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Myo1e  -  myosin IE

Rattus norvegicus

Synonyms: MYR5, Myosin heavy chain myr 3, Myr3, Unconventional myosin 1E, Unconventional myosin-Ie
 
 
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High impact information on Myo1e

  • Although purified Myr3 was observed to cross-link actin filaments, it bound in an ATP regulated manner to F-actin, and no evidence for a nucleotide-independent high affinity actin binding site that could explain the triphasic activation pattern was obtained [1].
  • Myr 3 was often present, but not specifically enriched in the intercellular junctions induced by constitutively active Rac1 [2].
  • Myo1e was found in hair cells of the auditory and vestibular epithelia; this isozyme was enriched in the cuticular plate, the actin meshwork that anchors the stereocilia [3].
 

Anatomical context of Myo1e

  • Myr 3, a member of the myosin-I family from rat, is shown in this study to be localized at adherens-type intercellular junctions in epithelial and nonepithelial tissues [2].

References

  1. The ATPase activity of Myr3, a rat myosin I, is allosterically inhibited by its own tail domain and by Ca2+ binding to its light chain calmodulin. Stöffler, H.E., Bähler, M. J. Biol. Chem. (1998) [Pubmed]
  2. Targeting of the myosin-I myr 3 to intercellular adherens type junctions induced by dominant active Cdc42 in HeLa cells. Stöffler, H.E., Honnert, U., Bauer, C.A., Höfer, D., Schwarz, H., Müller, R.T., Drenckhahn, D., Bähler, M. J. Cell. Sci. (1998) [Pubmed]
  3. Myosin-I isozymes in neonatal rodent auditory and vestibular epithelia. Dumont, R.A., Zhao, Y.D., Holt, J.R., Bähler, M., Gillespie, P.G. J. Assoc. Res. Otolaryngol. (2002) [Pubmed]
 
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