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Gene Review

MYH1B  -  myosin, heavy chain 1B, skeletal muscle...

Gallus gallus

Synonyms: MYH1, MYH2, MYH3, MYH4, MYH8
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Disease relevance of MYH3

  • Myosin heavy chains prepared from the pectoralis major and from the posterior latissimus dorsi of the same adult chicken exhibit different peptide maps when cleaved with Staphylococcus aureus V8 protease [1].
  • We synthesized the chicken skeletal myosin light chain in Escherichia coli and constructed mutants with substitutions within the Ca2+/Mg2+ binding site [2].
  • Here we report that myosin from vertebrate (chicken and rabbit skeletal) and molluscan (scallop adductor) striated muscles is cleaved in an unusual way with an enzyme from Pseudomonas aeruginosa [3].
  • These studies suggest that muscular dystrophy inhibits the myosin gene switching that normally occurs during muscle maturation [4].
  • We have expressed two truncated isoforms of chicken nonmuscle myosin II-B using the baculovirus expression system [5].

Psychiatry related information on MYH3


High impact information on MYH3

  • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state [7].
  • The crystal structures of an expressed vertebrate smooth muscle myosin motor domain (MD) and a motor domain-essential light chain (ELC) complex (MDE), both with a transition state analog (MgADP x AIF4-) in the active site, have been determined to 2.9 A and 3.5 A resolution, respectively [7].
  • The isoprotein-specific intracompartmental sorting of the three essential myosin light chains (LCs), the skeletal muscle LC-1f and LC-3f and the nonmuscle LC-3nm, was investigated [8].
  • Although ITP and GTP serve as myosin ATPase substrates, they do not cause BB contraction, myosin release, or phosphorylation [9].
  • Phosphorylation controls brush border motility by regulating myosin structure and association with the cytoskeleton [9].

Chemical compound and disease context of MYH3

  • Myocyte X melanoma heterokaryons ceased to express the skeletal muscle forms of myosin, desmin and creatine kinase, reinitiated DNA synthesis, and showed a loss of spontaneous fusion competence within 96 hr after their formation [10].
  • 1. The contractile speeds and tetanus/twitch ratios of the slow anterior latissimus dorsi (ALD) and fast posterior latissimus dorsi (PLD) muscles were studied during embryonic development and correlated with the type of myosin light chains present in these muscles as studied by one and two dimensional polyacrylamide gel electrophoresis [11].

Biological context of MYH3

  • Cloned mRNA sequences for two types of embryonic myosin heavy chains from chick skeletal muscle. I. DNA and derived amino acid sequence of light meromyosin [12].
  • All of the genes showed homologies in the nucleotide sequences which code for the globular head portion of the myosin protein while no extensive homologies were detected in the 5'-flanking sequences [13].
  • Although there is extensive homology in the chicken fast myosin rods, sequences within the hinge, within the central portion of the light meromyosin fragment, and at the carboxy terminus exhibit the largest number of amino acid substitutions [14].
  • We studied regulation of BB motility by analyzing myosin phosphorylation and its association with the cytoskeleton [9].
  • It identifies an epitope that is shared on adult and embryonic myosin, and detects two transitions in myosin expression during avian pectoralis myogenesis [15].

Anatomical context of MYH3

  • A more direct approach to the identity of the abundant class of myofibril mRNA indicates that it contains the templates for the synthesis of seven polypeptides that are synthesized in particularly large amounts in myogenic cultures, including myosin, actin and tropomyosin [16].
  • It is specific for an adult fast myosin epitope that is not detected in early developing pectoralis muscle [15].
  • Our results demonstrate that myosin associates with the cytoskeleton only when it is dephosphorylated [9].
  • Here we report similar photolabelling experiments with smooth muscle myosin (chicken gizzard) in which 3H-NANDP is trapped at the active site with vanadate and which show that both the heavy chains and the essential light chains are labelled [17].
  • Class-V myosin proceeds along actin filaments with large ( approximately 36 nm) steps [18].

Associations of MYH3 with chemical compounds

  • We have now confirmed these results and extended our observations to fibre bundles from which one or both of the regulatory light chains per myosin have been removed (by treatment with EDTA at 7 and 25 degrees C, respectively) and replaced by the corresponding light chains from other species [19].
  • When the aspartate residues at the first and sixth Ca2+ coordination positions are replaced by uncharged alanines, the light chains have a reduced Ca2+ binding capacity but still bind to scallop myosin with high affinity [2].
  • Adenosine 5'-O (3'-thiotriphosphate) only in the presence of Ca2+ induced irreversible Ca2+-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of 32P from [gamma-32P]adenosine triphosphate into the myosin light chains [20].
  • Here we investigated the role of myosins in retrograde flow, using two distinct modes of myosin inhibition: microinjection of NEM inactivated myosin S1 fragments, or treatment with 2,3-butanedione-2-monoxime, and inhibitor of myosin ATPase [21].
  • The major proteins remaining in the ghosts comigrate, on polyacrylamide gels in the presence of SDS, with chicken gizzard actin, myosin, filamin, and a 110-kdalton protein [22].

Physical interactions of MYH3


Enzymatic interactions of MYH3

  • MLCK is a calmodulin (CaM) regulated protein kinase that phosphorylates the light chain of myosin II [28].
  • Reversal of caldesmon binding to myosin with calcium-calmodulin or by phosphorylating caldesmon [29].
  • Mitogen-activated protein kinase activated protein (MAPKAP) kinase-2 was found to phosphorylate the regulatory light chain of myosin II (MRLC) in vitro in the absence of Ca2+/calmodulin [30].

Regulatory relationships of MYH3


Other interactions of MYH3

  • The derived amino acid sequence of clone 251 correlated well with sequences obtained by direct amino acid sequencing of adult rabbit back muscle myosin heavy chain protein (87% homology), as well as with cloned myosin heavy chain sequences from other species [12].
  • A chick embryonic myosin alkali light chain L23 gene that is expressed transiently at embryonic stages in chick skeletal, cardiac and smooth muscles and in brain continuously from embryo to adult stages, was isolated and characterized [35].
  • Caldesmon is a smooth muscle and nonmuscle regulatory protein that interacts with actin, myosin, tropomyosin, and calmodulin [36].
  • Native myosin-Va purified from chick brain, as well as the expressed globular tail domain of this myosin, but not head domain bound to microtubule-associated protein-free microtubules [37].
  • Two recombinant clones, lambda LC5 and lambda LC13, encompassing the entire regulatory myosin light chain 2 (MLC2A) gene of chicken heart muscle were isolated [38].

Analytical, diagnostic and therapeutic context of MYH3


  1. Myosin heavy chains from two different adult fast-twitch muscles have different peptide maps but identical mRNAs. Bandman, E., Matsuda, R., Strohman, R.C. Cell (1982) [Pubmed]
  2. Site-directed mutagenesis of the regulatory light-chain Ca2+/Mg2+ binding site and its role in hybrid myosins. Reinach, F.C., Nagai, K., Kendrick-Jones, J. Nature (1986) [Pubmed]
  3. A new myosin fragment: visualization of the regulatory domain. Winkelmann, D.A., Almeda, S., Vibert, P., Cohen, C. Nature (1984) [Pubmed]
  4. Continued expression of neonatal myosin heavy chain in adult dystrophic skeletal muscle. Bandman, E. Science (1985) [Pubmed]
  5. Baculovirus expression of chicken nonmuscle heavy meromyosin II-B. Characterization of alternatively spliced isoforms. Pato, M.D., Sellers, J.R., Preston, Y.A., Harvey, E.V., Adelstein, R.S. J. Biol. Chem. (1996) [Pubmed]
  6. Brain myosin-V is a two-headed unconventional myosin with motor activity. Cheney, R.E., O'Shea, M.K., Heuser, J.E., Coelho, M.V., Wolenski, J.S., Espreafico, E.M., Forscher, P., Larson, R.E., Mooseker, M.S. Cell (1993) [Pubmed]
  7. Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Dominguez, R., Freyzon, Y., Trybus, K.M., Cohen, C. Cell (1998) [Pubmed]
  8. Intracompartmental sorting of essential myosin light chains: molecular dissection and in vivo monitoring by epitope tagging. Soldati, T., Perriard, J.C. Cell (1991) [Pubmed]
  9. Phosphorylation controls brush border motility by regulating myosin structure and association with the cytoskeleton. Broschat, K.O., Stidwill, R.P., Burgess, D.R. Cell (1983) [Pubmed]
  10. Extinction of muscle-specific properties in somatic cell heterokaryons. Lawrence, J.B., Coleman, J.R. Dev. Biol. (1984) [Pubmed]
  11. Independent development of contractile properties and myosin light chains in embryonic chick fast and slow muscle. Pette, D., Vrbová, G., Whalen, R.C. Pflugers Arch. (1979) [Pubmed]
  12. Cloned mRNA sequences for two types of embryonic myosin heavy chains from chick skeletal muscle. I. DNA and derived amino acid sequence of light meromyosin. Kavinsky, C.J., Umeda, P.K., Sinha, A.M., Elzinga, M., Tong, S.W., Zak, R., Jakovcic, S., Rabinowitz, M. J. Biol. Chem. (1983) [Pubmed]
  13. The chicken myosin heavy chain family. Robbins, J., Horan, T., Gulick, J., Kropp, K. J. Biol. Chem. (1986) [Pubmed]
  14. Analysis of the chicken fast myosin heavy chain family. Localization of isoform-specific antibody epitopes and regions of divergence. Moore, L.A., Arrizubieta, M.J., Tidyman, W.E., Herman, L.A., Bandman, E. J. Mol. Biol. (1992) [Pubmed]
  15. Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis. Winkelmann, D.A., Lowey, S., Press, J.L. Cell (1983) [Pubmed]
  16. Changes in the mRNA population of chick myoblasts during myogenesis in vitro. Paterson, B.M., Bishop, J.O. Cell (1977) [Pubmed]
  17. The essential light chains constitute part of the active site of smooth muscle myosin. Okamoto, Y., Sekine, T., Grammer, J., Yount, R.G. Nature (1986) [Pubmed]
  18. The motor domain determines the large step of myosin-V. Tanaka, H., Homma, K., Iwane, A.H., Katayama, E., Ikebe, R., Saito, J., Yanagida, T., Ikebe, M. Nature (2002) [Pubmed]
  19. Control of tension development in scallop muscle fibres with foreign regulatory light chains. Simmons, R.M., Szent-Györgyi, A.G. Nature (1980) [Pubmed]
  20. Chicken gizzard: relation between calcium-activated phosphorylation and contraction. Hoar, P.E., Kerrick, W.G., Cassidy, P.S. Science (1979) [Pubmed]
  21. Myosin drives retrograde F-actin flow in neuronal growth cones. Lin, C.H., Espreafico, E.M., Mooseker, M.S., Forscher, P. Neuron (1996) [Pubmed]
  22. Transmembrane linkage between surface glycoproteins and components of the cytoplasm in neutrophil leukocytes. Sheterline, P., Hopkins, C.R. J. Cell Biol. (1981) [Pubmed]
  23. Molecular characterization of avian muscle titin. Tan, K.O., Sater, G.R., Myers, A.M., Robson, R.M., Huiatt, T.W. J. Biol. Chem. (1993) [Pubmed]
  24. Axial arrangement of the myosin rod in vertebrate thick filaments: immunoelectron microscopy with a monoclonal antibody to light meromyosin. Shimizu, T., Dennis, J.E., Masaki, T., Fischman, D.A. J. Cell Biol. (1985) [Pubmed]
  25. Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon-mediated inhibition of actin filament velocity. Wang, Z., Jiang, H., Yang, Z.Q., Chacko, S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  26. The kinetic mechanism of myosin V. De La Cruz, E.M., Wells, A.L., Rosenfeld, S.S., Ostap, E.M., Sweeney, H.L. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  27. N-terminal myosin-binding fragment of talin. Lin, Y., Kishi, H., Nakamura, A., Takagi, T., Kohama, K. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  28. Organization of the genetic locus for chicken myosin light chain kinase is complex: multiple proteins are encoded and exhibit differential expression and localization. Birukov, K.G., Schavocky, J.P., Shirinsky, V.P., Chibalina, M.V., Van Eldik, L.J., Watterson, D.M. J. Cell. Biochem. (1998) [Pubmed]
  29. Reversal of caldesmon binding to myosin with calcium-calmodulin or by phosphorylating caldesmon. Hemric, M.E., Lu, F.W., Shrager, R., Carey, J., Chalovich, J.M. J. Biol. Chem. (1993) [Pubmed]
  30. Phosphorylation by MAPKAP kinase 2 activates Mg(2+)-ATPase activity of myosin II. Komatsu, S., Hosoya, H. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  31. Cadherins promote skeletal muscle differentiation in three-dimensional cultures. Redfield, A., Nieman, M.T., Knudsen, K.A. J. Cell Biol. (1997) [Pubmed]
  32. Caldesmon and a 20-kDa actin-binding fragment of caldesmon inhibit tension development in skinned gizzard muscle fiber bundles. Pfitzer, G., Zeugner, C., Troschka, M., Chalovich, J.M. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  33. Zipper protein, a B-G protein with the ability to regulate actin/myosin 1 interactions in the intestinal brush border. Bikle, D.D., Munson, S., Komuves, L. J. Biol. Chem. (1996) [Pubmed]
  34. Two distinct nonmuscle myosin-heavy-chain mRNAs are differentially expressed in various chicken tissues. Identification of a novel gene family of vertebrate non-sarcomeric myosin heavy chains. Katsuragawa, Y., Yanagisawa, M., Inoue, A., Masaki, T. Eur. J. Biochem. (1989) [Pubmed]
  35. Isolation of the chick myosin alkali light chain gene expressed in embryonic gizzard muscle and transitional expression of the light chain gene family in vivo. Nabeshima, Y., Nabeshima, Y., Kawashima, M., Nakamura, S., Nonomura, Y., Fujii-Kuriyama, Y. J. Mol. Biol. (1988) [Pubmed]
  36. Cloning and expression of a smooth muscle caldesmon. Bryan, J., Imai, M., Lee, R., Moore, P., Cook, R.G., Lin, W.G. J. Biol. Chem. (1989) [Pubmed]
  37. Myosin-Va binds to and mechanochemically couples microtubules to actin filaments. Cao, T.T., Chang, W., Masters, S.E., Mooseker, M.S. Mol. Biol. Cell (2004) [Pubmed]
  38. Characterization of 5'-flanking region of heart myosin light chain 2A gene. Structural and functional evidence for promoter activity. Zarraga, A.M., Danishefsky, K., Deshpande, A., Nicholson, D., Mendola, C., Siddiqui, M.A. J. Biol. Chem. (1986) [Pubmed]
  39. The genes and mRNA coding for the heavy chains of chick embryonic skeletal myosin. Patrinou-Georgoulas, M., John, H.A. Cell (1977) [Pubmed]
  40. Fast and slow myosin within single skeletal muscle fibres of adult rabbits. Lutz, H., Weber, H., Billeter, R., Jenny, E. Nature (1979) [Pubmed]
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