MYO10
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Aliases | MYO10, myosin X, MyoX | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 601481; MGI: 107716; HomoloGene: 36328; GeneCards: MYO10; OMA:MYO10 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Myosin X, also known as MYO10, is a protein that in humans is encoded by the MYO10 gene.[5][6][7][8]
Myo10 is an actin-based motor protein that can localize to the tips of the finger-like cellular protrusions known as filopodia.[9][10] Myo10 is broadly expressed in mammalian tissues, although at relatively low levels.[8] Studies with knockout mice demonstrate that Myo10 has important functions in embryonic processes such as neural tube closure and eye development.[11][12][13] Myo10 also has important functions in cancer invasion and growth.[14][15][9][12][16][17]
Myo10 should not be confused with Myh10, which encodes the heavy chain of the class II myosin known as non-muscle myosin 2b.
Structure and function
[edit]![](http://178.128.105.246/content-http-upload.wikimedia.org/wikipedia/commons/thumb/6/68/Bar_Diagram_of_Full-length_and_Headless_MyoX.png/220px-Bar_Diagram_of_Full-length_and_Headless_MyoX.png)
The human MYO10 gene spans ~274 kb and is located on chromosome 5 band 5p15.1 (GRCh Ensembl release 89). It produces a full-length RNA transcript with 41 exons encoding a MYO10 heavy chain whose deduced sequence has 2058 amino acids and a predicted molecular weight of ~237 kDa. Like many motor proteins, the full-length Myo10 protein can be considered to consist of a head, neck, and tail.[8][21] The N-terminal head or myosin motor domain can bind to an actin filament, hydrolyze ATP, and produce force.[22][23] The neck or light chain binding domain consists of 3 IQ motifs, with each IQ motif providing a binding site for one molecule of calmodulin, a ~16.5 kDa calcium-binding protein.[22] Unlike most calmodulin binding sites, which only bind to calmodulin in the presence of calcium, the IQ motifs in Myo10 can bind to calmodulin in the absence of calcium. The Myo10 IQ motifs have also been reported to bind CALML3, a calmodulin-like protein expressed in epithelial cells, so CALML3 may serve as a Myo10 light chain in place of calmodulin in some situations.[24] The Myo10 tail begins with an alpha-helical region whose proximal portion forms a single, stable alpha helix (SAH domain) that lengthens the lever arm formed by the neck domain.[25][26] The distal portion of the alpha helical region can self-associate with a Kd of ~0.6 uM to form an antiparallel coiled coil, allowing two Myo10 heavy chains to form an antiparallel dimer, a unique structure among known myosins.[26][27]
The Myo10 tail includes several regions in addition to the SAH and coiled coil. These include a region with 3 PEST sequences—sequences enriched in the amino acids Proline (P), Glutamine (E), Serine (S), and T (Threonine) that are often associated with cleavage by proteases such as calpain.[8] The Myo10 tail is unique among known myosins in containing 3 PH domains (Pleckstrin Homology domain), a domain often involved in binding to membranes. The sequence of Myo10's first PH domain is somewhat unusual in that it is split by the presence of a surface loop that contains the second PH domain.[8][19] The second PH domain binds to the important signaling lipid phosphatidylinositol (3,4,5)-trisphosphate [PI(3,4,5)P3] and in some situations has been reported to bind to phosphatidylinositol (4,5)-bisphosphate [PI(4,5)P2].[28][19][29] Myo10's 3 PH domains are thought to work together to recruit it to the plasma membrane. The Myo10 tail ends in a supramodule consisting of a MyTH4 domain (Myosin Tail Homology 4) and a FERM domain (band 4.1, Ezrin, Radixin, Moesin).[18][20] Myo10's MyTH4 domain can bind to microtubules with a reported affinity of ~0.24 uM and gives full-length Myo10 the important ability to link an actin filament bound by its head to a microtubule bound by its tail.[30][18][31] The Myo10 FERM domain can bind to the cytoplasmic domains of several β-integrins, a major class of cell adhesion receptor, and to the cytoplasmic domains of the netrin receptors Deleted in Colorectal Cancer (DCC) and neogenin (Neo1).[32][33] Although full-length Myo10 protein appears to be expressed at relatively low levels, it can be detected in most mammalian tissues including brain, testes, kidney, lung, stomach, and pancreas.[8]
The native full-length Myo10 heavy chain can exist as a monomer with 3 calmodulin/calmodulin-like light chains or as an antiparallel dimer with 6 calmodulin/calmodulin-like light chains. An antiparallel Myo10 dimer with all 6 light chains would thus have 8 subunits and a native MW of ~574 kDa. Importantly, the tail in a Myo10 monomer can fold back onto the head to inhibit the head's motor activity.[29] Increases in plasma membrane PI(3,4,5)P3 levels are hypothesized to recruit Myo10 monomers to the plasma membrane via their PH domains, activating their motor activity and increasing their local concentration, leading to the formation of active antiparallel dimers that are capable moving along actin filaments. Myo10, like all known myosins other than Myo6, moves towards the barbed end of the actin filament.[34] Myo10 is capable of hydrolyzing ~10-20 ATP/s per head and has been reported to generate movement at rates of ~300-1500 nm/s.[23][27] Single-molecule studies show that native Myo10 dimers can take steps of up to ~55 nm, which are among the largest steps reported for a motor protein.[27] Myo10's large step size is due in part to the long lever arm formed by its neck domain and stable alpha helix, and in part due to the remarkably large swing of ~120° the Myo10 lever arm undergoes during its power stroke.[27] There is much interest in the mechanisms that target Myo10 to filopodial actin bundles, and in Myo10's ability to step from one actin filament in a bundle to another.[35][27][36] In addition to the full-length Myo10 described above, the use of alternative transcription start sites located in intron 19-20 of the full-length transcript results in the production of "headless" Myo10 transcripts that lack most of the myosin head domain, but include the rest of the Myo10 heavy chain.[37][38][39] The major headless transcripts in human are predicted to include exons 20-41 of full-length MYO10 and initiation of translation at M644 would result in a 1415 amino acid headless protein with a predicted MW of ~163 kDa that would be identical to amino acids 644-2058 of full-length MYO10.[37] Because headless Myo10 lacks most of the head domain, it lacks motor activity, but it retains all of Myo10's other domains and is thus expected to retain the ability to bind to light chains of the calmodulin superfamily, to membranes containing PI(3,4,5)P3 or PI(4,5)P3, to microtubules, and to proteins that bind the Myo10 tail such as DCC, neogenin, and β-integrins. Headless Myo10 has been hypothesized to act as a scaffolding protein for its various binding partners and/or as a "natural" dominant negative that can inhibit the actions of full-length Myo10.[37][38]
Evolutionary relationships
[edit]Myo10 is a member of an evolutionarily ancient group of myosins whose tails contain MyTH4-FERM domains and that have been shown to have important functions in cellular protrusions based on actin bundles such as filopodia, microvilli, and inner ear stereocilia.[40][41] The slime mold Dictyostelium expresses a MyTH4-FERM myosin known as myosin-7 that is involved in filopodia formation and has 2 MyTH4-FERM supramodules but no PH domains.[40] Myo10 appears to have originated from an ancestral myosin-7-like protein approximately a billion years ago by several changes including loss of 1 MyTH4-FERM supramodule and addition of 3 PH domains. A Myo10 gene is present in organisms ranging from filozoans and choanoflagellates (the protozoan groups most closely related to multicellular animals) to humans.[40] Myo10 was lost in the invertebrate lineages leading to organisms such as fruit flies and nematodes, although these lineages do express other MyTH4-FERM myosins such as myosin-7. Humans express 3 MyTH4-FERM myosins in addition to Myo10: MYO7A, the gene that is mutated in Usher syndrome 1b deaf-blindness; MYO7B, a component of an adhesion complex at the tips of microvilli; and MYO15A, a myosin that localizes to the tips of inner ear stereocilia and that is mutated in DFNB3 deafness.[41] The head domains of the other MyTH4-FERM myosins expressed in human exhibit at most 45% overall amino acid sequence identity with Myo10 and their tail domains each contain 2 MyTH4-FERM domains instead of the 3 PH domains and 1 MyTH4-FERM domain in Myo10.[8][41]
Cellular function
[edit]![](http://178.128.105.246/content-http-upload.wikimedia.org/wikipedia/commons/thumb/a/a0/Fluorescence_image_of_a_cell_showing_localization_of_Myo10_at_the_tips_of_filopodia.png/220px-Fluorescence_image_of_a_cell_showing_localization_of_Myo10_at_the_tips_of_filopodia.png)
Myo10 can localize to the tips of filopodia, a property most other myosins lack. When Myo10 was tagged with Green Fluorescent Protein (GFP) and expressed in cells, small puncta of GFP-Myo10 were observed moving forward within filopodia towards the tip at rates of ~100 nm/s.[42] Imaging with single-molecule sensitivity revealed similar movements of individual Myo10 dimers at rates of ~600-1400 nm/s.[43][44][45] GFP-Myo10 also moves rearward in filopodia at retrograde flow rates of ~15 nm/s. These observations led to the hypothesis that Myo10 molecules use their motor activity to move themselves rapidly forward along filopodial actin filaments and can bind to filopodial actin filaments to be carried slowly rearward by retrograde actin flow.[42] This "intrafilopodial motility" of Myo10 has led to suggestions that Myo10 functions as a motor protein for transporting cargos within filopodia. Myo10 also has important functions in the formation and/or stabilization of filopodia, with Myo10 overexpression increasing the number and length of filopodia, while knockdown or knockout of Myo10 decreases filopodia.[42][46][47] Myo10 also has important functions in cell division, particularly in mitotic spindle orientation.[30][48][49][50] Myo10 is also required to cluster the excess centrosomes that are a hallmark of cancer cells,[49] a process of great interest because cancer cells need to cluster their centrosomes to successfully divide.
Role in disease
[edit]Growing evidence demonstrates that Myo10 has important roles in cancer.[9] In addition to its role in clustering the excess centrosomes of cancer cells,[49] Myo10 is a key component of invadopodia, filopodia-related protrusions that cancer cells use to invade their surroundings.[51] Several microRNAs that suppress cancer cell invasion have also been reported to act in part by targeting the Myo10 mRNA.[52][53] Knockout or knockdown of Myo10 is reported to suppress cancer cell invasion or spread in experimental models of breast cancer,[14][15] lung cancer,[17] and glioma,[16] where knockout of Myo10 also increased the effectiveness of an otherwise ineffective chemotherapy agent. These results, plus research showing that knockout of Myo10 increased survival time by 260% in a mouse model of melanoma,[12] make Myo10 a potential anti-cancer target.
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000145555 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022272 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: MYO10 myosin X".
- ^ Bement WM, Hasson T, Wirth JA, Cheney RE, Mooseker MS (July 1994). "Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types". Proceedings of the National Academy of Sciences of the United States of America. 91 (14): 6549–53. Bibcode:1994PNAS...91.6549B. doi:10.1073/pnas.91.14.6549. PMC 44240. PMID 8022818.
- ^ Hasson T, Skowron JF, Gilbert DJ, Avraham KB, Perry WL, Bement WM, et al. (September 1996). "Mapping of unconventional myosins in mouse and human". Genomics. 36 (3): 431–9. doi:10.1006/geno.1996.0488. PMID 8884266.
- ^ a b c d e f g h Berg JS, Derfler BH, Pennisi CM, Corey DP, Cheney RE (October 2000). "Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin". Journal of Cell Science. 113. 113 Pt 19 (19): 3439–51. doi:10.1242/jcs.113.19.3439. PMID 10984435.
- ^ a b c Courson DS, Cheney RE (May 2015). "Myosin-X and disease". Experimental Cell Research. 334 (1): 10–5. doi:10.1016/j.yexcr.2015.03.014. PMC 4433855. PMID 25819274.
- ^ Tokuo H (2020). "Myosin X". Myosins. Advances in Experimental Medicine and Biology. Vol. 1239. pp. 391–403. doi:10.1007/978-3-030-38062-5_17. ISBN 978-3-030-38061-8. PMID 32451868. S2CID 218892501.
- ^ Heimsath EG, Yim YI, Mustapha M, Hammer JA, Cheney RE (December 2017). "Myosin-X knockout is semi-lethal and demonstrates that myosin-X functions in neural tube closure, pigmentation, hyaloid vasculature regression, and filopodia formation". Scientific Reports. 7 (1): 17354. Bibcode:2017NatSR...717354H. doi:10.1038/s41598-017-17638-x. PMC 5725431. PMID 29229982.
- ^ a b c Tokuo H, Bhawan J, Coluccio LM (July 2018). "Myosin X is required for efficient melanoblast migration and melanoma initiation and metastasis". Scientific Reports. 8 (1): 10449. Bibcode:2018NatSR...810449T. doi:10.1038/s41598-018-28717-y. PMC 6041326. PMID 29993000.
- ^ Bachg AC, Horsthemke M, Skryabin BV, Klasen T, Nagelmann N, Faber C, et al. (January 2019). "Phenotypic analysis of Myo10 knockout (Myo10tm2/tm2) mice lacking full-length (motorized) but not brain-specific headless myosin X". Scientific Reports. 9 (1): 597. Bibcode:2019NatSR...9..597B. doi:10.1038/s41598-018-37160-y. PMC 6345916. PMID 30679680.
- ^ a b Arjonen A, Kaukonen R, Mattila E, Rouhi P, Högnäs G, Sihto H, et al. (March 2014). "Mutant p53-associated myosin-X upregulation promotes breast cancer invasion and metastasis". The Journal of Clinical Investigation. 124 (3): 1069–82. doi:10.1172/JCI67280. PMC 3934176. PMID 24487586.
- ^ a b Cao R, Chen J, Zhang X, Zhai Y, Qing X, Xing W, et al. (July 2014). "Elevated expression of myosin X in tumours contributes to breast cancer aggressiveness and metastasis". British Journal of Cancer. 111 (3): 539–50. doi:10.1038/bjc.2014.298. PMC 4119973. PMID 24921915.
- ^ a b Kenchappa RS, Mistriotis P, Wisniewski E, Bhattacharya S, Kulkarni T, West R, et al. (December 2020). "Myosin 10 Regulates Invasion, Mitosis, and Metabolic Signaling in Glioblastoma". iScience. 23 (12): 101802. Bibcode:2020iSci...23j1802K. doi:10.1016/j.isci.2020.101802. PMC 7702012. PMID 33299973.
- ^ a b Summerbell ER, Mouw JK, Bell JS, Knippler CM, Pedro B, Arnst JL, et al. (July 2020). "Epigenetically heterogeneous tumor cells direct collective invasion through filopodia-driven fibronectin micropatterning". Science Advances. 6 (30): eaaz6197. Bibcode:2020SciA....6.6197S. doi:10.1126/sciadv.aaz6197. PMC 7439406. PMID 32832657.
- ^ a b c Hirano, Y., Hatano, T., Takahashi, A., Toriyama, M., Inagaki, N., and Hakoshima, T. (2011). Structural basis of cargo recognition by the myosin-X MyTH4-FERM domain. The EMBO journal 30, 2734-2747.
- ^ a b c Lu, Q., Yu, J., Yan, J., Wei, Z., and Zhang, M. (2011). Structural basis of the myosin X PH1(N)-PH2-PH1(C) tandem as a specific and acute cellular PI(3,4,5)P(3) sensor. Mol Biol Cell 22, 4268-4278.
- ^ a b Wei Z, Yan J, Lu Q, Pan L, Zhang M (March 2011). "Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain". Proceedings of the National Academy of Sciences of the United States of America. 108 (9): 3572–7. Bibcode:2011PNAS..108.3572W. doi:10.1073/pnas.1016567108. PMC 3048157. PMID 21321230.
- ^ Kerber ML, Cheney RE (November 2011). "Myosin-X: a MyTH-FERM myosin at the tips of filopodia". Journal of Cell Science. 124 (Pt 22): 3733–41. doi:10.1242/jcs.023549. PMC 3225264. PMID 22124140.
- ^ a b Homma K, Saito J, Ikebe R, Ikebe M (September 2001). "Motor function and regulation of myosin X". The Journal of Biological Chemistry. 276 (36): 34348–54. doi:10.1074/jbc.M104785200. PMID 11457842. S2CID 46029622.
- ^ a b Takagi Y, Farrow RE, Billington N, Nagy A, Batters C, Yang Y, et al. (May 2014). "Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load". Proceedings of the National Academy of Sciences of the United States of America. 111 (18): E1833-42. Bibcode:2014PNAS..111E1833T. doi:10.1073/pnas.1320122111. PMC 4020102. PMID 24753602.
- ^ Caride AJ, Bennett RD, Strehler EE (September 2010). "Kinetic analysis reveals differences in the binding mechanism of calmodulin and calmodulin-like protein to the IQ motifs of myosin-10". Biochemistry. 49 (37): 8105–16. doi:10.1021/bi100644q. PMC 3818122. PMID 20731332.
- ^ Knight PJ, Thirumurugan K, Xu Y, Wang F, Kalverda AP, Stafford WF, et al. (October 2005). "The predicted coiled-coil domain of myosin 10 forms a novel elongated domain that lengthens the head". The Journal of Biological Chemistry. 280 (41): 34702–8. doi:10.1074/jbc.M504887200. PMID 16030012. S2CID 22503825.
- ^ a b Lu Q, Ye F, Wei Z, Wen Z, Zhang M (October 2012). "Antiparallel coiled-coil-mediated dimerization of myosin X". Proceedings of the National Academy of Sciences of the United States of America. 109 (43): 17388–93. doi:10.1073/pnas.1208642109. PMC 3491486. PMID 23012428.
- ^ a b c d e Ropars V, Yang Z, Isabet T, Blanc F, Zhou K, Lin T, et al. (September 2016). "The myosin X motor is optimized for movement on actin bundles". Nature Communications. 7: 12456. Bibcode:2016NatCo...712456R. doi:10.1038/ncomms12456. PMC 5025751. PMID 27580874.
- ^ Plantard L, Arjonen A, Lock JG, Nurani G, Ivaska J, Strömblad S (October 2010). "PtdIns(3,4,5)P₃ is a regulator of myosin-X localization and filopodia formation". Journal of Cell Science. 123 (Pt 20): 3525–34. doi:10.1242/jcs.069609. PMID 20930142. S2CID 2070375.
- ^ a b Umeki N, Jung HS, Sakai T, Sato O, Ikebe R, Ikebe M (June 2011). "Phospholipid-dependent regulation of the motor activity of myosin X". Nature Structural & Molecular Biology. 18 (7): 783–8. doi:10.1038/nsmb.2065. PMID 21666676. S2CID 9755324.
- ^ a b Weber KL, Sokac AM, Berg JS, Cheney RE, Bement WM (September 2004). "A microtubule-binding myosin required for nuclear anchoring and spindle assembly". Nature. 431 (7006): 325–9. Bibcode:2004Natur.431..325W. doi:10.1038/nature02834. PMID 15372037. S2CID 4342360.
- ^ Planelles-Herrero VJ, Blanc F, Sirigu S, Sirkia H, Clause J, Sourigues Y, et al. (May 2016). "Myosin MyTH4-FERM structures highlight important principles of convergent evolution". Proceedings of the National Academy of Sciences of the United States of America. 113 (21): E2906-15. Bibcode:2016PNAS..113E2906P. doi:10.1073/pnas.1600736113. PMC 4889382. PMID 27166421.
- ^ Zhang H, Berg JS, Li Z, Wang Y, Lång P, Sousa AD, et al. (June 2004). "Myosin-X provides a motor-based link between integrins and the cytoskeleton". Nature Cell Biology. 6 (6): 523–31. doi:10.1038/ncb1136. PMID 15156152. S2CID 24260820.
- ^ Zhu XJ, Wang CZ, Dai PG, Xie Y, Song NN, Liu Y, et al. (February 2007). "Myosin X regulates netrin receptors and functions in axonal path-finding". Nature Cell Biology. 9 (2): 184–92. doi:10.1038/ncb1535. PMID 17237772. S2CID 7012749.
- ^ Homma K, Ikebe M (August 2005). "Myosin X is a high duty ratio motor". The Journal of Biological Chemistry. 280 (32): 29381–91. doi:10.1074/jbc.M504779200. PMID 15961399. S2CID 22330459.
- ^ Brawley CM, Rock RS (June 2009). "Unconventional myosin traffic in cells reveals a selective actin cytoskeleton". Proceedings of the National Academy of Sciences of the United States of America. 106 (24): 9685–90. Bibcode:2009PNAS..106.9685B. doi:10.1073/pnas.0810451106. PMC 2701044. PMID 19478066.
- ^ Vavra KC, Xia Y, Rock RS (June 2016). "Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection". Biophysical Journal. 110 (11): 2517–2527. Bibcode:2016BpJ...110.2517V. doi:10.1016/j.bpj.2016.04.048. PMC 4906270. PMID 27276269.
- ^ a b c Sousa AD, Berg JS, Robertson BW, Meeker RB, Cheney RE (January 2006). "Myo10 in brain: developmental regulation, identification of a headless isoform and dynamics in neurons". Journal of Cell Science. 119 (Pt 1): 184–94. doi:10.1242/jcs.02726. PMID 16371656. S2CID 3085103.
- ^ a b Raines AN, Nagdas S, Kerber ML, Cheney RE (July 2012). "Headless Myo10 is a negative regulator of full-length Myo10 and inhibits axon outgrowth in cortical neurons". The Journal of Biological Chemistry. 287 (30): 24873–83. doi:10.1074/jbc.M112.369173. PMC 3408153. PMID 22661706.
- ^ Lai M, Li L, Ju X, Yu H, Zhu X (2013). "Cloning, characterization, and promoter analysis of mouse Myo10 gene". Nucleosides, Nucleotides & Nucleic Acids. 32 (7): 354–65. doi:10.1080/15257770.2013.790551. PMID 23742061. S2CID 1942016.
- ^ a b c Petersen KJ, Goodson HV, Arthur AL, Luxton GW, Houdusse A, Titus MA (December 2016). "MyTH4-FERM myosins have an ancient and conserved role in filopod formation". Proceedings of the National Academy of Sciences of the United States of America. 113 (50): E8059–E8068. Bibcode:2016PNAS..113E8059P. doi:10.1073/pnas.1615392113. PMC 5167205. PMID 27911821.
- ^ a b c Weck ML, Grega-Larson NE, Tyska MJ (February 2017). "MyTH4-FERM myosins in the assembly and maintenance of actin-based protrusions". Current Opinion in Cell Biology. 44: 68–78. doi:10.1016/j.ceb.2016.10.002. PMC 5403704. PMID 27836411.
- ^ a b c Berg JS, Cheney RE (March 2002). "Myosin-X is an unconventional myosin that undergoes intrafilopodial motility". Nature Cell Biology. 4 (3): 246–50. doi:10.1038/ncb762. PMID 11854753. S2CID 22683743.
- ^ Kerber ML, Jacobs DT, Campagnola L, Dunn BD, Yin T, Sousa AD, et al. (June 2009). "A novel form of motility in filopodia revealed by imaging myosin-X at the single-molecule level". Current Biology. 19 (11): 967–73. Bibcode:2009CBio...19..967K. doi:10.1016/j.cub.2009.03.067. PMC 2817954. PMID 19398338.
- ^ Watanabe TM, Tokuo H, Gonda K, Higuchi H, Ikebe M (June 2010). "Myosin-X induces filopodia by multiple elongation mechanism". The Journal of Biological Chemistry. 285 (25): 19605–14. doi:10.1074/jbc.M109.093864. PMC 2885239. PMID 20392702.
- ^ Baboolal TG, Mashanov GI, Nenasheva TA, Peckham M, Molloy JE (October 2016). "A Combination of Diffusion and Active Translocation Localizes Myosin 10 to the Filopodial Tip". The Journal of Biological Chemistry. 291 (43): 22373–22385. doi:10.1074/jbc.M116.730689. PMC 5077179. PMID 27566544.
- ^ Bohil AB, Robertson BW, Cheney RE (August 2006). "Myosin-X is a molecular motor that functions in filopodia formation". Proceedings of the National Academy of Sciences of the United States of America. 103 (33): 12411–6. Bibcode:2006PNAS..10312411B. doi:10.1073/pnas.0602443103. PMC 1567893. PMID 16894163.
- ^ Tokuo H, Mabuchi K, Ikebe M (October 2007). "The motor activity of myosin-X promotes actin fiber convergence at the cell periphery to initiate filopodia formation". The Journal of Cell Biology. 179 (2): 229–38. doi:10.1083/jcb.200703178. PMC 2064759. PMID 17954606.
- ^ Toyoshima F, Nishida E (March 2007). "Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner". The EMBO Journal. 26 (6): 1487–98. doi:10.1038/sj.emboj.7601599. PMC 1829369. PMID 17318179.
- ^ a b c Kwon M, Bagonis M, Danuser G, Pellman D (August 2015). "Direct Microtubule-Binding by Myosin-10 Orients Centrosomes toward Retraction Fibers and Subcortical Actin Clouds". Developmental Cell. 34 (3): 323–37. doi:10.1016/j.devcel.2015.06.013. PMC 4672950. PMID 26235048.
- ^ Sandquist JC, Larson ME, Woolner S, Ding Z, Bement WM (March 2018). "An interaction between myosin-10 and the cell cycle regulator Wee1 links spindle dynamics to mitotic progression in epithelia". The Journal of Cell Biology. 217 (3): 849–859. doi:10.1083/jcb.201708072. PMC 5839792. PMID 29321170.
- ^ Schoumacher M, Goldman RD, Louvard D, Vignjevic DM (May 2010). "Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia". The Journal of Cell Biology. 189 (3): 541–56. doi:10.1083/jcb.200909113. PMC 2867303. PMID 20421424.
- ^ Sun Y, Ai X, Shen S, Lu S (April 2015). "NF-κB-mediated miR-124 suppresses metastasis of non-small-cell lung cancer by targeting MYO10". Oncotarget. 6 (10): 8244–54. doi:10.18632/oncotarget.3135. PMC 4480748. PMID 25749519.
- ^ Wang X, Li J, Xu X, Zheng J, Li Q (July 2018). "miR-129 inhibits tumor growth and potentiates chemosensitivity of neuroblastoma by targeting MYO10". Biomedicine & Pharmacotherapy. 103: 1312–1318. doi:10.1016/j.biopha.2018.04.153. PMID 29864913. S2CID 46926904.
Further reading
[edit]- Hasson T, Skowron JF, Gilbert DJ, Avraham KB, Perry WL, Bement WM, et al. (September 1996). "Mapping of unconventional myosins in mouse and human". Genomics. 36 (3): 431–9. doi:10.1006/geno.1996.0488. PMID 8884266.
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, et al. (October 1998). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.
- Rojas K, Serrano de la Peña L, Gallardo T, Simmons A, Nyce K, McGrath R, et al. (December 1999). "Physical map and characterization of transcripts in the candidate interval for familial chondrocalcinosis at chromosome 5p15.1". Genomics. 62 (2): 177–83. doi:10.1006/geno.1999.5997. PMID 10610710.
- Rogers MS, Strehler EE (April 2001). "The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X". The Journal of Biological Chemistry. 276 (15): 12182–9. doi:10.1074/jbc.M010056200. PMID 11278607.
- Cox D, Berg JS, Cammer M, Chinegwundoh JO, Dale BM, Cheney RE, Greenberg S (July 2002). "Myosin X is a downstream effector of PI(3)K during phagocytosis". Nature Cell Biology. 4 (7): 469–77. doi:10.1038/ncb805. PMID 12055636. S2CID 24127183.
- Navarro-Lérida I, Martínez Moreno M, Roncal F, Gavilanes F, Albar JP, Rodríguez-Crespo I (February 2004). "Proteomic identification of brain proteins that interact with dynein light chain LC8". Proteomics. 4 (2): 339–46. doi:10.1002/pmic.200300528. PMID 14760703. S2CID 8868600.
- Zhang H, Berg JS, Li Z, Wang Y, Lång P, Sousa AD, et al. (June 2004). "Myosin-X provides a motor-based link between integrins and the cytoskeleton". Nature Cell Biology. 6 (6): 523–31. doi:10.1038/ncb1136. PMID 15156152. S2CID 24260820.
- Tokuo H, Ikebe M (June 2004). "Myosin X transports Mena/VASP to the tip of filopodia". Biochemical and Biophysical Research Communications. 319 (1): 214–20. doi:10.1016/j.bbrc.2004.04.167. PMID 15158464.
- Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, et al. (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
- Sousa AD, Berg JS, Robertson BW, Meeker RB, Cheney RE (January 2006). "Myo10 in brain: developmental regulation, identification of a headless isoform and dynamics in neurons". Journal of Cell Science. 119 (Pt 1): 184–94. doi:10.1242/jcs.02726. PMID 16371656.
- Bohil AB, Robertson BW, Cheney RE (August 2006). "Myosin-X is a molecular motor that functions in filopodia formation". Proceedings of the National Academy of Sciences of the United States of America. 103 (33): 12411–6. Bibcode:2006PNAS..10312411B. doi:10.1073/pnas.0602443103. PMC 1567893. PMID 16894163.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.