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Gene Review

MYO5A  -  myosin VA (heavy chain 12, myoxin)

Homo sapiens

Synonyms: Dilute myosin heavy chain, non-muscle, GS1, MYH12, MYO5, MYR12, ...
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Disease relevance of MYO5A


Psychiatry related information on MYO5A


High impact information on MYO5A

  • In addition, RAB27A-deficient T cells exhibited reduced cytotoxicity and cytolytic granule exocytosis, whereas MYO5A-defective T cells did not [7].
  • We previously mapped the GS locus to chromosome 15q21 and found a mutation in a gene (MYO5A) encoding a molecular motor in two patients [7].
  • Here we provide direct evidence that myosin-V is indeed a processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament [8].
  • Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis [9].
  • The role of myosin-V, an unconventional myosin, in growth cone dynamics was examined by chromophore-assisted laser inactivation (CALI) [3].

Biological context of MYO5A

  • We also show that an identical phenotype can result from the deletion of the MYO5A F-exon, an exon with a tissue-restricted expression pattern [1].
  • We report the isolation and sequencing of "myoxin" (MYH12), the human homologue of the mouse dilute gene, and its assignment to human chromosome 15 [10].
  • Analysis of the myosin Va (Myo5a) gene of the dop genome showed the presence of a complex rearrangement consisting of a 306-bp inversion associated with 217-bp and 17-bp deletions [11].
  • Mlph is proposed to be a modular protein binding the melanosome-associated protein Rab27a, Myosin Va (MyoVa), actin, and microtubule end-binding protein (EB1), via distinct N-terminal Rab27a-binding domain (R27BD), medial MyoVa-binding domain (MBD), and C-terminal actin-binding domain (ABD), respectively [12].
  • Here, we identify and characterize the binding site of DLC on myosin Va [13].

Anatomical context of MYO5A


Associations of MYO5A with chemical compounds

  • Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein [16].
  • Transient transfection of antisense phosphorothioate oligodeoxynucleotides targeted against myosin Va mRNA reduced expression of myosin Va protein in cultured mouse melan-a melanocytes by over 70 % 20 h after transfection whereas a control (shuffled sequence) oligonucleotide did not [2].
  • The myosin V was labeled with bifunctional rhodamine on one of its calmodulin light chains [17].
  • We show that butanedione monoxime (BDM), a known inhibitor of muscle myosin II, inhibits nonmuscle myosin II and myosin V adenosine triphosphatases [18].
  • We introduced a tetracysteine motif in the upper 50-kDa domain (residues 292-297) of myosin V containing a single IQ domain (MV 1IQ), allowing us to label this site with the fluorescein biarscenical hairpin-binding dye (FlAsH) (MV 1IQ FlAsH) [19].

Physical interactions of MYO5A

  • We investigated the effect of DYNLL2 binding on the structure of a myosin Va heavy chain fragment that contains the DYNLL2 binding site and flanking sequence, only parts of which are strongly predicted to form a coiled coil [20].
  • 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 [21].
  • Here, we show by reconstitution using purified proteins that Rab27a and Mlph are sufficient to form a transport complex with myosin Va in vitro [22].
  • The kinectin-binding domain on the kinesin tail partially overlaps its head-binding domain and the myosin-Va binding domain [23].

Regulatory relationships of MYO5A

  • When our data are taken together, they suggest that exon B and its associated DLC2 have a significant effect on the structure of parts of the coiled-coil tail domains and such a way could influence the regulation and cargo-binding function of myosin Va [13].

Other interactions of MYO5A


Analytical, diagnostic and therapeutic context of MYO5A


  1. Griscelli syndrome restricted to hypopigmentation results from a melanophilin defect (GS3) or a MYO5A F-exon deletion (GS1). Ménasché, G., Ho, C.H., Sanal, O., Feldmann, J., Tezcan, I., Ersoy, F., Houdusse, A., Fischer, A., de Saint Basile, G. J. Clin. Invest. (2003) [Pubmed]
  2. Inhibition of dendrite formation in mouse melanocytes transiently transfected with antisense DNA to myosin Va. Edgar, A.J., Bennett, J.P. J. Anat. (1999) [Pubmed]
  3. 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]
  4. Does the myosin V neck region act as a lever? Moore, J.R., Krementsova, E.B., Trybus, K.M., Warshaw, D.M. J. Muscle Res. Cell. Motil. (2004) [Pubmed]
  5. Alpha-herpesvirus infection induces the formation of nuclear actin filaments. Feierbach, B., Piccinotti, S., Bisher, M., Denk, W., Enquist, L.W. PLoS Pathog. (2006) [Pubmed]
  6. Ca(2+)-dependent regulation of the motor activity of myosin V. Homma, K., Saito, J., Ikebe, R., Ikebe, M. J. Biol. Chem. (2000) [Pubmed]
  7. Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. Ménasché, G., Pastural, E., Feldmann, J., Certain, S., Ersoy, F., Dupuis, S., Wulffraat, N., Bianchi, D., Fischer, A., Le Deist, F., de Saint Basile, G. Nat. Genet. (2000) [Pubmed]
  8. Myosin-V is a processive actin-based motor. Mehta, A.D., Rock, R.S., Rief, M., Spudich, J.A., Mooseker, M.S., Cheney, R.E. Nature (1999) [Pubmed]
  9. Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Puthalakath, H., Villunger, A., O'Reilly, L.A., Beaumont, J.G., Coultas, L., Cheney, R.E., Huang, D.C., Strasser, A. Science (2001) [Pubmed]
  10. Cloning, analysis, and chromosomal localization of myoxin (MYH12), the human homologue to the mouse dilute gene. Engle, L.J., Kennett, R.H. Genomics (1994) [Pubmed]
  11. Myosin va mutation in rats is an animal model for the human hereditary neurological disease, griscelli syndrome type 1. Takagishi, Y., Murata, Y. Ann. N. Y. Acad. Sci. (2006) [Pubmed]
  12. A coiled-coil domain of melanophilin is essential for Myosin va recruitment and melanosome transport in melanocytes. Hume, A.N., Tarafder, A.K., Ramalho, J.S., Sviderskaya, E.V., Seabra, M.C. Mol. Biol. Cell (2006) [Pubmed]
  13. Alternatively spliced exon B of Myosin va is essential for binding the tail-associated light chain shared by Dynein. H??di, Z., N??meth, A.L., Radnai, L., Het??nyi, C., Schlett, K., Bodor, A., Perczel, A., Nyitray, L. Biochemistry (2006) [Pubmed]
  14. Interactions of human Myosin Va isoforms, endogenously expressed in human melanocytes, are tightly regulated by the tail domain. Westbroek, W., Lambert, J., Bahadoran, P., Busca, R., Herteleer, M.C., Smit, N., Mommaas, M., Ballotti, R., Naeyaert, J.M. J. Invest. Dermatol. (2003) [Pubmed]
  15. Myosin-V, a versatile motor for short-range vesicle transport. Langford, G.M. Traffic (2002) [Pubmed]
  16. Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. Naisbitt, S., Valtschanoff, J., Allison, D.W., Sala, C., Kim, E., Craig, A.M., Weinberg, R.J., Sheng, M. J. Neurosci. (2000) [Pubmed]
  17. Adaptability of myosin V studied by simultaneous detection of position and orientation. Syed, S., Snyder, G.E., Franzini-Armstrong, C., Selvin, P.R., Goldman, Y.E. EMBO J. (2006) [Pubmed]
  18. Myosin is involved in postmitotic cell spreading. Cramer, L.P., Mitchison, T.J. J. Cell Biol. (1995) [Pubmed]
  19. Dynamics of the upper 50-kDa domain of myosin V examined with fluorescence resonance energy transfer. Sun, M., Oakes, J.L., Ananthanarayanan, S.K., Hawley, K.H., Tsien, R.Y., Adams, S.R., Yengo, C.M. J. Biol. Chem. (2006) [Pubmed]
  20. The Binding of DYNLL2 to Myosin Va Requires Alternatively Spliced Exon B and Stabilizes a Portion of the Myosin's Coiled-Coil Domain. Wagner, W., Fodor, E., Ginsburg, A., Hammer, J.A. Biochemistry (2006) [Pubmed]
  21. 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]
  22. In vitro reconstitution of a transport complex containing Rab27a, melanophilin and myosin Va. Wu, X., Sakamoto, T., Zhang, F., Sellers, J.R., Hammer, J.A. FEBS Lett. (2006) [Pubmed]
  23. Kinectin-kinesin binding domains and their effects on organelle motility. Ong, L.L., Lim, A.P., Er, C.P., Kuznetsov, S.A., Yu, H. J. Biol. Chem. (2000) [Pubmed]
  24. Rab27b is up-regulated in human Griscelli syndrome type II melanocytes and linked to the actin cytoskeleton via exon F-Myosin Va transcripts. Westbroek, W., Lambert, J., De Schepper, S., Kleta, R., Van Den Bossche, K., Seabra, M.C., Huizing, M., Mommaas, M., Naeyaert, J.M. Pigment Cell Res. (2004) [Pubmed]
  25. Myosin vb is associated with plasma membrane recycling systems. Lapierre, L.A., Kumar, R., Hales, C.M., Navarre, J., Bhartur, S.G., Burnette, J.O., Provance, D.W., Mercer, J.A., Bähler, M., Goldenring, J.R. Mol. Biol. Cell (2001) [Pubmed]
  26. Myosin-IXb is a single-headed and processive motor. Post, P.L., Tyska, M.J., O'Connell, C.B., Johung, K., Hayward, A., Mooseker, M.S. J. Biol. Chem. (2002) [Pubmed]
  27. Cloning and regional assignment of the human myosin heavy chain 12 (MYH12) gene to chromosome band 15q21. Moore, K.J., Testa, J.R., Francke, U., Milatovich, A., Copeland, N.G., Jenkins, N.A. Cytogenet. Cell Genet. (1995) [Pubmed]
  28. Two-headed binding of a processive myosin to F-actin. Walker, M.L., Burgess, S.A., Sellers, J.R., Wang, F., Hammer, J.A., Trinick, J., Knight, P.J. Nature (2000) [Pubmed]
  29. Cloning and characterization of a novel RING finger protein that interacts with class V myosins. El-Husseini, A.E., Vincent, S.R. J. Biol. Chem. (1999) [Pubmed]
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