CoChat
Sign Up
Cited by 1Hearing, Cochlea, Tinnitus, GeneticsGenetic and Kidney Cyst DiseasesAdvanced Fluorescence Microscopy Techniques

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Single-molecule fluorescence microscopy reveals regulatory mechanisms of MYO7A-driven cargo transport in stereocilia of live inner ear hair cells

Open access
Miyoshi, Takushi, Vishwasrao, Harshad D., Belyantseva, Inna A., Miyoshi, Junko, Sajeevadathan, Mrudhula, Ishibashi, Yasuko, Adadey, Samuel M., Harada, Narinobu, Shroff, Hari, Friedman, Thomas B.·2025·Nature Communications
DOI 10.1038/s41467-025-63102-0PMC PMC12402077

Published version of a preprint

Open this paper in CoChat — free accountOpen PDF

Abstract

Stereocilia are F-actin-based cylindrical protrusions on the apical surface of inner ear hair cells that function as biological mechanosensors of sound and acceleration. During stereocilia development, specific unconventional myosins transport proteins and phospholipids as cargo and mediate elongation, differentiation and acquisition of the mechanoelectrical transduction (MET). How unconventional myosins localize themselves and cargo in stereocilia using energy from ATP hydrolysis is only partially understood. Here, we developed STELLA-SPIM microscopy to visualize movement of single myosin molecules in live hair cell stereocilia. STELLA-SPIM demonstrated that MYO7A, a component of MET machinery, shows processive movement toward stereocilia tips when chemically dimerized or constitutively activated by missense mutations disabling tail-mediated autoinhibition. Conversely, MYO7A shows step-wise but not processive movement in stereocilia when its tail is tethered to the plasma membrane or F-actin in the presence of MYO7A interacting partners. We posit that MYO7A dimerizes and moves processively in stereocilia when unleashed from autoinhibition.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/s41467-025-63102-0

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 121

  1. Olusanya, B. O., Davis, A. C. & Hoffman, H. J. Hearing loss: rising prevalence and impact. Bull. World Health Organ 97, 646–646A (2019). · DOI
  2. Tanna, R. J., Lin, J. W. & De Jesus, O. Sensorineural Hearing Loss, <https://www.ncbi.nlm.nih.gov/pubmed/33351419> (2024).
  3. Eatock, R. A. & Lysakowski, A. In Vertebrate Hair Cells (eds Ruth A. E., Fay R. R., & Popper A. N.) 348–442 (Springer New York, 2006). · DOI
  4. Sekerkova, G. et al. Espins are multifunctional actin cytoskeletal regulatory proteins in the microvilli of chemosensory and mechanosensory cells. J. Neurosci. 24, 5445–5456 (2004). · DOI
  5. Gillespie, P. G. & Muller, U. Mechanotransduction by hair cells: models, molecules, and mechanisms. Cell 139, 33–44 (2009). · DOI
  6. Corey, D. P. & Hudspeth, A. J. Ionic basis of the receptor potential in a vertebrate hair cell. Nature 281, 675–677 (1979). · DOI
  7. Glowatzki, E. & Fuchs, P. A. Transmitter release at the hair cell ribbon synapse. Nat. Neurosci. 5, 147–154 (2002). · DOI
  8. Corey, D. P. & Hudspeth, A. J. Kinetics of the receptor current in bullfrog saccular hair cells. J. Neurosci.: Off. J. Soc. Neurosci. 3, 962–976 (1983). · DOI
  9. Wong, A. C. & Ryan, A. F. Mechanisms of sensorineural cell damage, death and survival in the cochlea. Front. Aging Neurosci. 7, 58 (2015). · DOI
  10. Lv, J. et al. AAV1-hOTOF gene therapy for autosomal recessive deafness 9: a single-arm trial. Lancet. https://doi.org/10.1016/S0140-6736(23)02874-X. (2024) · DOI
  11. Qi, J. et al. AAV-mediated gene therapy restores hearing in patients with DFNB9 deafness. Adv. Sci. 11, e2306788 (2024). · DOI
  12. Wang, H. et al. Hair cell-specific Myo15 promoter-mediated gene therapy rescues hearing in DFNB9 mouse model. Mol. Ther. Nucleic Acids 35, 102135 (2024). · DOI
  13. Duan, M., Venail, F., Spencer, N. & Mezzina, M. Treatment of peripheral sensorineural hearing loss: gene therapy. Gene Ther. 11, S51–S56 (2004). · DOI
  14. Miyoshi, T., Belyantseva, I. A., Sajeevadathan, M. & Friedman, T. B. Pathophysiology of human hearing loss associated with variants in myosins. Front Physiol. 15, 1374901 (2024). · DOI
  15. Moreland, Z. G. & Bird, J. E. Myosin motors in sensory hair bundle assembly. Curr. Opin. cell Biol. 79, 102132 (2022). · DOI
  16. Li, J. & Zhang, M. Cargo binding by unconventional myosins. Adv. Exp. Med Biol. 1239, 21–40 (2020). · DOI
  17. Grati, M. & Kachar, B. Myosin VIIa and sans localization at stereocilia upper tip-link density implicates these Usher syndrome proteins in mechanotransduction. Proc. Natl. Acad. Sci. USA 108, 11476–11481 (2011). · DOI
  18. Dionne, G. et al. Mechanotransduction by PCDH15 Relies on a Novel cis-Dimeric Architecture. Neuron 99, 480–492 e485 (2018). · DOI
  19. Jaiganesh, A. et al. Zooming in on Cadherin-23: structural diversity and potential mechanisms of inherited deafness. Structure 26, 1210–1225 e1214 (2018). · DOI
  20. Grillet, N. et al. Harmonin mutations cause mechanotransduction defects in cochlear hair cells. Neuron 62, 375–387 (2009). · DOI
  21. Giese, A. P. J. et al. CIB2 interacts with TMC1 and TMC2 and is essential for mechanotransduction in auditory hair cells. Nat. Commun. 8, 43 (2017). · DOI
  22. Kurima, K. et al. TMC1 and TMC2 Localize at the Site of Mechanotransduction in mammalian inner ear hair cell stereocilia. Cell Rep. 12, 1606–1617 (2015). · DOI
  23. Trouillet, A. et al. Loxhd1 mutations cause mechanotransduction defects in cochlear hair cells. J. Neurosci. 41, 3331–3343 (2021). · DOI
  24. Zhao, B. et al. TMIE is an essential component of the mechanotransduction machinery of cochlear hair cells. Neuron 84, 954–967 (2014). · DOI
  25. Naz, S. et al. Mutations in a novel gene, TMIE, are associated with hearing loss linked to the DFNB6 locus. Am. J. Hum. Genet. 71, 632–636 (2002). · DOI
  26. Boeda, B. et al. Myosin VIIa, harmonin and cadherin 23, three Usher I gene products that cooperate to shape the sensory hair cell bundle. EMBO J. 21, 6689–6699 (2002). · DOI
  27. Lefevre, G. et al. A core cochlear phenotype in USH1 mouse mutants implicates fibrous links of the hair bundle in its cohesion, orientation and differential growth. Development 135, 1427–1437 (2008). · DOI
  28. Senften, M. et al. Physical and functional interaction between protocadherin 15 and myosin VIIa in mechanosensory hair cells. J. Neurosci. 26, 2060–2071 (2006). · DOI
  29. Belyantseva, I. A. et al. Myosin-XVa is required for tip localization of whirlin and differential elongation of hair-cell stereocilia. Nat. Cell Biol. 7, 148–156 (2005). · DOI
  30. Manor, U. et al. Regulation of stereocilia length by myosin XVa and whirlin depends on the actin-regulatory protein Eps8. Curr. Biol. 21, 167–172 (2011). · DOI
  31. Moreland, Z. G. et al. Myosin-based nucleation of actin filaments contributes to stereocilia development critical for hearing. Nat. Commun. 16, 947 (2025). · DOI
  32. Liu, H. et al. Myosin III-mediated cross-linking and stimulation of actin bundling activity of Espin. Elife 5. https://doi.org/10.7554/eLife.12856. (2016) · DOI
  33. Salles, F. T. et al. Myosin IIIa boosts elongation of stereocilia by transporting espin 1 to the plus ends of actin filaments. Nat. cell Biol. 11, 443–450 (2009). · DOI
  34. Ebrahim, S. et al. Stereocilia-staircase spacing is influenced by myosin III motors and their cargos espin-1 and espin-like. Nat. Commun. 7, 10833 (2016). · DOI
  35. Lelli, A. et al. Class III myosins shape the auditory hair bundles by limiting microvilli and stereocilia growth. J. Cell Biol. 212, 231–244 (2016). · DOI
  36. McGrath, J. et al. Actin at stereocilia tips is regulated by mechanotransduction and ADF/cofilin. Curr. Biol. https://doi.org/10.1016/j.cub.2020.12.006. (2020) · DOI
  37. Weil, D. et al. Defective myosin VIIA gene responsible for Usher syndrome type 1B. Nature 374, 60–61 (1995). · DOI · Paper page
  38. Yildiz, A. et al. Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 300, 2061–2065 (2003). · DOI
  39. Phichith, D. et al. Cargo binding induces dimerization of myosin VI. Proc. Natl. Acad. Sci. USA 106, 17320–17324 (2009). · DOI
  40. Shang, G. et al. Structure analyses reveal a regulated oligomerization mechanism of the PlexinD1/GIPC/myosin VI complex. Elife 6. https://doi.org/10.7554/eLife.27322. (2017) · DOI
  41. Yu, C. et al. Myosin VI undergoes cargo-mediated dimerization. Cell 138, 537–548 (2009). · DOI
  42. Chatterjee, P. et al. GIPC3 couples to MYO6 and PDZ domain proteins, and shapes the hair cell apical region. J. Cell Sci. 136. https://doi.org/10.1242/jcs.261100. (2023) · DOI
  43. El-Amraoui, A. et al. MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes. EMBO Rep. 3, 463–470 (2002). · DOI · Paper page
  44. Sakai, T., Umeki, N., Ikebe, R. & Ikebe, M. Cargo binding activates myosin VIIA motor function in cells. Proc. Natl. Acad. Sci. USA 108, 7028–7033 (2011). · DOI
  45. Peckham, M. Coiled coils and SAH domains in cytoskeletal molecular motors. Biochem. Soc. Trans. 39, 1142–1148 (2011). · DOI
  46. Simm, D., Hatje, K. & Kollmar, M. Distribution and evolution of stable single alpha-helices (SAH domains) in myosin motor proteins. PloS ONE 12, e0174639 (2017). · DOI
  47. De La Cruz, E. M. & Ostap, E. M. Relating biochemistry and function in the myosin superfamily. Curr. Opin. Cell Biol. 16, 61–67 (2004). · DOI
  48. Raval, M. H. et al. Impact of the motor and tail domains of class III myosins on regulating the formation and elongation of actin protrusions. J. Biol. Chem. 291, 22781–22792 (2016). · DOI
  49. Moreland, Z. G. et al. Phase separation of myosin-15 and centrin-2 contributes to stereocilia tip density formation. Biophys. J. 123, 276a (2024). · DOI
  50. Wu, Y. et al. Spatially isotropic four-dimensional imaging with dual-view plane illumination microscopy. Nat. Biotechnol. 31, 1032–1038 (2013). · DOI
  51. Miyoshi, T. et al. Semi-automated single-molecule microscopy screening of fast-dissociating specific antibodies directly from hybridoma cultures. Cell Rep. 34, 108708 (2021). · DOI
  52. Fitz, G. N., Weck, M. L., Bodnya, C., Perkins, O. L. & Tyska, M. J. Protrusion growth driven by myosin-generated force. Dev. cell 58, 18–33 e16 (2023). · DOI
  53. Umeki, N. et al. The tail binds to the head-neck domain, inhibiting ATPase activity of myosin VIIA. Proc. Natl. Acad. Sci. USA 106, 8483–8488 (2009). · DOI
  54. Yang, Y. et al. A FERM domain autoregulates Drosophila myosin 7a activity. Proc. Natl. Acad. Sci. USA 106, 4189–4194 (2009). · DOI
  55. Li, A., Xue, J. & Peterson, E. H. Architecture of the mouse utricle: macular organization and hair bundle heights. J. Neurophysiol. 99, 718–733 (2008). · DOI
  56. Belyantseva, I. A. Helios® gene gun-mediated transfection of the inner ear sensory epithelium: recent updates. Methods Mol. Biol. 1427, 3–26 (2016). · DOI
  57. Grimm, J. B. et al. A general method to improve fluorophores using deuterated auxochromes. JACS Au 1, 690–696 (2021). · DOI
  58. Drummond, M. C. et al. Live-cell imaging of actin dynamics reveals mechanisms of stereocilia length regulation in the inner ear. Nat. Commun. 6, 6873 (2015). · DOI
  59. Grimm, J. B. et al. Bright photoactivatable fluorophores for single-molecule imaging. Nat. methods 13, 985–988 (2016). · DOI
  60. Duda, R. O. & Hart, P. E. Pattern classification and scene analysis (Wiley, 1973).
  61. Endesfelder, U. & Heilemann, M. Direct stochastic optical reconstruction microscopy (dSTORM). Methods Mol. Biol. 1251, 263–276 (2015). · DOI
  62. Liao, X. et al. Myosin-dependent short actin filaments contribute to peripheral widening in developing stereocilia. Res. Sq. https://doi.org/10.21203/rs.3.rs-5448262/v1. (2024) · DOI
  63. Szent-Gyorgyi, A. G. Meromyosins, the subunits of myosin. Arch. Biochem. Biophys. 42, 305–320 (1953). · DOI
  64. Lowey, S. Myosin substructure: isolation of a helical subunit from heavy meromyosin. Science 145, 597–599 (1964). · DOI
  65. Matoo, S. et al. Comparative analysis of the MyTH4-FERM myosins reveals insights into the determinants of actin track selection in polarized epithelia. Mol. Biol. Cell 32, ar30 (2021). · DOI
  66. Clackson, T. et al. Redesigning an FKBP-ligand interface to generate chemical dimerizers with novel specificity. Proc. Natl. Acad. Sci. USA 95, 10437–10442 (1998). · DOI · Paper page
  67. Sato, O. et al. Human myosin VIIa is a very slow processive motor protein on various cellular actin structures. J. Biol. Chem. 292, 10950–10960 (2017). · DOI
  68. Kerber, M. L. et al. A novel form of motility in filopodia revealed by imaging myosin-X at the single-molecule level. Curr. Biol. 19, 967–973 (2009). · DOI
  69. Zhuravlev, P. I., Lan, Y., Minakova, M. S. & Papoian, G. A. Theory of active transport in filopodia and stereocilia. Proc. Natl. Acad. Sci. USA 109, 10849–10854 (2012). · DOI
  70. Sakai, T. et al. Structure and regulation of the movement of human myosin VIIA. J. Biol. Chem. 290, 17587–17598 (2015). · DOI
  71. Spink, B. J., Sivaramakrishnan, S., Lipfert, J., Doniach, S. & Spudich, J. A. Long single alpha-helical tail domains bridge the gap between structure and function of myosin VI. Nat. Struct. Mol. Biol. 15, 591–597 (2008). · DOI
  72. Thirumurugan, K., Sakamoto, T., Hammer, J. A. 3rd, Sellers, J. R., Knight, P. J. et al. The cargo-binding domain regulates structure and activity of myosin 5. Nature 442, 212–215 (2006). · DOI
  73. Li, J. et al. Structure of Myo7b/USH1C complex suggests a general PDZ domain binding mode by MyTH4-FERM myosins. Proc. Natl. Acad. Sci. USA 114, E3776–E3785 (2017).
  74. Siemens, J. et al. The Usher syndrome proteins cadherin 23 and harmonin form a complex by means of PDZ-domain interactions. Proc. Natl. Acad. Sci. USA 99, 14946–14951 (2002). · DOI
  75. Adato, A. et al. Interactions in the network of Usher syndrome type 1 proteins. Hum. Mol. Genet. 14, 347–356 (2005). · DOI
  76. Grati, M. et al. MYO3A causes human dominant deafness and interacts with protocadherin 15-CD2 Isoform. Hum. Mutat. 37, 481–487 (2016). · DOI
  77. Inobe, T. & Nukina, N. Rapamycin-induced oligomer formation system of FRB-FKBP fusion proteins. J. Biosci. Bioeng. 122, 40–46 (2016). · DOI
  78. Verpy, E. et al. A defect in harmonin, a PDZ domain-containing protein expressed in the inner ear sensory hair cells, underlies Usher syndrome type 1C. Nat. Genet. 26, 51–55 (2000). · DOI
  79. Yan, J., Pan, L., Chen, X., Wu, L. & Zhang, M. The structure of the harmonin/sans complex reveals an unexpected interaction mode of the two Usher syndrome proteins. Proc. Natl. Acad. Sci. USA 107, 4040–4045 (2010). · DOI
  80. Yan, W., Chen, G. & Li, J. Structure of the Harmonin PDZ2 and coiled-coil domains in a complex with CDHR2 tail and its implications. FASEB J. 36, e22425 (2022). · DOI
  81. Krey, J. F. & Barr-Gillespie, P. G. Molecular composition of vestibular hair bundles. Cold Spring Harb. Perspect. Med. 9. https://doi.org/10.1101/cshperspect.a033209. (2019) · DOI
  82. Rzadzinska, A. K., Nevalainen, E. M., Prosser, H. M., Lappalainen, P. & Steel, K. P. MyosinVIIa interacts with Twinfilin-2 at the tips of mechanosensory stereocilia in the inner ear. PloS ONE 4, e7097 (2009). · DOI
  83. Grati, M. et al. Localization of PDZD7 to the stereocilia ankle-link associates this scaffolding protein with the Usher syndrome protein network. J. Neurosci. 32, 14288–14293 (2012). · DOI
  84. Morgan, C. P. et al. PDZD7-MYO7A complex identified in enriched stereocilia membranes. Elife 5. https://doi.org/10.7554/eLife.18312. (2016) · DOI
  85. Liu, R. et al. A binding protein regulates myosin-7a dimerization and actin bundle assembly. Nat. Commun. 12, 563 (2021). · DOI
  86. Yu, I. M. et al. Myosin 7 and its adaptors link cadherins to actin. Nat. Commun. 8, 15864 (2017). · DOI
  87. Indzhykulian, A. A. et al. Molecular remodeling of tip links underlies mechanosensory regeneration in auditory hair cells. PLoS Biol. 11, e1001583 (2013). · DOI
  88. Elferich, J. et al. Molecular structures and conformations of protocadherin-15 and its complexes on stereocilia elucidated by cryo-electron tomography. Elife 10. https://doi.org/10.7554/eLife.74512. (2021) · DOI
  89. Les Erickson, F., Corsa, A. C., Dose, A. C. & Burnside, B. Localization of a class III myosin to filopodia tips in transfected HeLa cells requires an actin-binding site in its tail domain. Mol. Biol. Cell 14, 4173–4180 (2003). · DOI
  90. Merritt, R. C. et al. Myosin IIIB uses an actin-binding motif in its espin-1 cargo to reach the tips of actin protrusions. Curr. Biol. 22, 320–325 (2012). · DOI
  91. Jiang, F. et al. The ATPase mechanism of myosin 15, the molecular motor mutated in DFNB3 human deafness. J. Biol. Chem. https://doi.org/10.1074/jbc.RA120.014903 (2020). · DOI
  92. Mathur, P. D. & Yang, J. Usher syndrome and non-syndromic deafness: Functions of different whirlin isoforms in the cochlea, vestibular organs, and retina. Hearing Res. 375, 14–24 (2019). · DOI
  93. Lin, L. et al. Phase separation-mediated condensation of Whirlin-Myo15-Eps8 stereocilia tip complex. Cell Rep. 34, 108770 (2021). · DOI
  94. Houdusse, A. & Titus, M. A. The many roles of myosins in filopodia, microvilli and stereocilia. Curr. Biol. 31, R586–R602 (2021). · DOI
  95. Goutman, J. D., Elgoyhen, A. B. & Gomez-Casati, M. E. Cochlear hair cells: the sound-sensing machines. FEBS Lett. 589, 3354–3361 (2015). · DOI
  96. Hickox, A. E. et al. Global analysis of protein expression of inner ear hair cells. J. Neurosci. 37, 1320–1339 (2017). · DOI
  97. Cheng, J. et al. Accurate proteome-wide missense variant effect prediction with AlphaMissense. Science 381, eadg7492 (2023). · DOI · Paper page
  98. Radke, M. B. et al. Small molecule-mediated refolding and activation of myosin motor function. Elife 3, e01603 (2014). · DOI
  99. Martin, R., Mogg, A. E., Heywood, L. A., Nitschke, L. & Burke, J. F. Aminoglycoside suppression at UAG, UAA and UGA codons in Escherichia coli and human tissue culture cells. Mol. Gen. Genet 217, 411–418 (1989). · DOI
  100. Wilschanski, M. et al. Gentamicin-induced correction of CFTR function in patients with cystic fibrosis and CFTR stop mutations. N. Engl. J. Med. 349, 1433–1441 (2003). · DOI
  101. Bidou, L. et al. Premature stop codons involved in muscular dystrophies show a broad spectrum of readthrough efficiencies in response to gentamicin treatment. Gene Ther. 11, 619–627 (2004). · DOI
  102. Castillo, M., Freire, E. & Romero, V. I. Primary ciliary dyskinesia diagnosis and management and its implications in America: a mini review. Front. Pediatr. 11, 1091173 (2023). · DOI
  103. Hildebrandt, F., Benzing, T. & Katsanis, N. Ciliopathies. N. Engl. J. Med. 364, 1533–1543 (2011). · DOI · Paper page
  104. Lamptey, R. N. L. et al. A review of the common neurodegenerative disorders: current therapeutic approaches and the potential role of nanotherapeutics. Int. J. Mol. Sci. 23. https://doi.org/10.3390/ijms23031851. (2022). · DOI
  105. VanDussen, K. L. et al. Abnormal small intestinal epithelial microvilli in patients with Crohn’s disease. Gastroenterology 155, 815–828 (2018). · DOI
  106. Modl, B. et al. Defects in microvillus crosslinking sensitize to colitis and inflammatory bowel disease. EMBO Rep. 24, e57084 (2023). · DOI
  107. Jacquemet, G., Hamidi, H. & Ivaska, J. Filopodia in cell adhesion, 3D migration and cancer cell invasion. Curr. Opin. Cell Biol. 36, 23–31 (2015). · DOI
  108. Karginov, A. V., Ding, F., Kota, P., Dokholyan, N. V. & Hahn, K. M. Engineered allosteric activation of kinases in living cells. Nat. Biotechnol. 28, 743–747 (2010). · DOI
  109. Sun, X., Tie, H. C., Chen, B. & Lu, L. Glycans function as a Golgi export signal to promote the constitutive exocytic trafficking. J. Biol. Chem. 295, 14750–14762 (2020). · DOI
  110. Edelstein, A. D. et al. Advanced methods of microscope control using µManager software. J. Biol. Methods 1, https://doi.org/10.14440/jbm.2014.36 (2014). · DOI
  111. Schneider, C. A., Rasband, W. S. & Eliceiri, K. W. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671–675 (2012). · DOI · Paper page
  112. Ardiel, E. L. et al. Visualizing calcium flux in freely moving nematode embryos. Biophys. J. 112, 1975–1983 (2017). · DOI
  113. Nagashima, S., Aoki, T., Higuchi, T. & Kobayashi, K. A Subpixel Image Matching Technique Using Phase-Only Correlation. 2006 International Symposium on Intelligent Signal Processing and Communications. 701–704, https://doi.org/10.1109/ISPACS.2006.364751 (2007). · DOI
  114. Guo, M. et al. Accelerating iterative deconvolution and multiview fusion by orders of magnitude. https://doi.org/10.1101/647370 (2019). · DOI
  115. Schindelin, J. et al. Fiji: an open-source platform for biological-image analysis. Nat. Methods 9, 676–682 (2012). · DOI · Paper page
  116. Aguet, F., Van De Ville, D. & Unser, M. Model-based 2.5-d deconvolution for extended depth of field in brightfield microscopy. IEEE Trans. Image Process 17, 1144–1153 (2008). · DOI
  117. Born, M., Wolf, E. & Bhatia, A. B. Principles of optics : electromagnetic theory of propagation, interference, and diffraction of light (Cambridge University Press, Cambridge, 2019) https://doi.org/10.1017/9781108769914. · DOI
  118. Gentleman, R., Streibig, J. C., Parmigiani, G., Hornik, K. & Ritz, C. Use R! (Springer New York, 2009).
  119. Johnson, K. R. et al. Mouse models of USH1C and DFNB18: phenotypic and molecular analyses of two new spontaneous mutations of the Ush1c gene. Hum. Mol. Genet. 12, 3075–3086 (2003). · DOI
  120. Nagel-Wolfrum, K. et al. Expression and subcellular localization of USH1C/harmonin in human retina provides insights into pathomechanisms and therapy. Hum. Mol. Genet. 32, 431–449 (2023). · DOI
  121. Wu, L., Pan, L., Wei, Z. & Zhang, M. Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo. Science 331, 757–760 (2011). · DOI

Metadata

Authors
Miyoshi, T., Vishwasrao, H. D., Belyantseva, I. A., Miyoshi, J., Sajeevadathan, M., Ishibashi, Y., Adadey, S. M., Harada, N., Shroff, H., & Friedman, T. B.
Affiliations
  • Southern Illinois University Carbondale (US)
  • National Institutes of Health (US)
  • Howard Hughes Medical Institute (US)
Corresponding author
Miyoshi, Takushi
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2025-09-01
Volume
16
Issue
1
Pages
8149-8149
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-025-63102-0
PMC
PMC12402077
OpenAlex
W4413875073
Cited by
1
References
2
Citations by year
2026: 1
FWCI
0.63
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • Research Square (acceptedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed Central (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • U.S. Department of Health & Human Services | NIH | National Institute on Deafness and Other Communication Disorders (DC000039, 1R00DC019949)
  • U.S. Department of Health & Human Services | NIH | National Institute of Biomedical Imaging and Bioengineering
  • Howard Hughes Medical Institute
  • MEXT | Japan Society for the Promotion of Science
  • School of Medicine, Southern Illinois University
Topics
  • Life Sciences › Neuroscience › Sensory Systems › Hearing, Cochlea, Tinnitus, Genetics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
Keywords
MYO7A, unconventional myosins, stereocilia, inner ear hair cells, mechanoelectrical transduction, freight transport, F-actin, single-molecule fluorescence microscopy

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review