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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 (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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“With the addition of these new myosins-I, each of the four previously defined myosin-I subclasses (Mooseker and Cheney, 1995) now contains two genes in humans.”
BackgroundSelf-citationMyosin VI is an actin-based motor that moves backwards
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Unconventional Myosins in Cell Movement, Membrane Traffic, and Signal Transduction
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Self-citationLytic Cycle ofToxoplasma gondii
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Unconventional Myosins in Inner-Ear Sensory Epithelia
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“Despite their apparent similarity of function, at least a dozen distinct classes of myosin separated in ancient progenitors, and most of these classes have been retained in fungi, amoebas, plants, invertebrates, and vertebrates (Mooseker and Cheney, 1995).”
Self-citationMolecular motors: structural adaptations to cellular functions
Howard, J. (1997) · Nature · doi:10.1038/39247 · Cited by 489
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Griscelli disease maps to chromosome 15q21 and is associated with mutations in the Myosin-Va gene
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“If, as conjectured (Mooseker and Cheney, 1996), this portion of the myosin Va molecule contains the site that mediates myosin Va/ melanosome interaction, then it should compete with endogenous myosin Va for binding to the melanosome.”
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Lin, C., Espreáfico, E. M., Mooseker, M. S., & Forscher, P. (1996) · Neuron · doi:10.1016/s0896-6273(00)80097-5 · Cited by 407
Self-citationMicrotubule interaction site of the kinesin motor
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Guiding neuronal growth cones using Ca 2+ signals
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Vogl, A. W., Vaid, K., & Guttman, J. A. (2009) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-09597-4_11 · Cited by 307
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Self-citationLight Chain– dependent Regulation of Kinesin's Interaction with Microtubules
Verhey, K. J., Lizotte, D. L., Abramson, T., Barenboim, L., Schnapp, B. J., & Rapoport, T. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.4.1053 · Cited by 266
“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).”
BackgroundRho: a connection between membrane receptor signalling and the cytoskeleton
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“The myosin superfamily includes at least 11 different molecular motors that possess a conserved motor domain attached to a variety of neck and tail domains with distinguishing structural and biochemical characteristics (Cheney et al., 1993 b ; Mooseker and Cheney, 1995).”
BackgroundMyosin cooperates with microtubule motors during organelle transport in melanophores
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“To investigate myosins in T. gondii, we used a polyclonal antisera generated against a conserved peptide found in virtually all myosins described to date (the exception being the highly divergent ninaC of Drosophila) (Mooseker and Cheney, 1995).”
BackgroundMethodInfluentialWu, X., Bowers, B., Wei, Q., Kocher, B., & Hammer, J. A. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.7.847 · Cited by 230
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“…functions, which include vesicle transport, cytokinesis and such specialized functions as auditory perception (for recent reviews see BaÈhler, 1996; Fath and Burgess, 1994; Hammer, 1994; Hasson and Mooseker, 1995; Mermall et al., 1998; Mooseker and Cheney, 1995; Titus, 1993).”
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Conservation within the myosin motor domain: implications for structure and function
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“The other myosin classes are described in detail in two excellent reviews which have been published recently [6,26].”
InfluentialMyosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin
Berg, J. S., Derfler, B. H., Pennisi, C., Corey, D. P., & Cheney, R. E. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.19.3439 · Cited by 218
Self-citationDirect Involvement of Yeast Type I Myosins in Cdc42-Dependent Actin Polymerization
Lechler, T., Shevchenko, A., Shevchenko, A., & Li, R. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.2.363 · Cited by 217
“Type I myosins are highly conserved proteins that appear to play roles in numerous processes, such as endocytosis, membrane trafficking, contractility, and cell motility (Mooseker and Cheney, 1995).”
InfluentialYonemura, S., Tsukita, S., & Tsukita, S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.7.1497 · Cited by 212
“The free surface domain is characterized by various types of cellular protrusions such as microvilli, filopodia, and lamellipodia which contain abundant actin filaments (Bretscher, 1991; Condeelis, 1993; Hitt and Luna, 1994; Mooseker and Cheney, 1995; Mitchison and Cramer, 1996).”
Kouprina, N., Pavlı́ček, A., Collins, N. K., Nakano, M., Noskov, V. N., Ohzeki, J., Mochida, G. H., Risinger, J. I., Goldsmith, P. K., Gunsior, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi220 · Cited by 210
“IQ calmodulin-binding motifs comprise 20–25 amino acids, with the core fitting the consensus IQXXXRGXXXR (where X is any amino acid) (10,11).”
BackgroundChen, X., Leto, D. E., Chiang, S.-H., Wang, Q., & Saltiel, A. R. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.007 · Cited by 203
Transport of ER vesicles on actin filaments in neurons by myosin V
Tabb, J. S., Molyneaux, B. J., Cohen, D. L., Kuznetsov, S. A., & Langford, G. M. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.21.3221 · Cited by 204
Genetic Causes of Hearing Loss
Willems, P. J. (2000) · New England Journal of Medicine · doi:10.1056/nejm200004133421506 · Cited by 198
Myosin-1a Is Critical for Normal Brush Border Structure and Composition
Tyska, M. J., Mackey, A. T., Huang, J., Copeland, N. G., Jenkins, N. A., & Mooseker, M. S. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-12-1116 · Cited by 193
“Based on the results of in vitro motility studies (Mooseker and Cheney, 1995), it has been assumed that Myo1a bridges exert an outward (plus-end–directed) force on the MV membrane, but direct evidence for this has been lacking.”
BackgroundInfluentialSelf-citationBergman, L. W., Kaiser, K., Fujioka, H., et al. (2002) · Journal of Cell Science · doi:10.1242/jcs.00194 · Cited by 193
“Its putative short neck domain has no conserved IQ motifs (consensus IQXXXRGXXXRK) that function as light chain binding sites in the neck domains of many myosins (Mooseker and Cheney, 1995).”
BackgroundMyosin II Is Involved in the Production of Constitutive Transport Vesicles from the TGN
Müsch, A., Cohen, D., & Rodriguez-Boulan, E. J. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.2.291 · Cited by 184
“The important advances made in the identification of novel myosins in recent years (Hasson and Mooseker, 1995; Mooseker and Cheney, 1995) predict a plethora of trafficking functions for these molecules that are waiting to be discovered.”
BackgroundYoon, Y., Pitts, K. R., Dahan, S., & McNiven, M. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.779 · Cited by 183
“This prediction is consistent with the observations made for numerous other cytoskeletal and membrane-associated proteins such as the kinesins (Hirokawa, 1996; Moore and Endow, 1996), cytoplasmic myosins (Mooseker and Cheney, 1995), ADP ribosylation factors (ARFs; Goud, 1992; Clark et al.”
Function of Myosin-V in Filopodial Extension of Neuronal Growth Cones
Wang, F.-S., Wolenski, J. S., Cheney, R. E., Mooseker, M. S., & Jay, D. G. (1996) · Science · doi:10.1126/science.273.5275.660 · Cited by 183
Self-citationLiang, Y. Q., Wang, A., Belyantseva, I. A., Anderson, D. W., Probst, F. J., Barber, T. D., Miller, W., Touchman, J. W., Jin, L., Sullivan, S. L., et al. (1999) · Genomics · doi:10.1006/geno.1999.5976 · Cited by 179
Kinesin Light Chains Are Essential for Axonal Transport in Drosophila
Gindhart, J. G., Desai, C. J., Beushausen, S., Zinn, K., & Goldstein, L. S. B. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.2.443 · Cited by 179
“I ntracellular transport requires the action of molecular motors that bind cargo and generate movement coupled to ATP hydrolysis along cytoskeletal filaments (Gibbons et al., 1994; Bloom and Endow, 1995; Mooseker and Cheney, 1995).”
Myosin I Contributes to the Generation of Resting Cortical Tension
Dai, J., Ting‐Beall, H. P., Hochmuth, R. M., et al. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)76968-7 · Cited by 179
“Myosin I’s comprise a single heavy chain of 110–130 kDa and one to six lowmolecular-mass light chains (Mooseker and Cheney, 1995).”
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Provance, D. W., Wei, M. C., Ipe, V., & Mercer, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14554 · Cited by 172
Identification of a Second Myosin-II inSchizosaccharomyces pombe:
Bezanilla, M., Forsburg, S. L., & Pollard, T. D. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.12.2693 · Cited by 160
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Self-citationMyosin XI Is Essential for Tip Growth inPhyscomitrella patens
Vidali, L., Burkart, G. M., Augustine, R. C., et al. (2010) · The Plant Cell · doi:10.1105/tpc.109.073288 · Cited by 155
“They are most similar to class V myosins from animals and fungi (Mooseker and Cheney, 1995), in which homology is strikingly conserved throughout the protein, from the motor to the globular tail domain (Li and Nebenfuhr, 2007).”
BackgroundMyosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis
Krendel, M., Osterweil, E. K., & Mooseker, M. S. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.01.021 · Cited by 153
“Myo1E tail consists of a positively charged TH1 domain, a proline-rich TH2, and an SH3 (TH3) domain [2].”
BackgroundSelf-citationJansen, R. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.3.455 · Cited by 150
Nuclear Myosin VI Enhances RNA Polymerase II-Dependent Transcription
Vreugde, S., Ferrai, C., Miluzio, A., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.005 · Cited by 144
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Myosin VIIA Is Required for Aminoglycoside Accumulation in Cochlear Hair Cells
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Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport
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Self-citationCatlett, N. L., & Weisman, L. S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14799 · Cited by 137
MYO1A (Brush Border Myosin I) Dynamics in the Brush Border of LLC-PK1-CL4 Cells
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Self-citationThe Structural Basis of the Myosin ATPase Activity
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ADP Inhibition of Myosin V ATPase Activity
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“The cellular roles of these myosins are likely to be extremely varied (Mooseker and Cheney, 1995), which undoubtedly requires both structural and enzymatic specializations.”
BackgroundCART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling
Yan, Q., Sun, W., Kujala, P., Lotfi, Y., Vida, T. A., & Bean, A. J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-11-1014 · Cited by 131
“, 1996; Rodriguez and Cheney, 2002) that have been implicated in genetic diseases and membrane trafficking (Mooseker and Cheney, 1995; Hasson and Mooseker, 1996; Titus, 1997).”
BackgroundMolecular motors and their functions in plants
Reddy, A. S. N. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)04004-9 · Cited by 127
Anderson, B. L., Boldogh, I. R., Evangelista, M., Boone, C. M., Greene, L. A., & Pon, L. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.6.1357 · Cited by 124
“This superfamily consists of conven- tional (type II or muscle-like) myosins and at least ten classes of unconventional myosins (for review see Cheney and Mooseker, 1995; Sellers and Goodson, 1995).”
BackgroundEnzymatic Characterization and Functional Domain Mapping of Brain Myosin-V
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Self-citationTwo Components of Actin-based Retrograde Flow in Sea Urchin Coelomocytes
Henson, J. H., Svitkina, T., Burns, A. R., Hughes, H. E., MacPartland, K. J., Nazarian, R., & Borisy, G. G. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.12.4075 · Cited by 123
“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
Hasson, T., Walsh, J. C., Cable, J., Mooseker, M. S., Brown, S. D. M., & Steel, K. P. (1997) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(1997)37:2 · Cited by 122
Self-citationA Novel Fungal Gene Encoding Chitin Synthase with a Myosin Motor-like Domain
FUJIWARA, M. T., Horiuchi, H., Ohta, A., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6907 · Cited by 119
Plasticity of the brush border — the yin and yang of intestinal homeostasis
Delacour, D., Salomon, J., Robine, S., & Louvard, D. (2016) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.5 · Cited by 118
Wirth, J. A., Jensen, K. A., Post, P. L., Bement, W. M., & Mooseker, M. S. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.3.653 · Cited by 112
Self-citationFunctions of unconventional myosins
Wu, X., Jung, G., & Hammer, J. A. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)00055-1 · Cited by 113
Inhibitory Regulation of Higher-Plant Myosin by Ca2+Ions1
Yokota, E., Muto, S., & Shimmen, T. (1999) · PLANT PHYSIOLOGY · doi:10.1104/pp.119.1.231 · Cited by 112
An intact SH3 domain is required for myosin I‐induced actin polymerization
Geli, M., Lombardi, R., Schmelzl, B., & Riezman, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4281 · Cited by 111
A novel class of unconventional myosins from Toxoplasma gondii
Heintzelman, M. B., & Schwartzman, J. D. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1167 · Cited by 112
Molecular etiology of arthrogryposis in multiple families of mostly Turkish origin
Bayram, Y., Karaca, E., Coban‐Akdemir, Z., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84457 · Cited by 111
“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.
Weston, M. D., Kelley, P. M., Overbeck, L. D., Wagenaar, M., Orten, D. J., Hasson, T., Chen, Z., Corey, D. P., Mooseker, M. S., Sümegi, J., et al. (1996) · PubMed Central · Cited by 109
Self-citationHuman myosin-IXb is a mechanochemically active motor and a GAP for rho
Post, P. L., Bokoch, G., & Mooseker, M. S. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.7.941 · Cited by 106
Self-citationMyosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis
Cheng, J. C., Grassart, A., & Drubin, D. G. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-04-0383 · Cited by 108
“…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
Roth, D., Moseley, G. W., Glover, D. J., Pouton, C. W., & Jans, D. A. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00564.x · Cited by 103
Myosin at work: Motor adaptations for a variety of cellular functions
O’Connell, C. B., Tyska, M. J., & Mooseker, M. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.06.012 · Cited by 111
“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 101
Münchow, S., Sauter, C., & Jansen, R. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.10.1511 · Cited by 102
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
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
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
Motegi, F., Arai, R., & Mabuchi, I. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.5.1367 · Cited by 96
“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 98
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
Fifty Ways to Love Your Lever: Myosin Motors
Block, S. M. (1996) · Cell · doi:10.1016/s0092-8674(00)81332-x · Cited by 89
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
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
Nascimento, A. A. C., Amaral, R. G., Bizário, J. C. S., Larson, R. E., & Espreáfico, E. M. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.10.1971 · Cited by 90
“…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
“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
Lee, S.-F., Egelhoff, T. T., Mahasneh, A., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.27044 · Cited by 88
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
Myosin IXb is a single-headed minus-end-directed processive motor
Inoue, A., Saito, J., Ikebe, R., & Ikebe, M. (2002) · Nature Cell Biology · doi:10.1038/ncb774 · Cited by 87
Myosin Vb controls biogenesis of post-Golgi Rab10 carriers during axon development
Liu, Y., Xu, X., Chen, Q., Wang, T., Deng, C.-Y., Song, B., Du, J., & Luo, Z. (2013) · Nature Communications · doi:10.1038/ncomms3005 · Cited by 94
Septins may form a ubiquitous family of cytoskeletal filaments.
Cooper, J. A., & Kiehart, D. P. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.134.6.1345 · Cited by 84
Metadata
- 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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