메뉴 건너뛰기




Volumn 1833, Issue 3, 2013, Pages 698-711

A role for β-dystroglycan in the organization and structure of the nucleus in myoblasts

Author keywords

Dystroglycan; Emerin; Nuclear envelope; Nuclear lamins; Nucleoli

Indexed keywords

BETA DYSTROGLYCAN; CYCLOHEXIMIDE; EMERIN; LAMIN A; LAMIN B1; LAMIN C; MESSENGER RNA; NUCLEAR PROTEIN; P80 COILIN; PROTEIN NOPP140; PROTEIN P80; PROTEIN SC35; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84872029076     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2012.11.019     Document Type: Article
Times cited : (31)

References (64)
  • 1
    • 84855830585 scopus 로고    scopus 로고
    • Nuclear lamina at the crossroads of the cytoplasm and nucleus
    • Gerace L., Huber M.D. Nuclear lamina at the crossroads of the cytoplasm and nucleus. J. Struct. Biol. 2012, 177:24-31.
    • (2012) J. Struct. Biol. , vol.177 , pp. 24-31
    • Gerace, L.1    Huber, M.D.2
  • 2
    • 44449095617 scopus 로고    scopus 로고
    • The nuclear envelope as an integrator of nuclear and cytoplasmic architecture
    • Crisp M., Burke B. The nuclear envelope as an integrator of nuclear and cytoplasmic architecture. FEBS Lett. 2008, 582:2023-2032.
    • (2008) FEBS Lett. , vol.582 , pp. 2023-2032
    • Crisp, M.1    Burke, B.2
  • 4
    • 33644852058 scopus 로고    scopus 로고
    • Actin and myosin as transcription factors
    • Grummt I. Actin and myosin as transcription factors. Curr. Opin. Genet. Dev. 2006, 16:191-196.
    • (2006) Curr. Opin. Genet. Dev. , vol.16 , pp. 191-196
    • Grummt, I.1
  • 5
    • 33748291515 scopus 로고    scopus 로고
    • From the membrane to the nucleus and back again: bifunctional focal adhesion proteins
    • Hervy M., Hoffman L., Beckerle M.C. From the membrane to the nucleus and back again: bifunctional focal adhesion proteins. Curr. Opin. Cell Biol. 2006, 18:524-532.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 524-532
    • Hervy, M.1    Hoffman, L.2    Beckerle, M.C.3
  • 6
    • 79952650662 scopus 로고    scopus 로고
    • Actin-related proteins localized in the nucleus: from discovery to novel roles in nuclear organization
    • Oma Y., Harata M. Actin-related proteins localized in the nucleus: from discovery to novel roles in nuclear organization. Nucleus 2011, 2:38-46.
    • (2011) Nucleus , vol.2 , pp. 38-46
    • Oma, Y.1    Harata, M.2
  • 7
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J.M., Campbell K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 1993, 122:809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 9
    • 0030272647 scopus 로고    scopus 로고
    • Dystroglycan: an extracellular matrix receptor linked to the cytoskeleton
    • Henry M.D., Campbell K.P. Dystroglycan: an extracellular matrix receptor linked to the cytoskeleton. Curr. Opin. Cell Biol. 1996, 8:625-631.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 625-631
    • Henry, M.D.1    Campbell, K.P.2
  • 10
    • 0035252649 scopus 로고    scopus 로고
    • The complexities of dystroglycan
    • Winder S.J. The complexities of dystroglycan. Trends Biochem. Sci. 2001, 26:118-124.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 118-124
    • Winder, S.J.1
  • 11
    • 0034903234 scopus 로고    scopus 로고
    • The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation
    • Ilsley J.L., Sudol M., Winder S.J. The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation. Cell. Signal. 2001, 13:625-632.
    • (2001) Cell. Signal. , vol.13 , pp. 625-632
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 12
    • 0034027602 scopus 로고    scopus 로고
    • Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin
    • James M., Nuttall A., Ilsley J.L., Ottersbach K., Tinsley J.M., Sudol M., Winder S.J. Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin. J. Cell Sci. 2000, 113(Pt 10):1717-1726.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART. 10 , pp. 1717-1726
    • James, M.1    Nuttall, A.2    Ilsley, J.L.3    Ottersbach, K.4    Tinsley, J.M.5    Sudol, M.6    Winder, S.J.7
  • 13
    • 0035807788 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins
    • Sotgia F., Lee H., Bedford M.T., Petrucci T., Sudol M., Lisanti M.P. Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins. Biochemistry 2001, 40:14585-14592.
    • (2001) Biochemistry , vol.40 , pp. 14585-14592
    • Sotgia, F.1    Lee, H.2    Bedford, M.T.3    Petrucci, T.4    Sudol, M.5    Lisanti, M.P.6
  • 14
    • 2942604709 scopus 로고    scopus 로고
    • Dystroglycan, a scaffold for the ERK-MAP kinase cascade
    • Spence H.J., Dhillon A.S., James M., Winder S.J. Dystroglycan, a scaffold for the ERK-MAP kinase cascade. EMBO Rep. 2004, 5:484-489.
    • (2004) EMBO Rep. , vol.5 , pp. 484-489
    • Spence, H.J.1    Dhillon, A.S.2    James, M.3    Winder, S.J.4
  • 15
    • 33847033366 scopus 로고    scopus 로고
    • Recruitment of Dbl by ezrin and dystroglycan drives membrane proximal Cdc42 activation and filopodia formation
    • Batchelor C.L., Higginson J.R., Chen Y.J., Vanni C., Eva A., Winder S.J. Recruitment of Dbl by ezrin and dystroglycan drives membrane proximal Cdc42 activation and filopodia formation. Cell Cycle 2007, 6:353-363.
    • (2007) Cell Cycle , vol.6 , pp. 353-363
    • Batchelor, C.L.1    Higginson, J.R.2    Chen, Y.J.3    Vanni, C.4    Eva, A.5    Winder, S.J.6
  • 17
    • 0035190381 scopus 로고    scopus 로고
    • The dystrophin-glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies
    • Rando T.A. The dystrophin-glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies. Muscle Nerve 2001, 24:1575-1594.
    • (2001) Muscle Nerve , vol.24 , pp. 1575-1594
    • Rando, T.A.1
  • 18
    • 0036842214 scopus 로고    scopus 로고
    • Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells
    • Langenbach K.J., Rando T.A. Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells. Muscle Nerve 2002, 26:644-653.
    • (2002) Muscle Nerve , vol.26 , pp. 644-653
    • Langenbach, K.J.1    Rando, T.A.2
  • 20
    • 77949455857 scopus 로고    scopus 로고
    • Dystroglycan versatility in cell adhesion: a tale of multiple motifs
    • Moore C.J., Winder S.J. Dystroglycan versatility in cell adhesion: a tale of multiple motifs. Cell Commun. Signal 2010, 8:3.
    • (2010) Cell Commun. Signal , vol.8 , pp. 3
    • Moore, C.J.1    Winder, S.J.2
  • 21
    • 33748585194 scopus 로고    scopus 로고
    • Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: members of the nuclear DAPC associate with the nuclear matrix
    • Fuentes-Mera L., Rodriguez-Munoz R., Gonzalez-Ramirez R., Garcia-Sierra F., Gonzalez E., Mornet D., Cisneros B. Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: members of the nuclear DAPC associate with the nuclear matrix. Exp. Cell Res. 2006, 312:3023-3035.
    • (2006) Exp. Cell Res. , vol.312 , pp. 3023-3035
    • Fuentes-Mera, L.1    Rodriguez-Munoz, R.2    Gonzalez-Ramirez, R.3    Garcia-Sierra, F.4    Gonzalez, E.5    Mornet, D.6    Cisneros, B.7
  • 22
    • 54849413581 scopus 로고    scopus 로고
    • Nuclear and nuclear envelope localization of dystrophin Dp71 and dystrophin-associated proteins (DAPs) in the C2C12 muscle cells: DAPs nuclear localization is modulated during myogenesis
    • Gonzalez-Ramirez R., Morales-Lazaro S.L., Tapia-Ramirez V., Mornet D., Cisneros B. Nuclear and nuclear envelope localization of dystrophin Dp71 and dystrophin-associated proteins (DAPs) in the C2C12 muscle cells: DAPs nuclear localization is modulated during myogenesis. J. Cell. Biochem. 2008, 105:735-745.
    • (2008) J. Cell. Biochem. , vol.105 , pp. 735-745
    • Gonzalez-Ramirez, R.1    Morales-Lazaro, S.L.2    Tapia-Ramirez, V.3    Mornet, D.4    Cisneros, B.5
  • 24
    • 56149099408 scopus 로고    scopus 로고
    • Nuclear translocation of beta-dystroglycan reveals a distinctive trafficking pattern of autoproteolyzed mucins
    • Oppizzi M.L., Akhavan A., Singh M., Fata J.E., Muschler J.L. Nuclear translocation of beta-dystroglycan reveals a distinctive trafficking pattern of autoproteolyzed mucins. Traffic 2008, 9:2063-2072.
    • (2008) Traffic , vol.9 , pp. 2063-2072
    • Oppizzi, M.L.1    Akhavan, A.2    Singh, M.3    Fata, J.E.4    Muschler, J.L.5
  • 28
    • 42249084242 scopus 로고    scopus 로고
    • Beta-Dystroglycan modulates the interplay between actin and microtubules in human-adhered platelets
    • Cerecedo D., Cisneros B., Suarez-Sanchez R., Hernandez-Gonzalez E., Galvan I. beta-Dystroglycan modulates the interplay between actin and microtubules in human-adhered platelets. Br. J. Haematol. 2008, 141:517-528.
    • (2008) Br. J. Haematol. , vol.141 , pp. 517-528
    • Cerecedo, D.1    Cisneros, B.2    Suarez-Sanchez, R.3    Hernandez-Gonzalez, E.4    Galvan, I.5
  • 29
    • 4143115812 scopus 로고    scopus 로고
    • Beta-Dystroglycan can be revealed in microsomes from mdx mouse muscle by detergent treatment
    • Cluchague N., Moreau C., Rocher C., Pottier S., Leray G., Cherel Y., Le Rumeur E. beta-Dystroglycan can be revealed in microsomes from mdx mouse muscle by detergent treatment. FEBS Lett. 2004, 572:216-220.
    • (2004) FEBS Lett. , vol.572 , pp. 216-220
    • Cluchague, N.1    Moreau, C.2    Rocher, C.3    Pottier, S.4    Leray, G.5    Cherel, Y.6    Le Rumeur, E.7
  • 30
    • 35348891997 scopus 로고    scopus 로고
    • Altered expression of natively glycosylated alpha dystroglycan in pediatric solid tumors
    • Martin L.T., Glass M., Dosunmu E., Martin P.T. Altered expression of natively glycosylated alpha dystroglycan in pediatric solid tumors. Hum. Pathol. 2007, 38:1657-1668.
    • (2007) Hum. Pathol. , vol.38 , pp. 1657-1668
    • Martin, L.T.1    Glass, M.2    Dosunmu, E.3    Martin, P.T.4
  • 31
    • 73949088241 scopus 로고    scopus 로고
    • Mice lacking dystrophin or alpha sarcoglycan spontaneously develop embryonal rhabdomyosarcoma with cancer-associated p53 mutations and alternatively spliced or mutant Mdm2 transcripts
    • Fernandez K., Serinagaoglu Y., Hammond S., Martin L.T., Martin P.T. Mice lacking dystrophin or alpha sarcoglycan spontaneously develop embryonal rhabdomyosarcoma with cancer-associated p53 mutations and alternatively spliced or mutant Mdm2 transcripts. Am. J. Pathol. 2010, 176:416-434.
    • (2010) Am. J. Pathol. , vol.176 , pp. 416-434
    • Fernandez, K.1    Serinagaoglu, Y.2    Hammond, S.3    Martin, L.T.4    Martin, P.T.5
  • 33
    • 0037225049 scopus 로고    scopus 로고
    • Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy
    • Favreau C., Dubosclard E., Ostlund C., Vigouroux C., Capeau J., Wehnert M., Higuet D., Worman H.J., Courvalin J.C., Buendia B. Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy. Exp. Cell Res. 2003, 282:14-23.
    • (2003) Exp. Cell Res. , vol.282 , pp. 14-23
    • Favreau, C.1    Dubosclard, E.2    Ostlund, C.3    Vigouroux, C.4    Capeau, J.5    Wehnert, M.6    Higuet, D.7    Worman, H.J.8    Courvalin, J.C.9    Buendia, B.10
  • 37
    • 34548818532 scopus 로고    scopus 로고
    • A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane
    • Salpingidou G., Smertenko A., Hausmanowa-Petrucewicz I., Hussey P.J., Hutchison C.J. A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane. J. Cell Biol. 2007, 178:897-904.
    • (2007) J. Cell Biol. , vol.178 , pp. 897-904
    • Salpingidou, G.1    Smertenko, A.2    Hausmanowa-Petrucewicz, I.3    Hussey, P.J.4    Hutchison, C.J.5
  • 39
    • 33645116709 scopus 로고    scopus 로고
    • The truncated prelamin A in Hutchinson-Gilford progeria syndrome alters segregation of A-type and B-type lamin homopolymers
    • Delbarre E., Tramier M., Coppey-Moisan M., Gaillard C., Courvalin J.C., Buendia B. The truncated prelamin A in Hutchinson-Gilford progeria syndrome alters segregation of A-type and B-type lamin homopolymers. Hum. Mol. Genet. 2006, 15:1113-1122.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1113-1122
    • Delbarre, E.1    Tramier, M.2    Coppey-Moisan, M.3    Gaillard, C.4    Courvalin, J.C.5    Buendia, B.6
  • 40
    • 38949154474 scopus 로고    scopus 로고
    • Filaments made from A- and B-type lamins differ in structure and organization
    • Goldberg M.W., Huttenlauch I., Hutchison C.J., Stick R. Filaments made from A- and B-type lamins differ in structure and organization. J. Cell Sci. 2008, 121:215-225.
    • (2008) J. Cell Sci. , vol.121 , pp. 215-225
    • Goldberg, M.W.1    Huttenlauch, I.2    Hutchison, C.J.3    Stick, R.4
  • 41
    • 0032771080 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane
    • Fairley E.A., Kendrick-Jones J., Ellis J.A. The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane. J. Cell Sci. 1999, 112(Pt 15):2571-2582.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART. 15 , pp. 2571-2582
    • Fairley, E.A.1    Kendrick-Jones, J.2    Ellis, J.A.3
  • 43
    • 40149104495 scopus 로고    scopus 로고
    • Targeting of dystroglycan to the cleavage furrow and midbody in cytokinesis
    • Higginson J.R., Thompson O., Winder S.J. Targeting of dystroglycan to the cleavage furrow and midbody in cytokinesis. Int. J. Biochem. Cell Biol. 2008, 40:892-900.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 892-900
    • Higginson, J.R.1    Thompson, O.2    Winder, S.J.3
  • 45
    • 80053553994 scopus 로고    scopus 로고
    • The centrosome cycle: centriole biogenesis, duplication and inherent asymmetries
    • Nigg E.A., Stearns T. The centrosome cycle: centriole biogenesis, duplication and inherent asymmetries. Nat. Cell Biol. 2011, 13:1154-1160.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1154-1160
    • Nigg, E.A.1    Stearns, T.2
  • 48
    • 38949130017 scopus 로고    scopus 로고
    • Biology of the striated muscle dystrophin-glycoprotein complex
    • Ervasti J.M., Sonnemann K.J. Biology of the striated muscle dystrophin-glycoprotein complex. Int. Rev. Cytol. 2008, 265:191-225.
    • (2008) Int. Rev. Cytol. , vol.265 , pp. 191-225
    • Ervasti, J.M.1    Sonnemann, K.J.2
  • 49
    • 0023745057 scopus 로고
    • Intragenic deletions in 21 Duchenne muscular dystrophy (DMD)/Becker muscular dystrophy (BMD) families studied with the dystrophin cDNA: location of breakpoints on HindIII and BglII exon-containing fragment maps, meiotic and mitotic origin of the mutations
    • Darras B.T., Blattner P., Harper J.F., Spiro A.J., Alter S., Francke U. Intragenic deletions in 21 Duchenne muscular dystrophy (DMD)/Becker muscular dystrophy (BMD) families studied with the dystrophin cDNA: location of breakpoints on HindIII and BglII exon-containing fragment maps, meiotic and mitotic origin of the mutations. Am. J. Hum. Genet. 1988, 43:620-629.
    • (1988) Am. J. Hum. Genet. , vol.43 , pp. 620-629
    • Darras, B.T.1    Blattner, P.2    Harper, J.F.3    Spiro, A.J.4    Alter, S.5    Francke, U.6
  • 50
    • 34447638686 scopus 로고    scopus 로고
    • Ins and outs of therapy in limb girdle muscular dystrophies
    • Daniele N., Richard I., Bartoli M. Ins and outs of therapy in limb girdle muscular dystrophies. Int. J. Biochem. Cell Biol. 2007, 39:1608-1624.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1608-1624
    • Daniele, N.1    Richard, I.2    Bartoli, M.3
  • 52
    • 80052040544 scopus 로고    scopus 로고
    • Exclusion of WWP1 mutations in a cohort of dystroglycanopathy patients
    • Godfrey C., Clement E., Abbs S., Muntoni F. Exclusion of WWP1 mutations in a cohort of dystroglycanopathy patients. Muscle Nerve 2011, 44:388-392.
    • (2011) Muscle Nerve , vol.44 , pp. 388-392
    • Godfrey, C.1    Clement, E.2    Abbs, S.3    Muntoni, F.4
  • 53
    • 7944232477 scopus 로고    scopus 로고
    • Decreased mechanical stiffness in LMNA-/- cells is caused by defective nucleo-cytoskeletal integrity: implications for the development of laminopathies
    • Broers J.L., Peeters E.A., Kuijpers H.J., Endert J., Bouten C.V., Oomens C.W., Baaijens F.P., Ramaekers F.C. Decreased mechanical stiffness in LMNA-/- cells is caused by defective nucleo-cytoskeletal integrity: implications for the development of laminopathies. Hum. Mol. Genet. 2004, 13:2567-2580.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2567-2580
    • Broers, J.L.1    Peeters, E.A.2    Kuijpers, H.J.3    Endert, J.4    Bouten, C.V.5    Oomens, C.W.6    Baaijens, F.P.7    Ramaekers, F.C.8
  • 54
    • 0035153087 scopus 로고    scopus 로고
    • Lamins in disease: why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes?
    • Hutchison C.J., Alvarez-Reyes M., Vaughan O.A. Lamins in disease: why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes?. J. Cell Sci. 2001, 114:9-19.
    • (2001) J. Cell Sci. , vol.114 , pp. 9-19
    • Hutchison, C.J.1    Alvarez-Reyes, M.2    Vaughan, O.A.3
  • 56
    • 68849119046 scopus 로고    scopus 로고
    • Laminopathies and the long strange trip from basic cell biology to therapy
    • Worman H.J., Fong L.G., Muchir A., Young S.G. Laminopathies and the long strange trip from basic cell biology to therapy. J. Clin. Invest. 2009, 119:1825-1836.
    • (2009) J. Clin. Invest. , vol.119 , pp. 1825-1836
    • Worman, H.J.1    Fong, L.G.2    Muchir, A.3    Young, S.G.4
  • 57
    • 0034176682 scopus 로고    scopus 로고
    • The nuclear envelope, muscular dystrophy and gene expression
    • Wilson K.L. The nuclear envelope, muscular dystrophy and gene expression. Trends Cell Biol. 2000, 10:125-129.
    • (2000) Trends Cell Biol. , vol.10 , pp. 125-129
    • Wilson, K.L.1
  • 62
    • 43149091675 scopus 로고    scopus 로고
    • The integrity of a lamin-B1-dependent nucleoskeleton is a fundamental determinant of RNA synthesis in human cells
    • Tang C.W., Maya-Mendoza A., Martin C., Zeng K., Chen S., Feret D., Wilson S.A., Jackson D.A. The integrity of a lamin-B1-dependent nucleoskeleton is a fundamental determinant of RNA synthesis in human cells. J. Cell Sci. 2008, 121:1014-1024.
    • (2008) J. Cell Sci. , vol.121 , pp. 1014-1024
    • Tang, C.W.1    Maya-Mendoza, A.2    Martin, C.3    Zeng, K.4    Chen, S.5    Feret, D.6    Wilson, S.A.7    Jackson, D.A.8
  • 64
    • 84872921028 scopus 로고    scopus 로고
    • Dystroglycan function is a novel determinant of tumor growth and behavior in prostate cancer
    • (Epub ahead of print)
    • Mitchell A., Mathew G., Jiang T., Hamdy F.C., Cross S.S., Eaton C., Winder S.J. Dystroglycan function is a novel determinant of tumor growth and behavior in prostate cancer. Prostate 2012, (Epub ahead of print). 10.1002/pros.22581.
    • (2012) Prostate
    • Mitchell, A.1    Mathew, G.2    Jiang, T.3    Hamdy, F.C.4    Cross, S.S.5    Eaton, C.6    Winder, S.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.