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Gene Review

MYO5C  -  myosin VC

Homo sapiens

Synonyms: MGC74969, Unconventional myosin-Vc
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Disease relevance of MYO5C


Psychiatry related information on MYO5C

  • From these and other data, we conclude that the essential role(s) of myosin I in A. nidulans is probably structural, requiring little, if any, actin-activated MgATPase or motor activity, which have long been considered the defining characteristics of the myosin family [6].
  • Cardiac myosin binding protein C gene is specifically expressed in heart during murine and human development [7].
  • After exercise, the recovery of phosphocreatine-an index of oxidative metabolic capacity of the muscle-was slower in the beta myosin heavy chain group (mean half time 0.65 (0.08) minutes) than in the troponin T group (0.60 (0.17) minutes) or controls (0.48 (0.14) minutes) [8].
  • In hyperthyroidism, the cross-bridge movement significantly preceded tension development, suggesting that hyperthyroid myosin (V1) has a longer latency period between the shift to the vicinity of the thin filament and force development [9].
  • Newly-reported structural information about certain proximities between points on bound nucleotide and points on the heavy chain of myosin S-1 are incorporated into a previously-reported [Botts, J. Thomason, J.F. & Morales, M.F. Proc. Nat. Acad. Sci. USA, 86, 2204-2208 (1989)] structure of S-1 [10].

High impact information on MYO5C

  • Kinetics shows that the binding of myosin to actin is a two-step process which affects ATP and ADP affinity [11].
  • Molecular genetics of myosin [12].
  • Structural and biochemical studies suggest that the position of tropomyosin (Tm) and troponin (Tn) on the thin filament determines the interaction of myosin with the binding sites on actin [13].
  • 3) The initial rate of force development depends mostly on the extent of Ca(2+) activation of the thin filament and myosin kinetic properties but depends little on the initial force level [13].
  • Second, the technology to measure picoNewton forces and nanometer distances has provided direct determinations of the force and step length generated by a single myosin molecule interacting with a single actin filament [14].

Chemical compound and disease context of MYO5C

  • These approximately 190-kDa myotonic dystrophy kinase-related Cdc42-binding kinases (MRCKs) preferentially phosphorylate nonmuscle myosin light chain at serine 19, which is known to be crucial for activating actin-myosin contractility [15].
  • DESIGN AND METHODS: Serum myosin heavy-chain fragments, TnT, and TnI were studied up to 12 days after diagnosis in relationship to the serum creatine kinase level in 20 patients with rhabdomyolysis [16].
  • METHODS AND RESULTS: Syngeneic splenocytes, coupled with cardiac myosin by use of ethylene carbodiimide, were administered intravenously before disease induction, and the effects of this peripheral tolerization on myosin-induced myocarditis were assessed [17].
  • Compounds interfering with actin function, including phalloidin, the catalytic subunit of Clostridium botulinum C2 toxin, and N-ethylmaleimide-treated myosin S1 fragments were microinjected into the axon [18].
  • The presence of ventricular myosin light chains in the atria of children with congenital heart disease was demonstrated by two-dimensional polyacrylamide gel electrophoresis, peptide mapping, and Western blot analysis [19].

Biological context of MYO5C

  • Myosin-binding protein C (MyBP-C) binds to myosin with two binding sites, one close to the N terminus and the other at the C terminus [20].
  • The growth kinetics and morphological features of these cells were determined in vitro and the expression of the different myosin heavy (embryonic, fetal, fast, and slow) and light chain isoforms was analyzed [21].
  • Myosin light chain gene expression associated with disease states of the human heart [22].
  • Because of the phenotype resulting in the dilute mouse and because of their potential role in intracellular transport, unconventional myosin-encoding genes were regarded as candidate genes for Griscelli disease [23].
  • Myosin is a highly conserved, ubiquitous protein found in all eukaryotic cells, where it provides the motor function for diverse movements such as cytokinesis, phagocytosis, and muscle contraction [24].

Anatomical context of MYO5C

  • Additionally, S2 possesses a conserved charge distribution with three prominent rings of negative potential within S2-Delta, the first of which may provide a binding interface for the "blocked head" of smooth muscle myosin in the OFF state [25].
  • The observation that many disease-associated mutations affect the second negatively charged ring further suggests that charge interactions play an important role in regulation of cardiac muscle activity through myosin-binding protein C [25].
  • Myosin diversity in the human epithelial cell line Caco-2BBe, the porcine epithelial cell line LLC-PK1 (CL-4), human peripheral blood leukocytes, and human liver was analyzed [26].
  • The leukemic protein core binding factor beta (CBFbeta)-smooth-muscle myosin heavy chain sequesters CBFalpha2 into cytoskeletal filaments and aggregates [27].
  • Class V myosins are one of the most ancient and widely distributed groups of the myosin superfamily and are hypothesized to function as motors for actin-dependent organelle transport [28].

Associations of MYO5C with chemical compounds

  • To do so, the cells were treated with ML-7, a myosin II light chain kinase inhibitor, or Y-27632, an inhibitor of Rho-kinase (ROCK), both of which block actomyosin contraction [29].
  • We show that butanedione monoxime (BDM), a known inhibitor of muscle myosin II, inhibits nonmuscle myosin II and myosin V adenosine triphosphatases [30].
  • The gelation induced by warming (to 25 degrees C) the 100,000 g supernatant fraction (extract) of HeLa cells lysed in a buffer containing sucrose, ATP, DTE, EGTA, imidazole, and Triton X-100 was studied in the presence of myosin and heavy meromyosin (HMM) [31].
  • Myosin light chain kinase functions downstream of Ras/ERK to promote migration of urokinase-type plasminogen activator-stimulated cells in an integrin-selective manner [32].
  • Using nondenaturing polyacrylamide gel electrophoresis, we have identified two distinct myosin isoenzymes in human atrial tissue that correspond to the V1 and V3 isomyosins found in rat ventricular tissue [33].

Physical interactions of MYO5C

  • This supports the notion that nucleotide-free myosin V is an excellent model for strongly bound myosin and allows us to describe the actin-myosin interface [34].

Other interactions of MYO5C

  • Myosin VI is an unconventional myosin that may play a role in vesicular membrane traffic through actin rich regions of the cytoplasm in eukaryotic cells [35].
  • CHC22 expression is also increased in regenerating muscle fibers with the same time course as embryonic myosin, indicating a role in muscle repair [36].
  • Here, we examined the structure of the actin bundle formed by human fascin-1 (actin/fascin bundle), and its mode of interaction with myosin in vitro [37].
  • The role of myosin-V, an unconventional myosin, in growth cone dynamics was examined by chromophore-assisted laser inactivation (CALI) [38].
  • We also review work on the elementary processes of the dynamin GTPase at high ionic strength and compare these to the ATPase of the force-generating protein myosin and the GTPase of the signalling protein Ras [39].

Analytical, diagnostic and therapeutic context of MYO5C

  • PCR amplification yielded 8-11 putative myosins (depending on the cDNA source) representing six distinct myosin classes [26].
  • Co-immunoprecipitation experiments reveal that Dictyostelium M7 (DdM7) interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion [40].
  • Using NMR spectroscopy and isothermal titration calorimetry we demonstrate that cC2 alone binds to a fragment of myosin, S2Delta, with low affinity (k(D) = 1.1 mm) but exhibits a highly specific binding site [20].
  • In all satellite cell cultures, only the four fast-type light chains (MLC1emb, MLC1F, MLC2F, and MLC3F) were synthesized and no slow myosin light chains were ever detected [21].
  • AP-actin binds to skeletal myosin subfragment 1 (S1) and forms a homogeneous complex as demonstrated by analytical ultracentrifugation [41].


  1. Fusion between transcription factor CBF beta/PEBP2 beta and a myosin heavy chain in acute myeloid leukemia. Liu, P., Tarlé, S.A., Hajra, A., Claxton, D.F., Marlton, P., Freedman, M., Siciliano, M.J., Collins, F.S. Science (1993) [Pubmed]
  2. From flies' eyes to our ears: mutations in a human class III myosin cause progressive nonsyndromic hearing loss DFNB30. Walsh, T., Walsh, V., Vreugde, S., Hertzano, R., Shahin, H., Haika, S., Lee, M.K., Kanaan, M., King, M.C., Avraham, K.B. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. A novel human myosin alkali light chain is developmentally regulated. Expression in fetal cardiac and skeletal muscle and in adult atria. Arnold, H.H., Lohse, P., Seidel, U., Bober, E. Eur. J. Biochem. (1988) [Pubmed]
  4. Mutations in myosin heavy chain 11 cause a syndrome associating thoracic aortic aneurysm/aortic dissection and patent ductus arteriosus. Zhu, L., Vranckx, R., Van Kien, P.K., Lalande, A., Boisset, N., Mathieu, F., Wegman, M., Glancy, L., Gasc, J.M., Brunotte, F., Bruneval, P., Wolf, J.E., Michel, J.B., Jeunemaitre, X. Nat. Genet. (2006) [Pubmed]
  5. Induction of autoimmune myocarditis in interleukin-2-deficient mice. Grässl, G., Pummerer, C.L., Horak, I., Neu, N. Circulation (1997) [Pubmed]
  6. Myosin I mutants with only 1% of wild-type actin-activated MgATPase activity retain essential in vivo function(s). Liu, X., Osherov, N., Yamashita, R., Brzeska, H., Korn, E.D., May, G.S. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  7. Cardiac myosin binding protein C gene is specifically expressed in heart during murine and human development. Fougerousse, F., Delezoide, A.L., Fiszman, M.Y., Schwartz, K., Beckmann, J.S., Carrier, L. Circ. Res. (1998) [Pubmed]
  8. Abnormal skeletal muscle bioenergetics in familial hypertrophic cardiomyopathy. Thompson, C.H., Kemp, G.J., Taylor, D.J., Conway, M., Rajagopalan, B., O'Donoghue, A., Styles, P., McKenna, W.J., Radda, G.K. Heart (1997) [Pubmed]
  9. Cross-bridge and calcium behavior in ferret papillary muscle in different thyroid states. Yagi, N., Saeki, Y., Ishikawa, T., Kurihara, S. Jpn. J. Physiol. (2001) [Pubmed]
  10. The region in myosin S-1 that may be involved in energy transduction. Morales, M.F., Ue, K., Bivin, D.B. Adv. Exp. Med. Biol. (1993) [Pubmed]
  11. Structural mechanism of muscle contraction. Geeves, M.A., Holmes, K.C. Annu. Rev. Biochem. (1999) [Pubmed]
  12. Molecular genetics of myosin. Emerson, C.P., Bernstein, S.I. Annu. Rev. Biochem. (1987) [Pubmed]
  13. Regulation of contraction in striated muscle. Gordon, A.M., Homsher, E., Regnier, M. Physiol. Rev. (2000) [Pubmed]
  14. Actomyosin interaction in striated muscle. Cooke, R. Physiol. Rev. (1997) [Pubmed]
  15. Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization. Leung, T., Chen, X.Q., Tan, I., Manser, E., Lim, L. Mol. Cell. Biol. (1998) [Pubmed]
  16. Myosin heavy-chain fragments and cardiac troponins in the serum in rhabdomyolysis. Diagnostic specificity of new biochemical markers. Löfberg, M., Tähtelä, R., Härkönen, M., Somer, H. Arch. Neurol. (1995) [Pubmed]
  17. Prevention of autoimmune myocarditis through the induction of antigen-specific peripheral immune tolerance. Godsel, L.M., Wang, K., Schodin, B.A., Leon, J.S., Miller, S.D., Engman, D.M. Circulation (2001) [Pubmed]
  18. Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton. Shupliakov, O., Bloom, O., Gustafsson, J.S., Kjaerulff, O., Low, P., Tomilin, N., Pieribone, V.A., Greengard, P., Brodin, L. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  19. Expression of ventricular myosin subunits in the atria of children with congenital heart malformations. Shi, Q.W., Danilczyk, U., Wang, J.X., See, Y.P., Williams, W.G., Trusler, G.A., Beaulieu, R., Rose, V., Jackowski, G. Circ. Res. (1991) [Pubmed]
  20. Dissecting the N-terminal Myosin Binding Site of Human Cardiac Myosin-binding Protein C: STRUCTURE AND MYOSIN BINDING OF DOMAIN C2. Ababou, A., Gautel, M., Pfuhl, M. J. Biol. Chem. (2007) [Pubmed]
  21. Clones of human satellite cells can express in vitro both fast and slow myosin heavy chains. Edom, F., Mouly, V., Barbet, J.P., Fiszman, M.Y., Butler-Browne, G.S. Dev. Biol. (1994) [Pubmed]
  22. Myosin light chain gene expression associated with disease states of the human heart. Trahair, T., Yeoh, T., Cartmill, T., Keogh, A., Spratt, P., Chang, V., dos Remedios, C.G., Gunning, P. J. Mol. Cell. Cardiol. (1993) [Pubmed]
  23. Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene. Pastural, E., Barrat, F.J., Dufourcq-Lagelouse, R., Certain, S., Sanal, O., Jabado, N., Seger, R., Griscelli, C., Fischer, A., de Saint Basile, G. Nat. Genet. (1997) [Pubmed]
  24. The mammalian myosin heavy chain gene family. Weiss, A., Leinwand, L.A. Annu. Rev. Cell Dev. Biol. (1996) [Pubmed]
  25. Crystal structures of human cardiac beta-myosin II S2-{Delta} provide insight into the functional role of the S2 subfragment. Blankenfeldt, W., Thom??, N.H., Wray, J.S., Gautel, M., Schlichting, I. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  26. Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. Bement, W.M., Hasson, T., Wirth, J.A., Cheney, R.E., Mooseker, M.S. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  27. The leukemic protein core binding factor beta (CBFbeta)-smooth-muscle myosin heavy chain sequesters CBFalpha2 into cytoskeletal filaments and aggregates. Adya, N., Stacy, T., Speck, N.A., Liu, P.P. Mol. Cell. Biol. (1998) [Pubmed]
  28. Human myosin-Vc is a novel class V myosin expressed in epithelial cells. Rodriguez, O.C., Cheney, R.E. J. Cell. Sci. (2002) [Pubmed]
  29. Myosin-mediated cytoskeleton contraction and Rho GTPases regulate laminin-5 matrix assembly. DeHart, G.W., Jones, J.C. Cell Motil. Cytoskeleton (2004) [Pubmed]
  30. Myosin is involved in postmitotic cell spreading. Cramer, L.P., Mitchison, T.J. J. Cell Biol. (1995) [Pubmed]
  31. Effects of myosin and heavy meromyosin on actin-related gelation of HeLa cell extracts. Weihing, R.R. J. Cell Biol. (1977) [Pubmed]
  32. Myosin light chain kinase functions downstream of Ras/ERK to promote migration of urokinase-type plasminogen activator-stimulated cells in an integrin-selective manner. Nguyen, D.H., Catling, A.D., Webb, D.J., Sankovic, M., Walker, L.A., Somlyo, A.V., Weber, M.J., Gonias, S.L. J. Cell Biol. (1999) [Pubmed]
  33. Myosin isoenzyme distribution in overloaded human atrial tissue. Buttrick, P.M., Malhotra, A., Brodman, R., McDermott, L., Lam, L. Circulation (1986) [Pubmed]
  34. The structure of the rigor complex and its implications for the power stroke. Holmes, K.C., Schröder, R.R., Sweeney, H.L., Houdusse, A. Philos. Trans. R. Soc. Lond., B, Biol. Sci. (2004) [Pubmed]
  35. The localization of myosin VI at the golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation. Buss, F., Kendrick-Jones, J., Lionne, C., Knight, A.E., Côté, G.P., Paul Luzio, J. J. Cell Biol. (1998) [Pubmed]
  36. Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration. Towler, M.C., Gleeson, P.A., Hoshino, S., Rahkila, P., Manalo, V., Ohkoshi, N., Ordahl, C., Parton, R.G., Brodsky, F.M. Mol. Biol. Cell (2004) [Pubmed]
  37. Polarized actin bundles formed by human fascin-1: their sliding and disassembly on myosin II and myosin V in vitro. Ishikawa, R., Sakamoto, T., Ando, T., Higashi-Fujime, S., Kohama, K. J. Neurochem. (2003) [Pubmed]
  38. Function of myosin-V in filopodial extension of neuronal growth cones. Wang, F.S., Wolenski, J.S., Cheney, R.E., Mooseker, M.S., Jay, D.G. Science (1996) [Pubmed]
  39. Oligomerization and kinetic mechanism of the dynamin GTPase. Eccleston, J.F., Binns, D.D., Davis, C.T., Albanesi, J.P., Jameson, D.M. Eur. Biophys. J. (2002) [Pubmed]
  40. Identification of a myosin VII-talin complex. Tuxworth, R.I., Stephens, S., Ryan, Z.C., Titus, M.A. J. Biol. Chem. (2005) [Pubmed]
  41. Expression of a nonpolymerizable actin mutant in Sf9 cells. Joel, P.B., Fagnant, P.M., Trybus, K.M. Biochemistry (2004) [Pubmed]
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