Biology:MYO1C
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Myosin-Ic is a protein that in humans is encoded by the MYO1C gene.[1][2]
This gene encodes a member of the unconventional myosin protein family, which are actin-based molecular motors. The protein is found in the cytoplasm, and one isoform with a unique N-terminus is also found in the nucleus. The nuclear isoform associates with RNA polymerase I and II and functions in transcription initiation. The mouse ortholog of this protein also functions in intracellular vesicle transport to the plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene. The related gene myosin IE has been referred to as myosin IC in the literature, but it is a distinct locus on chromosome 19.[2]
References
- ↑ "Cloning of the genes encoding two murine and human cochlear unconventional type I myosins". Genomics 40 (2): 332–41. Apr 1997. doi:10.1006/geno.1996.4526. PMID 9119401.
- ↑ 2.0 2.1 "Entrez Gene: MYO1C myosin IC". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4641.
Further reading
- "Localization of the rat myosin I molecules myr 1 and myr 2 and in vivo targeting of their tail domains.". J. Cell Sci. 108 (12): 3775–86. 1997. doi:10.1242/jcs.108.12.3775. PMID 8719884.
- "Mapping of unconventional myosins in mouse and human.". Genomics 36 (3): 431–9. 1997. doi:10.1006/geno.1996.0488. PMID 8884266.
- "Human brush border myosin-I and myosin-Ic expression in human intestine and Caco-2BBe cells.". Cell Motil. Cytoskeleton 41 (4): 308–24. 1999. doi:10.1002/(SICI)1097-0169(1998)41:4<308::AID-CM4>3.0.CO;2-J. PMID 9858156.
- "A myosin I isoform in the nucleus.". Science 290 (5490): 337–41. 2000. doi:10.1126/science.290.5490.337. PMID 11030652. Bibcode: 2000Sci...290..337P.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707–16. 2005. doi:10.1038/nbt971. PMID 15146197.
- "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. 2004. doi:10.1073/pnas.0404720101. PMID 15302935. Bibcode: 2004PNAS..10112130B.
- "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions.". Genome Res. 14 (9): 1711–8. 2004. doi:10.1101/gr.2435604. PMID 15342556.
- "Nuclear actin and myosin I are required for RNA polymerase I transcription.". Nat. Cell Biol. 6 (12): 1165–72. 2005. doi:10.1038/ncb1190. PMID 15558034.
- "Nuclear distribution of actin and myosin I depends on transcriptional activity of the cell.". Histochem. Cell Biol. 124 (5): 347–58. 2005. doi:10.1007/s00418-005-0042-8. PMID 16133118.
- "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. 2006. doi:10.1101/gr.4039406. PMID 16344560.
- "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription.". J. Biol. Chem. 281 (24): 16264–71. 2006. doi:10.1074/jbc.M600233200. PMID 16603771.
- "Small ribosomal subunits associate with nuclear myosin and actin in transit to the nuclear pores.". FASEB J. 20 (11): 1901–3. 2006. doi:10.1096/fj.05-5278fje. PMID 16877530.
- "Nuclear myosin is ubiquitously expressed and evolutionary conserved in vertebrates.". Histochem. Cell Biol. 127 (2): 139–48. 2007. doi:10.1007/s00418-006-0231-0. PMID 16957816.
- "Nuclear myosin I is necessary for the formation of the first phosphodiester bond during transcription initiation by RNA polymerase II.". J. Cell. Biochem. 99 (4): 1001–9. 2006. doi:10.1002/jcb.21035. PMID 16960872.
- "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. 2007. doi:10.1038/msb4100134. PMID 17353931.
External links
- Overview of all the structural information available in the PDB for UniProt: O00159 (Unconventional myosin-Ic) at the PDBe-KB.
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