메뉴 건너뛰기




Volumn 1307, Issue , 2010, Pages 53-62

Protein 4.1 expression in the developing hair cells of the mouse inner ear

Author keywords

Inner ear hair cell; MyosinXV whirlin complex; Protein 4.1B; Protein 4.1G; Stereocilia

Indexed keywords

ERYTHROCYTE BAND 4.1 PROTEIN; GENE PRODUCT; MEMBRANE ASSOCIATED GUANYLATE CYCLASE KINASE; MYOSIN; PROTEIN P55;

EID: 70749085164     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2009.10.039     Document Type: Article
Times cited : (11)

References (42)
  • 2
    • 0345133276 scopus 로고    scopus 로고
    • Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and is essential for staircase formation of the hair bundle
    • Belyantseva I.A., Boger E.T., and Friedman T.B. Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and is essential for staircase formation of the hair bundle. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 13958-13963
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13958-13963
    • Belyantseva, I.A.1    Boger, E.T.2    Friedman, T.B.3
  • 5
    • 40849106619 scopus 로고    scopus 로고
    • Quiet as a mouse: dissecting the molecular and genetic basis of hearing
    • Brown S.D., Hardisty-Hughes R.E., and Mburu P. Quiet as a mouse: dissecting the molecular and genetic basis of hearing. Nat. Rev. Genet. 9 (2008) 277-290
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 277-290
    • Brown, S.D.1    Hardisty-Hughes, R.E.2    Mburu, P.3
  • 6
    • 32844458453 scopus 로고    scopus 로고
    • New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium
    • Calinisan V., Gravem D., Chen R.P., Brittin S., Mohandas N., Lecomte M.C., and Gascard P. New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium. Front. Biosci. 11 (2006) 1646-1666
    • (2006) Front. Biosci. , vol.11 , pp. 1646-1666
    • Calinisan, V.1    Gravem, D.2    Chen, R.P.3    Brittin, S.4    Mohandas, N.5    Lecomte, M.C.6    Gascard, P.7
  • 8
    • 0032941447 scopus 로고    scopus 로고
    • The role of alternative pre-mRNA splicing in regulating the structure and function of skeletal protein 4.1
    • Conboy J. The role of alternative pre-mRNA splicing in regulating the structure and function of skeletal protein 4.1. Proc. Soc. Exp. Biol. Med. 220 (1999) 73-78
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.220 , pp. 73-78
    • Conboy, J.1
  • 11
    • 33750727697 scopus 로고    scopus 로고
    • Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1/FERM superfamily
    • Diakowski W., Grzybek M., and Sikorski A.F. Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1/FERM superfamily. Folia Histochem. Cytobiol. 44 (2006) 231-248
    • (2006) Folia Histochem. Cytobiol. , vol.44 , pp. 231-248
    • Diakowski, W.1    Grzybek, M.2    Sikorski, A.F.3
  • 13
    • 13544276523 scopus 로고    scopus 로고
    • Mutant analysis reveals whirlin as a dynamic organizer in the growing hair cell stereocilium
    • Kikkawa Y., Mburu P., Morse S., Kominami R., Townsend S., and Brown S.D. Mutant analysis reveals whirlin as a dynamic organizer in the growing hair cell stereocilium. Hum. Mol. Genet. 14 (2005) 391-400
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 391-400
    • Kikkawa, Y.1    Mburu, P.2    Morse, S.3    Kominami, R.4    Townsend, S.5    Brown, S.D.6
  • 15
    • 4644308500 scopus 로고    scopus 로고
    • Cytoskeletal protein 4.1G is a binding partner of the metabotropic glutamate receptor subtype 1 alpha
    • Lu D., Yan H., Othman T., and Rivkees S.A. Cytoskeletal protein 4.1G is a binding partner of the metabotropic glutamate receptor subtype 1 alpha. J. Neurosci. Res. 78 (2004) 49-55
    • (2004) J. Neurosci. Res. , vol.78 , pp. 49-55
    • Lu, D.1    Yan, H.2    Othman, T.3    Rivkees, S.A.4
  • 19
    • 0034637458 scopus 로고    scopus 로고
    • Regulation of protein 4.1R, p55, and glycophorin C ternary complex in human erythrocyte membrane
    • Nunomura W., Takakuwa Y., Parra M., Conboy J., and Mohandas N. Regulation of protein 4.1R, p55, and glycophorin C ternary complex in human erythrocyte membrane. J. Biol. Chem. 275 (2000) 24540-24546
    • (2000) J. Biol. Chem. , vol.275 , pp. 24540-24546
    • Nunomura, W.1    Takakuwa, Y.2    Parra, M.3    Conboy, J.4    Mohandas, N.5
  • 22
    • 0000104067 scopus 로고    scopus 로고
    • Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family
    • Parra M., Gascard P., Walensky L.D., Snyder S.H., Mohandas N., and Conboy J.G. Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family. Genomics 49 (1998) 298-306
    • (1998) Genomics , vol.49 , pp. 298-306
    • Parra, M.1    Gascard, P.2    Walensky, L.D.3    Snyder, S.H.4    Mohandas, N.5    Conboy, J.G.6
  • 23
    • 34548282131 scopus 로고    scopus 로고
    • Dynamical control of the shape and size of stereocilia and microvilli
    • Prost J., Barbetta C., Joanny J., and Dynamical F. Dynamical control of the shape and size of stereocilia and microvilli. Biophys. J. 4 (2007) 1124-1133
    • (2007) Biophys. J. , vol.4 , pp. 1124-1133
    • Prost, J.1    Barbetta, C.2    Joanny, J.3    Dynamical, F.4
  • 26
    • 44649169675 scopus 로고    scopus 로고
    • Band 4.1 proteins are expressed in the retina and interact with both isoforms of the metabotropic glutamate receptor type 8
    • Rose M., Dütting E., and Enz R. Band 4.1 proteins are expressed in the retina and interact with both isoforms of the metabotropic glutamate receptor type 8. J. Neurochem. 105 (2008) 2375-2387
    • (2008) J. Neurochem. , vol.105 , pp. 2375-2387
    • Rose, M.1    Dütting, E.2    Enz, R.3
  • 27
    • 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., and Kachar B. An actin molecular treadmill and myosins maintain stereocilia functional architecture and self-renewal. J. Cell Biol. 164 (2004) 887-897
    • (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
  • 29
    • 0030897070 scopus 로고    scopus 로고
    • Cell shape-dependent regulation of protein 4.1 alternative pre-mRNA splicing in mammary epithelial cells
    • Schischmanoff P.O., Yaswen P., Parra M.K., Lee G., Chasis J.A., Mohandas N., and Conboy J.G. Cell shape-dependent regulation of protein 4.1 alternative pre-mRNA splicing in mammary epithelial cells. J. Biol. Chem. 272 (1997) 10254-10259
    • (1997) J. Biol. Chem. , vol.272 , pp. 10254-10259
    • Schischmanoff, P.O.1    Yaswen, P.2    Parra, M.K.3    Lee, G.4    Chasis, J.A.5    Mohandas, N.6    Conboy, J.G.7
  • 32
    • 0036860545 scopus 로고    scopus 로고
    • Protein 4.1 tumor suppressors: getting a FERM grip on growth regulation
    • Sun C.X., Robb V.A., and Gutmann D.H. Protein 4.1 tumor suppressors: getting a FERM grip on growth regulation. J. Cell Sci. 115 (2002) 3991-4000
    • (2002) J. Cell Sci. , vol.115 , pp. 3991-4000
    • Sun, C.X.1    Robb, V.A.2    Gutmann, D.H.3
  • 33
  • 34
    • 27744578563 scopus 로고    scopus 로고
    • Immunohistochemical study of a membrane skeletal molecule, protein 4.1G, in mouse seminiferous tubules
    • Terada N., Ohno N., Yamakawa H., Ohara O., Liao X., Baba T., and Ohno S. Immunohistochemical study of a membrane skeletal molecule, protein 4.1G, in mouse seminiferous tubules. Histochem. Cell Biol. 124 (2005) 303-311
    • (2005) Histochem. Cell Biol. , vol.124 , pp. 303-311
    • Terada, N.1    Ohno, N.2    Yamakawa, H.3    Ohara, O.4    Liao, X.5    Baba, T.6    Ohno, S.7
  • 35
    • 36349037047 scopus 로고    scopus 로고
    • Interaction of membrane skeletal protein, protein 4.1B and p55, and sodium bicarbonate cotransporter1 in mouse renal S1-S2 proximal tubules
    • Terada N., Ohno N., Saitoh S., Seki G., Komada M., Suzuki T., Yamakawa H., Soleimani M., and Ohno S. Interaction of membrane skeletal protein, protein 4.1B and p55, and sodium bicarbonate cotransporter1 in mouse renal S1-S2 proximal tubules. J. Histochem. Cytochem. 55 (2007) 1199-1206
    • (2007) J. Histochem. Cytochem. , vol.55 , pp. 1199-1206
    • Terada, N.1    Ohno, N.2    Saitoh, S.3    Seki, G.4    Komada, M.5    Suzuki, T.6    Yamakawa, H.7    Soleimani, M.8    Ohno, S.9
  • 36
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins
    • Tsukita S., and Yonemura S. Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J. Biol. Chem. 274 (1999) 34507-34510
    • (1999) J. Biol. Chem. , vol.274 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 37
    • 34547700102 scopus 로고    scopus 로고
    • The micromachinery of mechanotransduction in hair cells
    • Vollrath M.A., Kwan K.Y., and Corey D.P. The micromachinery of mechanotransduction in hair cells. Annu. Rev. Neurosci. 30 (2007) 339-365
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 339-365
    • Vollrath, M.A.1    Kwan, K.Y.2    Corey, D.P.3
  • 40
    • 0034595322 scopus 로고    scopus 로고
    • Comparison of mRNA and protein levels of four members of the protein 4.1 family: the type II brain 4.1/4.1B/KIAA0987 is the most predominant member of the protein 4.1 family in rat brain
    • Yamakawa H., and Ohara O. Comparison of mRNA and protein levels of four members of the protein 4.1 family: the type II brain 4.1/4.1B/KIAA0987 is the most predominant member of the protein 4.1 family in rat brain. Gene 248 (2000) 137-145
    • (2000) Gene , vol.248 , pp. 137-145
    • Yamakawa, H.1    Ohara, O.2
  • 41
    • 27644457349 scopus 로고    scopus 로고
    • Loss of the putative tumor suppressor band 4.1B/Dal1 gene is dispensable for normal development and does not predispose to cancer
    • Yi C., McCarty J.H., Troutman S.A., Eckman M.S., Bronson R.T., and Kissil J.L. Loss of the putative tumor suppressor band 4.1B/Dal1 gene is dispensable for normal development and does not predispose to cancer. Mol. Cell. Biol. 25 (2005) 10052-10059
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10052-10059
    • Yi, C.1    McCarty, J.H.2    Troutman, S.A.3    Eckman, M.S.4    Bronson, R.T.5    Kissil, J.L.6
  • 42
    • 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., Sekerková G., Vranich K., Tilney L.G., Mugnaini E., and Bartles J.R. 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 (2000) 377-385
    • (2000) Cell , vol.102 , pp. 377-385
    • Zheng, L.1    Sekerková, G.2    Vranich, K.3    Tilney, L.G.4    Mugnaini, E.5    Bartles, J.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.