Historical Background
Nuclear myosin I (NM1) belongs to the group of class I myosins, which are monomeric, nonprocessive, slow-rate, and low-duty ratio molecular motors transforming free chemical energy stored in ATP into mechanical force. Nuclear myosin I was discovered by testing antibodies to adrenal myosin 1. The antibody was staining a 120 kDa nuclear protein with ATPase activity, and the protein was ATP-, actin-, and calmodulin- binding, which are the typical features of unconventional myosins. At that time, there were no myosins known to be present in the cell nucleus, hence the discovered protein was called nuclear myosin I (Pestic-Dragovich et al. 2000). The mass spectrometric analysis of the NM1 showed a high homology to the Myosin 1c (Myo1c) protein, the first single-headed myosin isolated from mammals, also known as mammalian myosin I, or myosin 1β. However, with the increasing numbers of myosins discovered, there...
This is a preview of subscription content, log in via an institution to check access.
References
Almuzzaini B, Sarshad AA, Farrants AK, Percipalle P. Nuclear myosin 1 contributes to a chromatin landscape compatible with RNA polymerase II transcription activation. BMC Biol. 2015;13:35. doi:10.1186/s12915-015-0147-z.
Chuang CH, Carpenter AE, Fuchsova B, Johnson T, de Lanerolle P, Belmont AS. Long-range directional movement of an interphase chromosome site. Curr Biol. 2006;16:825–31. doi:10.1016/j.cub.2006.03.059.
Coluccio LM. Myosin I. Am J Physiol. 1997;273:C347–C59.
Dundr M, Ospina JK, Sung MH, John S, Upender M, Ried T, et al. Actin-dependent intranuclear repositioning of an active gene locus in vivo. J Cell Biol. 2007;179:1095–103. doi:10.1083/jcb.200710058.
Dzijak R, Yildirim S, Kahle M, Novak P, Hnilicova J, Venit T, et al. Specific nuclear localizing sequence directs two myosin isoforms to the cell nucleus in calmodulin-sensitive manner. PLoS One. 2012;7:e30529. doi:10.1371/journal.pone.0030529.
Gillespie PG, Albanesi JP, Bahler M, Bement WM, Berg JS, Burgess DR, et al. Myosin-I nomenclature. J Cell Biol. 2001;155:703–4. doi:10.1083/jcb.200110032.
Grummt I. Actin and myosin as transcription factors. Curr Opin Genet Dev. 2006;16:191–6. doi:10.1016/j.gde.2006.02.001.
Hedberg Oldfors C, Dios DG, Linder A, Visuttijai K, Samuelson E, Karlsson S, et al. Analysis of an independent tumor suppressor locus telomeric to Tp53 suggested Inpp5k and Myo1c as novel tumor suppressor gene candidates in this region. BMC Genet. 2015;16:80. doi:10.1186/s12863-015-0238-4.
Kahle M, Pridalova J, Spacek M, Dzijak R, Hozak P. Nuclear myosin is ubiquitously expressed and evolutionary conserved in vertebrates. Histochem Cell Biol. 2007;127:139–48. doi:10.1007/s00418-006-0231-0.
Kalendova A, Kalasova I, Yamazaki S, Ulicna L, Harata M, Hozak P. Nuclear actin filaments recruit cofilin and actin-related protein 3, and their formation is connected with a mitotic block. Histochem Cell Biol. 2014;142:139–52. doi:10.1007/s00418-014-1243-9.
Percipalle P, Fomproix N, Cavellan E, Voit R, Reimer G, Kruger T, et al. The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin 1 and has a role in RNA polymerase I transcription. EMBO Rep. 2006;7:525–30. doi:10.1038/sj.embor.7400657.
Pestic-Dragovich L, Stojiljkovic L, Philimonenko AA, Nowak G, Ke Y, Settlage RE, et al. A myosin I isoform in the nucleus. Science. 2000;290:337–41.
Philimonenko VV, Zhao J, Iben S, Dingova H, Kysela K, Kahle M, et al. Nuclear actin and myosin I are required for RNA polymerase I transcription. Nat Cell Biol. 2004;6:1165–72. doi:10.1038/ncb1190.
Sarshad A, Sadeghifar F, Louvet E, Mori R, Bohm S, Al-Muzzaini B, et al. Nuclear myosin 1c facilitates the chromatin modifications required to activate rRNA gene transcription and cell cycle progression. PLoS Genet. 2013;9:e1003397. doi:10.1371/journal.pgen.1003397.
Sarshad AA, Corcoran M, Al-Muzzaini B, Borgonovo-Brandter L, Von Euler A, Lamont D, et al. Glycogen synthase kinase (GSK) 3beta phosphorylates and protects nuclear myosin 1c from proteasome-mediated degradation to activate rDNA transcription in early G1 cells. PLoS Genet. 2014;10:e1004390. doi:10.1371/journal.pgen.1004390.
Sielski NL, Ihnatovych I, Hagen JJ, Hofmann WA. Tissue specific expression of Myosin IC Isoforms. Bmc Cell Biol. 2014;15. doi:10.1186/1471-2121-15-8.
Suresh S. Biomechanics and biophysics of cancer cells. Acta Biomater. 2007;3:413–38. doi:10.1016/j.actbio.2007.04.002.
Venit T, Dzijak R, Kalendova A, Kahle M, Rohozkova J, Schmidt V, et al. Mouse nuclear myosin I knock-out shows interchangeability and redundancy of myosin isoforms in the cell nucleus. PLoS One 2013;8. doi:10.1371/journal.pone.0061406.
Venit T, Kalendova A, Petr M, Dzijak R, Pastorek L, Rohozkova J, et al. Nuclear myosin I regulates cell membrane tension. Sci Rep. 2016;6:30864. doi:10.1038/srep30864.
Ye J, Zhao J, Hoffmann-Rohrer U, Grummt I. Nuclear myosin I acts in concert with polymeric actin to drive RNA polymerase I transcription. Genes Dev. 2008;22:322–30. doi:10.1101/gad.455908.
Yildirim S, Castano E, Sobol M, Philimonenko VV, Dzijak R, Venit T, et al. Involvement of phosphatidylinositol 4,5-bisphosphate in RNA polymerase I transcription. J Cell Sci. 2013;126:2730–9. doi:10.1242/jcs.123661.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2016 Springer Science+Business Media LLC
About this entry
Cite this entry
Venit, T., Hozak, P. (2016). Nuclear Myosin I. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_101485-1
Download citation
DOI: https://doi.org/10.1007/978-1-4614-6438-9_101485-1
Received:
Accepted:
Published:
Publisher Name: Springer, New York, NY
Online ISBN: 978-1-4614-6438-9
eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences