk-1 binding is dependent on serum response factor (SRF) binding to a nearby CArG box [22].
  • Northern blot, Western blot, and histochemical studies show that the 220-kDa MLCK is widely expressed during development as well as in several adult smooth muscle and nonmuscle tissues [23].
  • We also show by immunoblotting and immunohistochemistry of various mouse tissues that the antibody used in this study has cross-reactivity to MLCK of various muscle and non-muscle tissues of the mouse [21].
  • MLCK levels and activity are increased in various animal models of disease and in human clinical disease samples [24].


  1. Epithelial myosin light chain kinase-dependent barrier dysfunction mediates T cell activation-induced diarrhea in vivo. Clayburgh, D.R., Barrett, T.A., Tang, Y., Meddings, J.B., Van Eldik, L.J., Watterson, D.M., Clarke, L.L., Mrsny, R.J., Turner, J.R. J. Clin. Invest. (2005) [Pubmed]
  2. Intestinal infection with Giardia spp. reduces epithelial barrier function in a myosin light chain kinase-dependent fashion. Scott, K.G., Meddings, J.B., Kirk, D.R., Lees-Miller, S.P., Buret, A.G. Gastroenterology (2002) [Pubmed]
  3. Effects of antibodies to myosin light chain kinase on contractility and myosin phosphorylation in chemically permeabilized smooth muscle. De Lanerolle, P., Strauss, J.D., Felsen, R., Doerman, G.E., Paul, R.J. Circ. Res. (1991) [Pubmed]
  4. Rapid response of cardiac obscurin gene cluster to aortic stenosis: differential activation of Rho-GEF and MLCK and involvement in hypertrophic growth. Borisov, A.B., Raeker, M.O., Kontrogianni-Konstantopoulos, A., Yang, K., Kurnit, D.M., Bloch, R.J., Russell, M.W. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  5. A fluorescent protein biosensor of myosin II regulatory light chain phosphorylation reports a gradient of phosphorylated myosin II in migrating cells. Post, P.L., DeBiasio, R.L., Taylor, D.L. Mol. Biol. Cell (1995) [Pubmed]
  6. Periodic lamellipodial contractions correlate with rearward actin waves. Giannone, G., Dubin-Thaler, B.J., Döbereiner, H.G., Kieffer, N., Bresnick, A.R., Sheetz, M.P. Cell (2004) [Pubmed]
  7. Production and characterization of an antibody to myosin light chain kinase and intracellular localization of the enzyme. Guerriero, V., Rowley, D.R., Means, A.R. Cell (1981) [Pubmed]
  8. The myosin light chain kinase gene is not duplicated in mouse: partial structure and chromosomal localization of Mylk. Giorgi, D., Ferraz, C., Mattéi, M.G., Demaille, J., Rouquier, S. Genomics (2001) [Pubmed]
  9. Activation of the smooth muscle-specific telokin gene by thyrotroph embryonic factor (TEF). Zhou, J., Hoggatt, A.M., Herring, B.P. J. Biol. Chem. (2004) [Pubmed]
  10. Smooth muscle of telokin-deficient mice exhibits increased sensitivity to Ca2+ and decreased cGMP-induced relaxation. Khromov, A.S., Wang, H., Choudhury, N., McDuffie, M., Herring, B.P., Nakamoto, R., Owens, G.K., Somlyo, A.P., Somlyo, A.V. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  11. Hepatocyte nuclear factor-3 homologue 1 (HFH-1) represses transcription of smooth muscle-specific genes. Hoggatt, A.M., Kriegel, A.M., Smith, A.F., Herring, B.P. J. Biol. Chem. (2000) [Pubmed]
  12. Smooth muscle myosin light chain kinase expression in cardiac and skeletal muscle. Herring, B.P., Dixon, S., Gallagher, P.J. Am. J. Physiol., Cell Physiol. (2000) [Pubmed]
  13. Protein kinase involved in lung injury susceptibility: evidence from enzyme isoform genetic knockout and in vivo inhibitor treatment. Wainwright, M.S., Rossi, J., Schavocky, J., Crawford, S., Steinhorn, D., Velentza, A.V., Zasadzki, M., Shirinsky, V., Jia, Y., Haiech, J., Van Eldik, L.J., Watterson, D.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  14. Deletion of MLCK210 induces subtle changes in vascular reactivity but does not affect cardiac function. Ohlmann, P., Tesse, A., Loichot, C., Ralay Ranaivo, H., Roul, G., Philippe, C., Watterson, D.M., Haiech, J., Andriantsitohaina, R. Am. J. Physiol. Heart Circ. Physiol. (2005) [Pubmed]
  15. Real-time evaluation of myosin light chain kinase activation in smooth muscle tissues from a transgenic calmodulin-biosensor mouse. Isotani, E., Zhi, G., Lau, K.S., Huang, J., Mizuno, Y., Persechini, A., Geguchadze, R., Kamm, K.E., Stull, J.T. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  16. Regulation of smooth muscle-specific gene expression by homeodomain proteins, Hoxa10 and Hoxb8. El-Mounayri, O., Triplett, J.W., Yates, C.W., Herring, B.P. J. Biol. Chem. (2005) [Pubmed]
  17. GATA-6 can act as a positive or negative regulator of smooth muscle-specific gene expression. Yin, F., Herring, B.P. J. Biol. Chem. (2005) [Pubmed]
  18. Expression of a novel myosin light chain kinase in embryonic tissues and cultured cells. Gallagher, P.J., Garcia, J.G., Herring, B.P. J. Biol. Chem. (1995) [Pubmed]
  19. Contractile units in stress fibers of fetal human astroglia in tissue culture. Abd-el-Basset, E.M., Fedoroff, S. J. Chem. Neuroanat. (1994) [Pubmed]
  20. Telokin expression is restricted to smooth muscle tissues during mouse development. Herring, B.P., Lyons, G.E., Hoggatt, A.M., Gallagher, P.J. Am. J. Physiol., Cell Physiol. (2001) [Pubmed]
  21. Immunocytochemical detection and spatial distribution of myosin light-chain kinase in preimplantation mouse embryos. Kabir, N., Yamamura, H., Niki, I., Iida, Y., Uzzaman, M., Sarkar, D., Hayasaka, S., Takagishi, Y., Inouye, M., Hidaka, H. J. Exp. Zool. (1997) [Pubmed]
  22. Smooth muscle-specific genes are differentially sensitive to inhibition by Elk-1. Zhou, J., Hu, G., Herring, B.P. Mol. Cell. Biol. (2005) [Pubmed]
  23. 220- and 130-kDa MLCKs have distinct tissue distributions and intracellular localization patterns. Blue, E.K., Goeckeler, Z.M., Jin, Y., Hou, L., Dixon, S.A., Herring, B.P., Wysolmerski, R.B., Gallagher, P.J. Am. J. Physiol., Cell Physiol. (2002) [Pubmed]
  24. Development of a novel bioavailable inhibitor of the calmodulin-regulated protein kinase MLCK: A lead compound that attenuates vascular leak. Behanna, H.A., Watterson, D.M., Ranaivo, H.R. Biochim. Biophys. Acta (2006) [Pubmed]
WikiGenes - Universities