Unconventional myosins
Abstract
Myosins are molecular motors that upon interaction with actin filaments convert energy from ATP hydrolysis into mechanical force. Evidence has emerged for the existence of a large, widely expressed and evolutionarily ancient superfamily of myosin genes. In addition to the well-catheterized conventional, filament-forming, two-headed myosin-II of muscle and nonmuscle cells, at least ten additional classes of myosins have been identified. In vertebrates, at least seven of the eleven classes are expressed, and many myosins can be expressed in a single cell type. This review summarizes known structural and functional features of these novel unconventional myosins.
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Many myosins are inhibited for actin interaction in a light chain-dependent manner by sequences downstream of their motor domains.
“Many myosins are inhibited for actin interaction in a light chain-dependent manner by sequences downstream of their motor domains (Cross et al., 1988; Mooseker and Cheney, 1995).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Mooseker and Cheney, 1995
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Self-citationDirect Involvement of Yeast Type I Myosins in Cdc42-Dependent Actin Polymerization
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Self-citationTwo Components of Actin-based Retrograde Flow in Sea Urchin Coelomocytes
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“Despite the major advances made in research on unconventional myosins (for reviews, see Mooseker and Cheney, 1995; Ostap and Pollard, 1996), conventional myosin II remains the only myosin type capable of forming bipolar minifilaments, which can interact with actin in a contractile manner (Cheney et…”
BackgroundEffects of shaker-1 mutations on myosin-VIIa protein and mRNA expression
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Self-citationFunctions of unconventional myosins
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“MYO9A is one of the unconventional myosins that are members of the myosin superfamily that display the general domains of conventional myosins (63, 64).”
BackgroundMyosin VIIA mutation screening in 189 Usher syndrome type 1 patients.
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Self-citationHuman myosin-IXb is a mechanochemically active motor and a GAP for rho
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“…short (Myo1A, 1B, 1C, 1D, 1G, and 1H), consisting of a putative pleckstrin-homology domain within a tail-homology domain (TH1), or long (Myo1E and 1F), with a proline-rich TH2 and a Src-homology 3 (SH3) domain in addition to the TH1 domain (Mooseker and Cheney, 1995; McConnell and Tyska, 2010).”
InfluentialA Microtubule‐Facilitated Nuclear Import Pathway for Cancer Regulatory Proteins
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“Myo1a (brush border myosin I) forms cross-links between the underlying actin core and the plasma membrane of intestinal microvilli [24].”
BackgroundSelf-citationTransient Kinetic Analysis of the 130-kDa Myosin I (MYR-1 Gene Product) from Rat Liver
Coluccio, L. M., & Geeves, M. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21575 · Cited by 102 · see citing works
Münchow, S., Sauter, C., & Jansen, R. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.10.1511 · Cited by 102 · see citing works
Molecular Genetic Dissection of Mouse Unconventional Myosin-VA: Tail Region Mutations
Huang, J., Mermall, V., Strobel, M. C., et al. (1998) · Genetics · doi:10.1093/genetics/148.4.1963 · Cited by 100 · see citing works
Self-citationMaples, C. J., Ruiz, W. G., & Apodaca, G. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6741 · Cited by 96 · see citing works
Regulation of Class I and Class II Myosins by Heavy Chain Phosphorylation
Brzeska, H., & Korn, E. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.16983 · Cited by 96 · see citing works
Motegi, F., Arai, R., & Mabuchi, I. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.5.1367 · Cited by 96 · see citing works
“First, the neck domain of Myo4 contains six 23- to 25-amino acid repeats referred to as IQ motifs (Figure 1), which are potent binding sites for calmodulin and other light chains (Mooseker and Cheney, 1995).”
BackgroundInfluentialThe Rat Myosin myr 5 Is a GTPase-activating Protein for Rho In Vivo: Essential Role of Arginine 1695
Müller, R. T., Honnert, U., Reinhard, J., & Bähler, M. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.10.2039 · Cited by 95 · see citing works
Ca2+-dependent Regulation of the Motor Activity of Myosin V
Homma, K., Saito, J., Ikebe, R., & Ikebe, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003132200 · Cited by 89 · see citing works
Fifty Ways to Love Your Lever: Myosin Motors
Block, S. M. (1996) · Cell · doi:10.1016/s0092-8674(00)81332-x · Cited by 89 · see citing works
Cloning and characterization of myr 6, an unconventional myosin of the dilute/myosin-V family.
Zhao, L., Koslovsky, J. S., Reinhard, J., Bähler, M., Witt, A. E., Provance, D. W., & Mercer, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.10826 · Cited by 90 · see citing works
Molecular motors in higher plants
Asada, T., & Collings, D. A. (1997) · Trends in Plant Science · doi:10.1016/s1360-1385(96)10051-0 · Cited by 90 · see citing works
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“…and the immunolocalization data showing a punctate staining pattern for myosin-V in cultured neurons and astrocytes (Espreafico et al., 1992) have led to the hypothesis of a role for class V myosins in polarized organelle translocation (for review see Mooseker and Cheney, 1995; Larson, 1996).”
BackgroundMutational spectrum ofMYO15A: the large N-terminal extension of myosin XVA is required for hearing
Nal, N., Ahmed, Z. M., Erkal, E., Alper, Ö. M., Lüleci, G., Dinç, O., Waryah, A. M., Ain, Q. U., Tasneem, S., Husnaın, T., et al. (2007) · Human Mutation · doi:10.1002/humu.20556 · Cited by 90 · see citing works
“The conserved motor domain of myosin contains a nucleotide binding pocket, an actin binding site, and a converter region, which links the motor domain to the neck [Mooseker and Cheney, 1995].”
BackgroundMutational Analysis of the Switch II Loop ofDictyostelium Myosin II
Sasaki, N., Shimada, T., & Sutoh, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20334 · Cited by 88 · see citing works
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The tail binds to the head–neck domain, inhibiting ATPase activity of myosin VIIA
Umeki, N., Jung, H. S., Watanabe, S., Sakai, T., Li, X., Ikebe, R., Craig, R., & Ikebe, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812930106 · Cited by 86 · see citing works
Myosin IXb is a single-headed minus-end-directed processive motor
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Myosin Vb controls biogenesis of post-Golgi Rab10 carriers during axon development
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Septins may form a ubiquitous family of cytoskeletal filaments.
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- Authors
- Mooseker, M. S., & Cheney, R. E.
- Affiliations
- Yale University (US)
- ORCID
- Cheney, Richard E.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 1995-11
- Volume
- 11
- Issue
- 1
- Pages
- 633-675
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W4234290082
- Cited by
- 370
- References
- 0
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2022: 3 · 2021: 5 · 2020: 2 · 2019: 4 · 2018: 1 · 2017: 5 · 2016: 7 · 2015: 5 · 2014: 4 · 2013: 3 · 2012: 10
- FWCI
- 38.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5p01dk038979-05)
- National Institute of General Medical Sciences (GM25387)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 38979, DK-34989, P30DK034989)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- unconventional myosins, myosin superfamily, molecular motors, F-actin, ATP hydrolysis, myosin II, myosin structure, myosin function
- MeSH terms
- Acanthamoeba, Amino Acid Sequence, Animals, Deafness, Drosophila, Humans, Molecular Sequence Data, Myosins, Phylogeny, Saccharomyces cerevisiae, Swine, Arabidopsis, Sequence Homology, Amino Acid, Mice
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