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Gene Review

MYO1A  -  myosin IA

Homo sapiens

Synonyms: BBM-I, BBMI, Brush border myosin I, DFNA48, MIHC, ...
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Disease relevance of MYO1A

  • Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line [1].
  • Higher BBMI was predictive of a lower long-term weight gain, while dose was not a significant predictor of greater longer term weight change [2].

High impact information on MYO1A

  • In contrast, arcs and rings contained no apparent enrichment of microtubules, brush border myosin-I immunogens, or myosin-V [3].
  • MYO1A, which is located within the DFNA48 locus, is the first myosin I family member found to be involved in causing deafness and may be a major contributor to autosomal dominant-hearing loss [4].
  • Here, we report the identification of a nonsense mutation, of a trinucleotide insertion leading to an addition of an amino acid, and of six missense mutations in MYO1A cDNA sequence in a group of hearing-impaired patients from Italy [4].
  • Multiple mutations of MYO1A, a cochlear-expressed gene, in sensorineural hearing loss [4].
  • We determined the rates for ATP binding to BBM-I and brush border actomyosin-I (actoBBM-I), the rate of actoBBM-I dissociation by ATP, and the rates for the steps in ADP dissociation from actoBBM-I [5].

Biological context of MYO1A

  • To analyze whether a myosin was involved in endocytosis, we produced, in this polarized cell line, truncated, non-functional, brush border, myosin I proteins (BBMI) that we have previously demonstrated to have a dominant negative effect on endocytosis of unpolarized cells [6].

Anatomical context of MYO1A


Other interactions of MYO1A


Analytical, diagnostic and therapeutic context of MYO1A

  • Baseline body mass index (BBMI; kg/m2) and dose (mg/day) were investigated as predictors of long-term weight change experienced during olanzapine treatment [2].


  1. Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line. Durrbach, A., Collins, K., Matsudaira, P., Louvard, D., Coudrier, E. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. Long-term olanzapine treatment: weight change and weight-related health factors in schizophrenia. Kinon, B.J., Basson, B.R., Gilmore, J.A., Tollefson, G.D. The Journal of clinical psychiatry. (2001) [Pubmed]
  3. A novel cytoskeletal structure involved in purse string wound closure and cell polarity maintenance. Bement, W.M., Forscher, P., Mooseker, M.S. J. Cell Biol. (1993) [Pubmed]
  4. Multiple mutations of MYO1A, a cochlear-expressed gene, in sensorineural hearing loss. Donaudy, F., Ferrara, A., Esposito, L., Hertzano, R., Ben-David, O., Bell, R.E., Melchionda, S., Zelante, L., Avraham, K.B., Gasparini, P. Am. J. Hum. Genet. (2003) [Pubmed]
  5. Kinetic characterization of brush border myosin-I ATPase. Jontes, J.D., Milligan, R.A., Pollard, T.D., Ostap, E.M. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  6. Truncated brush border myosin I affects membrane traffic in polarized epithelial cells. Durrbach, A., Raposo, G., Tenza, D., Louvard, D., Coudrier, E. Traffic (2000) [Pubmed]
  7. MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells. Tyska, M.J., Mooseker, M.S. Biophys. J. (2002) [Pubmed]
  8. Brush border myosin I (BBMI): a basally localized transcript in human jejunal enterocytes. Li, W., Wang, J., Coluccio, L.M., Matsudaira, P., Grand, R.J. J. Histochem. Cytochem. (2000) [Pubmed]
  9. Immunochemical evidence that myosin I heavy chain-like protein is identical to the 110-kilodalton brush-border protein. Hoshimaru, M., Fujio, Y., Sobue, K., Sugimoto, T., Nakanishi, S. J. Biochem. (1989) [Pubmed]
  10. Conformational changes due to calcium-induced calmodulin dissociation in brush border myosin I-decorated F-actin revealed by cryoelectron microscopy and image analysis. Whittaker, M., Milligan, R.A. J. Mol. Biol. (1997) [Pubmed]
  11. Human brush border myosin-I and myosin-Ic expression in human intestine and Caco-2BBe cells. Skowron, J.F., Bement, W.M., Mooseker, M.S. Cell Motil. Cytoskeleton (1998) [Pubmed]
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