메뉴 건너뛰기




Volumn 11, Issue 4, 2009, Pages 443-450

Myosin IIIa boosts elongation of stereocilia by transporting espin 1 to the plus ends of actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

ESPIN 1; F ACTIN; ISOPROTEIN; MYOSIN III; MYOSIN IIIA; UNCLASSIFIED DRUG;

EID: 64049087801     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1851     Document Type: Article
Times cited : (127)

References (32)
  • 1
    • 0037188476 scopus 로고    scopus 로고
    • From flies' eyes to our ears: Mutations in a human class III myosin cause progressive non-syndromic hearing loss DFNB30
    • Walsh, T. et al. From flies' eyes to our ears: Mutations in a human class III myosin cause progressive non-syndromic hearing loss DFNB30. Proc. Natl Acad. Sci. USA 99, 7518-7523 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7518-7523
    • Walsh, T.1
  • 2
    • 0038015108 scopus 로고    scopus 로고
    • Determination of human myosin III as a motor protein having a protein kinase activity
    • Komaba, S., Inoue, A., Maruta, S., Hosoya, H. & Ikebe, M. Determination of human myosin III as a motor protein having a protein kinase activity. J. Biol. Chem. 278, 21352-21360 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 21352-21360
    • Komaba, S.1    Inoue, A.2    Maruta, S.3    Hosoya, H.4    Ikebe, M.5
  • 3
    • 0034604349 scopus 로고    scopus 로고
    • The deaf jerker mouse has a mutation in the gene encoding the espin actin-bundling proteins of hair cell stereocilia and lacks espins
    • Zheng, L. et al. The deaf jerker mouse has a mutation in the gene encoding the espin actin-bundling proteins of hair cell stereocilia and lacks espins. Cell 102, 377-385 (2000).
    • (2000) Cell , vol.102 , pp. 377-385
    • Zheng, L.1
  • 4
    • 32944469631 scopus 로고    scopus 로고
    • Espin gene (ESPN) mutations associated with autosomal dominant hearing loss cause defects in microvillar elongation or organisation
    • Donaudy, F. et al. Espin gene (ESPN) mutations associated with autosomal dominant hearing loss cause defects in microvillar elongation or organisation. J. Med. Genet. 43, 157-161 (2006).
    • (2006) J. Med. Genet , vol.43 , pp. 157-161
    • Donaudy, F.1
  • 5
    • 2942593267 scopus 로고    scopus 로고
    • Mutations of ESPN cause autosomal recessive deafness and vestibular dysfunction
    • Naz, S. et al. Mutations of ESPN cause autosomal recessive deafness and vestibular dysfunction. J. Med. Genet. 41, 591-595 (2004).
    • (2004) J. Med. Genet , vol.41 , pp. 591-595
    • Naz, S.1
  • 6
    • 33750450039 scopus 로고    scopus 로고
    • Espins and the actin cytoskeleton of hair cell stereocilia and sensory cell microvilli
    • Sekerkova, G., Zheng, L., Loomis, P. A., Mugnaini, E. & Bartles, J. R. Espins and the actin cytoskeleton of hair cell stereocilia and sensory cell microvilli. Cell. Mol. Life Sci. 63, 2329-2341 (2006).
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 2329-2341
    • Sekerkova, G.1    Zheng, L.2    Loomis, P.A.3    Mugnaini, E.4    Bartles, J.R.5
  • 7
    • 33749520665 scopus 로고    scopus 로고
    • A new compartment at stereocilia tips defined by spatial and temporal patterns of myosin IIIa expression
    • Schneider, M. E. et al. A new compartment at stereocilia tips defined by spatial and temporal patterns of myosin IIIa expression. J. Neurosci. 26, 10243-10252 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 10243-10252
    • Schneider, M.E.1
  • 9
    • 1642322799 scopus 로고    scopus 로고
    • An actin molecular treadmill and myosins maintain stereocilia functional architecture and self-renewal
    • Rzadzinska, A. K., Schneider, M. E., Davies, C., Riordan, G. P. & Kachar, B. An actin molecular treadmill and myosins maintain stereocilia functional architecture and self-renewal. J. Cell Biol. 164, 887-897 (2004).
    • (2004) J. Cell Biol , vol.164 , pp. 887-897
    • Rzadzinska, A.K.1    Schneider, M.E.2    Davies, C.3    Riordan, G.P.4    Kachar, B.5
  • 10
    • 12344276516 scopus 로고    scopus 로고
    • When size matters: The dynamic regulation of stereocilia lengths
    • Lin, H. W., Schneider, M. E. & Kachar, B. When size matters: The dynamic regulation of stereocilia lengths. Curr. Opin. Cell Biol. 17, 55-61 (2005).
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 55-61
    • Lin, H.W.1    Schneider, M.E.2    Kachar, B.3
  • 12
    • 54549117918 scopus 로고    scopus 로고
    • Dynamic length regulation of sensory stereocilia
    • Manor, U. & Kachar, B. Dynamic length regulation of sensory stereocilia. Semin. Cell Dev. Biol. 19, 502-510 (2008).
    • (2008) Semin. Cell Dev. Biol , vol.19 , pp. 502-510
    • Manor, U.1    Kachar, B.2
  • 13
    • 13944260197 scopus 로고    scopus 로고
    • Myosin-XVa is required for tip localization of whirlin and differential elongation of hair-cell stereocilia
    • Belyantseva, I. A. et al. Myosin-XVa is required for tip localization of whirlin and differential elongation of hair-cell stereocilia. Nature Cell Biol. 7, 148-156 (2005).
    • (2005) Nature Cell Biol , vol.7 , pp. 148-156
    • Belyantseva, I.A.1
  • 14
    • 40749103397 scopus 로고    scopus 로고
    • Mosaic complementation demonstrates a regulatory role for myosin VIIa in actin dynamics of stereocilia
    • Prosser, H. M., Rzadzinska, A. K., Steel, K. P. & Bradley, A. Mosaic complementation demonstrates a regulatory role for myosin VIIa in actin dynamics of stereocilia. Mol. Cell Biol. 28, 1702-1712 (2008).
    • (2008) Mol. Cell Biol , vol.28 , pp. 1702-1712
    • Prosser, H.M.1    Rzadzinska, A.K.2    Steel, K.P.3    Bradley, A.4
  • 15
    • 35548932103 scopus 로고    scopus 로고
    • The motor activity of myosin-X promotes actin fiber convergence at the cell periphery to initiate filopodia formation
    • Tokuo, H., Mabuchi, K. & Ikebe, M. The motor activity of myosin-X promotes actin fiber convergence at the cell periphery to initiate filopodia formation. J. Cell Biol. 179, 229-238 (2007).
    • (2007) J. Cell Biol , vol.179 , pp. 229-238
    • Tokuo, H.1    Mabuchi, K.2    Ikebe, M.3
  • 16
    • 2442718690 scopus 로고    scopus 로고
    • Myosin X transports Mena/VASP to the tip of filopodia
    • Tokuo, H. & Ikebe, M. Myosin X transports Mena/VASP to the tip of filopodia. Biochem. Biophys. Res. Commun. 319, 214-220 (2004).
    • (2004) Biochem. Biophys. Res. Commun , vol.319 , pp. 214-220
    • Tokuo, H.1    Ikebe, M.2
  • 17
    • 37249014360 scopus 로고    scopus 로고
    • Stepwise morphological and functional maturation of mechanotransduction in rat outer hair cells
    • Waguespack, J., Salles, F. T., Kachar, B. & Ricci, A. J. Stepwise morphological and functional maturation of mechanotransduction in rat outer hair cells. J. Neurosci. 27, 13890-13902 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 13890-13902
    • Waguespack, J.1    Salles, F.T.2    Kachar, B.3    Ricci, A.J.4
  • 18
    • 0141429959 scopus 로고    scopus 로고
    • Localization of a class III myosin to filopodia tips in transfected HeLa cells requires an actin-binding site in its tail domain
    • 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).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4173-4180
    • Les Erickson, F.1    Corsa, A.C.2    Dose, A.C.3    Burnside, B.4
  • 19
    • 33747622327 scopus 로고    scopus 로고
    • Myosin-X is a molecular motor that functions in filopodia formation
    • Bohil, A. B., Robertson, B. W. & Cheney, R. E. Myosin-X is a molecular motor that functions in filopodia formation. Proc. Natl Acad. Sci. USA 103, 12411-12416 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12411-12416
    • Bohil, A.B.1    Robertson, B.W.2    Cheney, R.E.3
  • 20
    • 0037342963 scopus 로고    scopus 로고
    • Myo3A, one of two class III myosin genes expressed in vertebrate retina, is localized to the calycal processes of rod and cone photoreceptors and is expressed in the sacculus
    • Dose, A. C. et al. Myo3A, one of two class III myosin genes expressed in vertebrate retina, is localized to the calycal processes of rod and cone photoreceptors and is expressed in the sacculus. Mol. Biol. Cell 14, 1058-1073 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1058-1073
    • Dose, A.C.1
  • 21
    • 13444292982 scopus 로고    scopus 로고
    • Drosophila Spire is an actin nucleation factor
    • Quinlan, M. E., Heuser, J. E., Kerkhoff, E. & Mullins, R. D. Drosophila Spire is an actin nucleation factor. Nature 433, 382-388 (2005).
    • (2005) Nature , vol.433 , pp. 382-388
    • Quinlan, M.E.1    Heuser, J.E.2    Kerkhoff, E.3    Mullins, R.D.4
  • 22
    • 33646683606 scopus 로고    scopus 로고
    • Targeted wild-type and jerker espins reveal a novel, WH2-domain-dependent way to make actin bundles in cells
    • Loomis, P. A. et al. Targeted wild-type and jerker espins reveal a novel, WH2-domain-dependent way to make actin bundles in cells. J. Cell Sci. 119, 1655-1665 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 1655-1665
    • Loomis, P.A.1
  • 23
    • 58749106804 scopus 로고    scopus 로고
    • Protein localization by actin treadmilling and molecular motors regulates stereocilia shape and treadmilling rate
    • Naoz, M., Manor, U., Sakaguchi, H., Kachar, B. & Gov, N. Protein localization by actin treadmilling and molecular motors regulates stereocilia shape and treadmilling rate. Biophys. J. (2008).
    • (2008) Biophys. J
    • Naoz, M.1    Manor, U.2    Sakaguchi, H.3    Kachar, B.4    Gov, N.5
  • 24
    • 0032825265 scopus 로고    scopus 로고
    • Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction
    • Mallavarapu, A. & Mitchison, T. Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction. J. Cell Biol. 146, 1097-1106 (1999).
    • (1999) J. Cell Biol , vol.146 , pp. 1097-1106
    • Mallavarapu, A.1    Mitchison, T.2
  • 25
    • 46849113840 scopus 로고    scopus 로고
    • Sakaguchi, H. et al. Dynamic compartmentalization of protein tyrosine phosphatase receptor Q. at the proximal end of stereocilia: Implication of myosin VI-based transport. Cell. Motil. Cytoskeleton (2008).
    • Sakaguchi, H. et al. Dynamic compartmentalization of protein tyrosine phosphatase receptor Q. at the proximal end of stereocilia: Implication of myosin VI-based transport. Cell. Motil. Cytoskeleton (2008).
  • 26
    • 39749193988 scopus 로고    scopus 로고
    • The kinase domain alters the kinetic properties of the myosin IIIA motor
    • Dose, A. C. et al. The kinase domain alters the kinetic properties of the myosin IIIA motor. Biochemistry 47, 2485-2496 (2008).
    • (2008) Biochemistry , vol.47 , pp. 2485-2496
    • Dose, A.C.1
  • 27
    • 33845988750 scopus 로고    scopus 로고
    • Human myosin III is a motor having an extremely high affinity for actin
    • Kambara, T., Komaba, S. & Ikebe, M. Human myosin III is a motor having an extremely high affinity for actin. J. Biol. Chem. 281, 37291-37301 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 37291-37301
    • Kambara, T.1    Komaba, S.2    Ikebe, M.3
  • 28
    • 33745061269 scopus 로고    scopus 로고
    • Mechano-electrical transduction: New insights into old ideas
    • Ricci, A. J., Kachar, B., Gale, J. & Van Netten, S. M. Mechano-electrical transduction: New insights into old ideas. J. Membr. Biol. 209, 71-88 (2006).
    • (2006) J. Membr. Biol , vol.209 , pp. 71-88
    • Ricci, A.J.1    Kachar, B.2    Gale, J.3    Van Netten, S.M.4
  • 29
    • 0027768695 scopus 로고
    • Dependence of calmodulin localization in the retina on the NINAC unconventional myosin
    • Porter, J. A., Yu, M., Doberstein, S. K., Pollard, T. D. & Montell, C. Dependence of calmodulin localization in the retina on the NINAC unconventional myosin. Science 262, 1038-1042 (1993).
    • (1993) Science , vol.262 , pp. 1038-1042
    • Porter, J.A.1    Yu, M.2    Doberstein, S.K.3    Pollard, T.D.4    Montell, C.5
  • 30
    • 0033366539 scopus 로고    scopus 로고
    • Termination of phototransduction requires binding of the NINAC myosin III and the PDZ protein INAD
    • Wes, P. D. et al. Termination of phototransduction requires binding of the NINAC myosin III and the PDZ protein INAD. Nature Neurosci. 2, 447-453 (1999).
    • (1999) Nature Neurosci , vol.2 , pp. 447-453
    • Wes, P.D.1
  • 31
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi, L. K., Cammett, T. J., Desrosiers, D. C. & Peng, Z. Y. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci. 13, 1435-1448 (2004).
    • (2004) Protein Sci , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1    Cammett, T.J.2    Desrosiers, D.C.3    Peng, Z.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.