Alternative titles; symbols
HGNC Approved Gene Symbol: MYO1C
Cytogenetic location: 17p13.3 Genomic coordinates (GRCh38): 17:1,464,186-1,492,686 (from NCBI)
Myosins are molecular motors that, upon interaction with actin filaments, utilize energy from ATP hydrolysis to generate mechanical force. For further background information on myosins, see MYO1A (601478).
By screening a kidney cDNA library with a mouse Myo1c probe, Crozet et al. (1997) obtained a human cDNA encoding MYO1C. The deduced 1,028-amino acid protein, which is 96% identical to the mouse protein, contains ATP- and actin-binding sequences in the motor (or head) domain, followed by three 23-residue IQ motifs and a tail domain rich in basic residues that is expected to interact with negatively charged membrane phospholipids. Northern blot analysis revealed ubiquitous expression of Myo1c in adult mouse tissues.
MYO1C, also known as myosin I-beta and MYR2, was thought to mediate the slow component of adaptation by hair cells, the sensory cells of the inner ear. To test this hypothesis, Holt et al. (2002) mutated tyr61 of MYO1C to gly, conferring susceptibility to inhibition by N6-modified ADP analogs. They expressed the mutant MYO1C in utricular hair cells of transgenic mice, delivered an ADP analog through a whole-cell recording pipette, and found that the analog rapidly blocked adaptation to positive and negative deflections in transgenic cells but not in wildtype cells. The speed and specificity of inhibition suggested that MYO1C participates in adaptation in hair cells.
Bose et al. (2002) reported that the unconventional myosin MYO1C is present in GLUT4 (138190)-containing vesicles purified from 3T3-L1 adipocytes. MYO1C is highly expressed in primary and cultured adipocytes. Insulin (176730) enhances the localization of MYO1C with GLUT4 in cortical tubulovesicular structures associated with actin filaments, and this colocalization is insensitive to wortmannin. Insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane is augmented by the expression of wildtype MYO1C and inhibited by a dominant-negative cargo domain of MYO1C. A decrease in the expression of endogenous MYO1C mediated by small interfering RNAs inhibited insulin-stimulated uptake of 2-deoxyglucose. Thus, Bose et al. (2002) concluded that MYO1C functions in a phosphatidylinositol-3-hydroxykinase (PI3K; see 601232)-independent insulin signaling pathway that controls the movement of intracellular GLUT4-containing vesicles to the plasma membrane.
Lebreton et al. (2018) showed that Drosophila Myo1D (606539) and Myo1C are sufficient to generate de novo directional twisting of cells, single organs, or the whole body in opposite directions. Directionality lies in the myosins' motor domain and is swappable between Myo1D and Myo1C. In addition, Myo1D drives gliding of actin filaments in circular, counterclockwise paths in vitro. Altogether, Lebreton et al. (2018) concluded that their results revealed the molecular motor Myo1D as a chiral determinant that is sufficient to break symmetry at all biologic scales through chiral interaction with the actin cytoskeleton.
Using PCR and radiation hybrid analysis, Crozet et al. (1997) mapped the MYO1C gene to 17p13.
A report by Nunez et al. (2008) indicating that 3-dimensional motor-dependent interchromosomal interactions involving MYO1C are required to achieve enhanced transcription of specific estrogen-receptor target genes was retracted.
Bose, A., Guilherme, A., Robida, S. I., Nicoloro, S. M. C., Zhou, Q. L., Jiang, Z. Y., Pomerleau, D. P., Czech, M. P. Glucose transporter recycling in response to insulin is facilitated by myosin Myo1c. Nature 420: 821-824, 2002. [PubMed: 12490950] [Full Text: https://doi.org/10.1038/nature01246]
Crozet, F., Amraoui, A. E., Blanchard, S., Lenoir, M., Ripoll, C., Vago, P., Hamel, C., Fizames, C., Levi-Acobas, F., Depetris, D., Mattei, M.-G., Weil, D., Pujol, R., Petit, C. Cloning of the genes encoding two murine and human cochlear unconventional type I myosins. Genomics 40: 332-341, 1997. [PubMed: 9119401] [Full Text: https://doi.org/10.1006/geno.1996.4526]
Holt, J. R., Gillespie, S. K. H., Provance, D. W., Jr., Shah, K., Shokat, K. M., Corey, D. P., Mercer, J. A., Gillespie, P. G. A chemical-genetic strategy implicates myosin-1c in adaptation by hair cells. Cell 108: 371-381, 2002. [PubMed: 11853671] [Full Text: https://doi.org/10.1016/s0092-8674(02)00629-3]
Lebreton, G., Geminard, C., Lapraz, F., Pyrpassopoulos, S., Cerezo, D., Speder, P., Ostap, E. M., Noselli, S. Molecular to organismal chirality is induced by the conserved myosin 1D. Science 362: 949-952, 2018. [PubMed: 30467170] [Full Text: https://doi.org/10.1126/science.aat8642]
Nunez, E., Kwon, Y.-S., Hutt, K. R., Hu, Q., Cardamone, M. D., Ohgi, K. A., Garcia-Bassets, I., Rose, D. W., Glass, C. K., Rosenfeld, M. G., Fu, X.-D. Nuclear receptor-enhanced transcription requires motor- and LSD1-dependent gene networking in interchromatin granules. Cell 132: 996-1010, 2008. Note: Retraction: Cell 134: 189 only, 2008. [PubMed: 18358812] [Full Text: https://doi.org/10.1016/j.cell.2008.01.051]