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Gene Review

Myo5a  -  myosin VA

Rattus norvegicus

Synonyms: Dilute myosin heavy chain, non-muscle, Dop, Myh12, Unconventional myosin-Va
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Disease relevance of Myo5a

  • They also contribute to our understanding of the neurological disease mechanisms of the human hereditary disease Griscelli syndrome type 1, which is caused by mutation of the Myo5a gene [1].

High impact information on Myo5a


Biological context of Myo5a

  • Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A [2].
  • The latter suggests a possible involvement of M-Va in nerve regeneration processes [6].
  • 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 [1].
  • We conclude that myosin-Va undergoes intracellular proteolysis by endogenous calpain, when synaptosomes are depolarized in the presence of calcium, at the same cleavage site previously identified in vitro, thus, making it a target for calcium signaling during synaptic activation [7].

Anatomical context of Myo5a


Associations of Myo5a with chemical compounds


Co-localisations of Myo5a

  • Immunocytochemical localization of myosin-Va in cultured hippocampal neurons shows that it partially colocalizes with PSD-95 at synapses and is also diffusely localized in cell bodies, dendrites, and axons [11].

Other interactions of Myo5a


Analytical, diagnostic and therapeutic context of Myo5a

  • Myosin Va (M-Va) in the nerve was detected by using SDS-PAGE and Western blot techniques with a polyclonal antibody specifically raised against the M-Va globular tail domain [6].
  • Moreover, a significant increment of transcripts coding for M-Va heavy chain was detected through time using RT-PCR after nerve injury and compared to intact nerves [6].
  • In addition, purification of M-Va from the rat sciatic nerve prior to immunoblotting yielded a M-Va standard band [6].
  • A polyclonal antibody (pAb) against the motor domain of myosin Va showed prominent nonrandom immunofluorescence labeling in PARP domains [13].
  • We show that intracellular proteolysis of myosin-Va occurs in rat cortical synaptosomes depolarized in the presence of calcium, evidenced by the formation of an 80 k polypeptide that co-migrates in SDS-PAGE with the 80 k fragment produced by the in vitro proteolysis of myosin-Va by calpain [7].


  1. 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]
  2. Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A. Watanabe, M., Nomura, K., Ohyama, A., Ishikawa, R., Komiya, Y., Hosaka, K., Yamauchi, E., Taniguchi, H., Sasakawa, N., Kumakura, K., Ushiki, T., Sato, O., Ikebe, M., Igarashi, M. Mol. Biol. Cell (2005) [Pubmed]
  3. Involvement of the Rab27 binding protein Slac2c/MyRIP in insulin exocytosis. Waselle, L., Coppola, T., Fukuda, M., Iezzi, M., El-Amraoui, A., Petit, C., Regazzi, R. Mol. Biol. Cell (2003) [Pubmed]
  4. Hydrogen peroxide alters membrane and cytoskeleton properties and increases intercellular connections in astrocytes. Zhu, D., Tan, K.S., Zhang, X., Sun, A.Y., Sun, G.Y., Lee, J.C. J. Cell. Sci. (2005) [Pubmed]
  5. The small GTPase Rab27B regulates amylase release from rat parotid acinar cells. Imai, A., Yoshie, S., Nashida, T., Shimomura, H., Fukuda, M. J. Cell. Sci. (2004) [Pubmed]
  6. Myosin Va is locally synthesized following nerve injury. Calliari, A., Sotelo-Silveira, J., Costa, M.C., Nogueira, J., Cameron, L.C., Kun, A., Benech, J., Sotelo, J.R. Cell Motil. Cytoskeleton (2002) [Pubmed]
  7. Myosin-Va proteolysis by Ca2+/calpain in depolarized nerve endings from rat brain. Casaletti, L., Tauhata, S.B., Moreira, J.E., Larson, R.E. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  8. Myosin Va facilitates the distribution of secretory granules in the F-actin rich cortex of PC12 cells. Rudolf, R., Kögel, T., Kuznetsov, S.A., Salm, T., Schlicker, O., Hellwig, A., Hammer, J.A., Gerdes, H.H. J. Cell. Sci. (2003) [Pubmed]
  9. Localization of myosin II and V isoforms in cultured rat sympathetic neurones and their potential involvement in presynaptic function. Takagishi, Y., Futaki, S., Itoh, K., Espreafico, E.M., Murakami, N., Murata, Y., Mochida, S. J. Physiol. (Lond.) (2005) [Pubmed]
  10. Myosin Va is proteolysed in rat cerebellar granule neurons after excitotoxic injury. Alavez, S., Morán, J., Franco-Cea, A., Ortega-Gómez, A., Casaletti, L., Cameron, L.C. Neurosci. Lett. (2004) [Pubmed]
  11. Identification of proteins in the postsynaptic density fraction by mass spectrometry. Walikonis, R.S., Jensen, O.N., Mann, M., Provance, D.W., Mercer, J.A., Kennedy, M.B. J. Neurosci. (2000) [Pubmed]
  12. Molecular motors involved in chromaffin cell secretion. Rosé, S.D., Lejen, T., Casaletti, L., Larson, R.E., Pene, T.D., Trifaró, J.M. Ann. N. Y. Acad. Sci. (2002) [Pubmed]
  13. Myosin Va and kinesin II motor proteins are concentrated in ribosomal domains (periaxoplasmic ribosomal plaques) of myelinated axons. Sotelo-Silveira, J.R., Calliari, A., Cárdenas, M., Koenig, E., Sotelo, J.R. J. Neurobiol. (2004) [Pubmed]
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