메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

SRSF1 and hnRNP H antagonistically regulate splicing of COLQ exon 16 in a congenital myasthenic syndrome

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINESTERASE; COLLAGEN; COLQ PROTEIN, HUMAN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN GROUP F H; HNRNPH2 PROTEIN, HUMAN; MUSCLE PROTEIN; PROTEIN BINDING; RNA SPLICING; SERINE ARGININE RICH SPLICING FACTOR; SRSF1 PROTEIN, HUMAN;

EID: 84939455168     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep13208     Document Type: Article
Times cited : (31)

References (51)
  • 1
    • 0037530441 scopus 로고    scopus 로고
    • Sleuthing molecular targets for neurological diseases at the neuromuscular junction
    • Engel, A. G., Ohno, K. & Sine, S. M. Sleuthing molecular targets for neurological diseases at the neuromuscular junction. Nat Rev Neurosci 4, 339-352 (2003).
    • (2003) Nat Rev Neurosci , vol.4 , pp. 339-352
    • Engel, A.G.1    Ohno, K.2    Sine, S.M.3
  • 2
    • 84856343171 scopus 로고    scopus 로고
    • Current status of the congenital myasthenic syndromes
    • Engel, A. G. Current status of the congenital myasthenic syndromes. Neuromuscul Disord 22, 99-111 (2012).
    • (2012) Neuromuscul Disord , vol.22 , pp. 99-111
    • Engel, A.G.1
  • 3
    • 0015890033 scopus 로고
    • Multiple forms of acetylcholinesterase and their distribution in endplate and non-endplate regions of rat diaphragm muscle
    • Hall, Z. W. Multiple forms of acetylcholinesterase and their distribution in endplate and non-endplate regions of rat diaphragm muscle. J Neurobiol 4, 343-361 (1973).
    • (1973) J Neurobiol , vol.4 , pp. 343-361
    • Hall, Z.W.1
  • 4
    • 0032483003 scopus 로고    scopus 로고
    • Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme
    • Ohno, K., Brengman, J., Tsujino, A. & Engel, A. G. Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme. Proc Natl Acad Sci USA 95, 9654-9659 (1998).
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9654-9659
    • Ohno, K.1    Brengman, J.2    Tsujino, A.3    Engel, A.G.4
  • 5
    • 84987755154 scopus 로고    scopus 로고
    • Molecular genetics of congenital myasthenic syndromes
    • John Wiley & Sons, Inc
    • Ohno, K., Ohkawara, B., Ito, M. & Engel, A. G. Molecular Genetics of Congenital Myasthenic Syndromes. in eLS doi: 10.1002/9780470015902.a9780470024314 (John Wiley & Sons, Inc., 2014).
    • (2014) ELS
    • Ohno, K.1    Ohkawara, B.2    Ito, M.3    Engel, A.G.4
  • 6
    • 17344391484 scopus 로고    scopus 로고
    • The spectrum of mutations causing endplate acetylcholinesterase deficiency
    • Ohno, K. et al. The spectrum of mutations causing endplate acetylcholinesterase deficiency. Ann Neurol 47, 162-170 (2000).
    • (2000) Ann Neurol , vol.47 , pp. 162-170
    • Ohno, K.1
  • 7
    • 0033577899 scopus 로고    scopus 로고
    • Acetylcholinesterase clustering at the neuromuscular junction involves perlecan and dystroglycan
    • Peng, H. B., Xie, H., Rossi, S. G. & Rotundo, R. L. Acetylcholinesterase clustering at the neuromuscular junction involves perlecan and dystroglycan. J Cell Biol 145, 911-921 (1999).
    • (1999) J Cell Biol , vol.145 , pp. 911-921
    • Peng, H.B.1    Xie, H.2    Rossi, S.G.3    Rotundo, R.L.4
  • 8
    • 2542487390 scopus 로고    scopus 로고
    • MuSK is required for anchoring acetylcholinesterase at the neuromuscular junction
    • Cartaud, A. et al. MuSK is required for anchoring acetylcholinesterase at the neuromuscular junction. J Cell Biol 165, 505-515 (2004).
    • (2004) J Cell Biol , vol.165 , pp. 505-515
    • Cartaud, A.1
  • 9
    • 84863441080 scopus 로고    scopus 로고
    • Protein-anchoring strategy for delivering acetylcholinesterase to the neuromuscular junction
    • Ito, M. et al. Protein-anchoring strategy for delivering acetylcholinesterase to the neuromuscular junction. Mol Ther 20, 1384-1392 (2012).
    • (2012) Mol Ther , vol.20 , pp. 1384-1392
    • Ito, M.1
  • 10
    • 33947497536 scopus 로고    scopus 로고
    • The therapy of congenital myasthenic syndromes
    • Engel, A. G. The therapy of congenital myasthenic syndromes. Neurotherapeutics 4, 252-257 (2007).
    • (2007) Neurotherapeutics , vol.4 , pp. 252-257
    • Engel, A.G.1
  • 11
    • 80054848752 scopus 로고    scopus 로고
    • Beneficial effects of albuterol in congenital endplate acetylcholinesterase deficiency and dok-7 myasthenia
    • Liewluck, T., Selcen, D. & Engel, A. G. Beneficial Effects of Albuterol in Congenital Endplate Acetylcholinesterase Deficiency and Dok-7 Myasthenia. Muscle Nerve 44, 789-794 (2011).
    • (2011) Muscle Nerve , vol.44 , pp. 789-794
    • Liewluck, T.1    Selcen, D.2    Engel, A.G.3
  • 12
    • 84876839218 scopus 로고    scopus 로고
    • Genome-wide analysis reveals SR protein cooperation and competition in regulated splicing
    • Pandit, S. et al. Genome-wide analysis reveals SR protein cooperation and competition in regulated splicing. Mol Cell 50, 223-235 (2013).
    • (2013) Mol Cell , vol.50 , pp. 223-235
    • Pandit, S.1
  • 13
    • 8844219677 scopus 로고    scopus 로고
    • Involvement of SR proteins in mRNA surveillance
    • Zhang, Z. & Krainer, A. R. Involvement of SR proteins in mRNA surveillance. Mol Cell 16, 597-607 (2004).
    • (2004) Mol Cell , vol.16 , pp. 597-607
    • Zhang, Z.1    Krainer, A.R.2
  • 14
    • 0037470052 scopus 로고    scopus 로고
    • Characterization and in vivo functional analysis of splice variants of cypher
    • Huang, C. et al. Characterization and in vivo functional analysis of splice variants of cypher. J Biol Chem 278, 7360-7365 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 7360-7365
    • Huang, C.1
  • 15
    • 77949270281 scopus 로고    scopus 로고
    • SF2/ASF autoregulation involves multiple layers of post-transcriptional and translational control
    • Sun, S., Zhang, Z., Sinha, R., Karni, R. & Krainer, A. R. SF2/ASF autoregulation involves multiple layers of post-transcriptional and translational control. Nat Struct Mol Biol 17, 306-312 (2010).
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 306-312
    • Sun, S.1    Zhang, Z.2    Sinha, R.3    Karni, R.4    Krainer, A.R.5
  • 16
    • 33847630730 scopus 로고    scopus 로고
    • The gene encoding the splicing factor SF2/ASF is a proto-oncogene
    • Karni, R. et al. The gene encoding the splicing factor SF2/ASF is a proto-oncogene. Nat Struct Mol Biol 14, 185-193 (2007).
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 185-193
    • Karni, R.1
  • 17
    • 21844480060 scopus 로고    scopus 로고
    • A combinatorial code for splicing silencing: UAGG and GGGG motifs
    • Han, K., Yeo, G., An, P., Burge, C. B. & Grabowski, P. J. A combinatorial code for splicing silencing: UAGG and GGGG motifs. PLoS Biol 3, 843-860 (2005).
    • (2005) PLoS Biol , vol.3 , pp. 843-860
    • Han, K.1    Yeo, G.2    An, P.3    Burge, C.B.4    Grabowski, P.J.5
  • 18
    • 0032953308 scopus 로고    scopus 로고
    • HnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells
    • Chou, M. Y., Rooke, N., Turck, C. W. & Black, D. L. hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells. Mol Cell Biol 19, 69-77 (1999).
    • (1999) Mol Cell Biol , vol.19 , pp. 69-77
    • Chou, M.Y.1    Rooke, N.2    Turck, C.W.3    Black, D.L.4
  • 19
    • 0037083819 scopus 로고    scopus 로고
    • SR proteins and hnRNP H regulate the splicing of the HIV-1 tev-specific exon 6D
    • Caputi, M. & Zahler, A. M. SR proteins and hnRNP H regulate the splicing of the HIV-1 tev-specific exon 6D. EMBO J 21, 845-855 (2002).
    • (2002) EMBO J , vol.21 , pp. 845-855
    • Caputi, M.1    Zahler, A.M.2
  • 20
    • 34547634562 scopus 로고    scopus 로고
    • PLP/DM20 ratio is regulated by hnRNPH and F and a novel G-rich enhancer in oligodendrocytes
    • Wang, E. M., Dimova, N. & Cambi, F. PLP/DM20 ratio is regulated by hnRNPH and F and a novel G-rich enhancer in oligodendrocytes. Nucleic Acids Res 35, 4164-4178 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. 4164-4178
    • Wang, E.M.1    Dimova, N.2    Cambi, F.3
  • 21
    • 1642442637 scopus 로고    scopus 로고
    • C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse
    • Kimbell, L. M., Ohno, K., Engel, A. G. & Rotundo, R. L. C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse. J Biol Chem 279, 10997-11005 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 10997-11005
    • Kimbell, L.M.1    Ohno, K.2    Engel, A.G.3    Rotundo, R.L.4
  • 22
    • 70349465009 scopus 로고    scopus 로고
    • DISC1 splice variants are upregulated in schizophrenia and associated with risk polymorphisms
    • Nakata, K. et al. DISC1 splice variants are upregulated in schizophrenia and associated with risk polymorphisms. Proc Natl Acad Sci USA 106, 15873-15878 (2009).
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15873-15878
    • Nakata, K.1
  • 23
    • 0029142841 scopus 로고
    • Hnrnp-L binds a cis-acting RNA sequence element that enables intron-independent gene-expression
    • Liu, X. D. & Mertz, J. E. Hnrnp-L Binds a Cis-Acting Rna Sequence Element That Enables Intron-Independent Gene-Expression. Genes Dev 9, 1766-1780 (1995).
    • (1995) Genes Dev , vol.9 , pp. 1766-1780
    • Liu, X.D.1    Mertz, J.E.2
  • 24
    • 61849139645 scopus 로고    scopus 로고
    • Splicing factor SFRS1 recognizes a functionally diverse landscape of RNA transcripts
    • Sanford, J. R. et al. Splicing factor SFRS1 recognizes a functionally diverse landscape of RNA transcripts. Genome Res 19, 381-394 (2009).
    • (2009) Genome Res , vol.19 , pp. 381-394
    • Sanford, J.R.1
  • 25
    • 0037083819 scopus 로고    scopus 로고
    • SR proteins and hnRNP H regulate the splicing of the HIV-1 tev-specific exon 6D
    • Caputi, M. & Zahler, A. M. SR proteins and hnRNP H regulate the splicing of the HIV-1 tev-specific exon 6D. EMBO J 21, 845-855 (2002).
    • (2002) EMBO J , vol.21 , pp. 845-855
    • Caputi, M.1    Zahler, A.M.2
  • 26
    • 57149106806 scopus 로고    scopus 로고
    • HnRNP H enhances skipping of a nonfunctional exon P3A in CHRNA1 and a mutation disrupting its binding causes congenital myasthenic syndrome
    • Masuda, A. et al. hnRNP H enhances skipping of a nonfunctional exon P3A in CHRNA1 and a mutation disrupting its binding causes congenital myasthenic syndrome. Hum Mol Genet 17, 4022-4035 (2008).
    • (2008) Hum Mol Genet , vol.17 , pp. 4022-4035
    • Masuda, A.1
  • 27
    • 84861161751 scopus 로고    scopus 로고
    • Integrative genome-wide analysis reveals cooperative regulation of alternative splicing by hnRNP proteins
    • Huelga, S. C. et al. Integrative genome-wide analysis reveals cooperative regulation of alternative splicing by hnRNP proteins. Cell Rep 1, 167-178 (2012).
    • (2012) Cell Rep , vol.1 , pp. 167-178
    • Huelga, S.C.1
  • 28
    • 0032128255 scopus 로고    scopus 로고
    • Identification of functional exonic splicing enhancer motifs recognized by individual SR proteins
    • Liu, H. X., Zhang, M. & Krainer, A. R. Identification of functional exonic splicing enhancer motifs recognized by individual SR proteins. Genes Dev 12, 1998-2012 (1998).
    • (1998) Genes Dev , vol.12 , pp. 1998-2012
    • Liu, H.X.1    Zhang, M.2    Krainer, A.R.3
  • 29
  • 30
    • 0242522413 scopus 로고    scopus 로고
    • Missense mutations in hMLH1 and hMSH2 are associated with exonic splicing enhancers
    • Gorlov, I. P., Gorlova, O. Y., Frazier, M. L. & Amos, C. I. Missense mutations in hMLH1 and hMSH2 are associated with exonic splicing enhancers. Am J Hum Genet 73, 1157-1161 (2003).
    • (2003) Am J Hum Genet , vol.73 , pp. 1157-1161
    • Gorlov, I.P.1    Gorlova, O.Y.2    Frazier, M.L.3    Amos, C.I.4
  • 31
    • 84923349666 scopus 로고    scopus 로고
    • HnRNP C, YB-1 and hnRNP L coordinately enhance skipping of human MUSK exon 10 to generate a Wntinsensitive MuSK isoform
    • Nasrin, F. et al. HnRNP C, YB-1 and hnRNP L coordinately enhance skipping of human MUSK exon 10 to generate a Wntinsensitive MuSK isoform. Sci Rep 4, 6841 (2014).
    • (2014) Sci Rep , vol.4 , pp. 6841
    • Nasrin, F.1
  • 32
    • 80052607346 scopus 로고    scopus 로고
    • CDK4 and cyclin D1 allow human myogenic cells to recapture growth property without compromising differentiation potential
    • Shiomi, K. et al. CDK4 and cyclin D1 allow human myogenic cells to recapture growth property without compromising differentiation potential. Gene Ther 18, 857-866 (2011).
    • (2011) Gene Ther , vol.18 , pp. 857-866
    • Shiomi, K.1
  • 34
    • 33747881833 scopus 로고    scopus 로고
    • Immortalization of human myogenic progenitor cell clone retaining multipotentiality
    • Hashimoto, N. et al. Immortalization of human myogenic progenitor cell clone retaining multipotentiality. Biochem Biophys Res Commun 348, 1383-1388 (2006).
    • (2006) Biochem Biophys Res Commun , vol.348 , pp. 1383-1388
    • Hashimoto, N.1
  • 35
    • 84886871632 scopus 로고    scopus 로고
    • HnRNP L and hnRNP LL antagonistically modulate PTB-mediated splicing suppression of CHRNA1 premRNA
    • Rahman, M. A. et al. HnRNP L and hnRNP LL antagonistically modulate PTB-mediated splicing suppression of CHRNA1 premRNA. Sci Rep 3, 2931 (2013).
    • (2013) Sci Rep , vol.3 , pp. 2931
    • Rahman, M.A.1
  • 36
  • 37
    • 0036544654 scopus 로고    scopus 로고
    • Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1
    • Cartegni, L. & Krainer, A. R. Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1. Nat Genet 30, 377-384 (2002).
    • (2002) Nat Genet , vol.30 , pp. 377-384
    • Cartegni, L.1    Krainer, A.R.2
  • 38
    • 0041665176 scopus 로고    scopus 로고
    • A negative element in SMN2 exon 7 inhibits splicing in spinal muscular atrophy
    • Kashima, T. & Manley, J. L. A negative element in SMN2 exon 7 inhibits splicing in spinal muscular atrophy. Nat Genet 34, 460-463 (2003).
    • (2003) Nat Genet , vol.34 , pp. 460-463
    • Kashima, T.1    Manley, J.L.2
  • 39
    • 36248987806 scopus 로고    scopus 로고
    • HnRNP A1 functions with specificity in repression of SMN2 exon 7 splicing
    • Kashima, T., Rao, N., David, C. J. & Manley, J. L. hnRNP A1 functions with specificity in repression of SMN2 exon 7 splicing. Hum Mol Genet 16, 3149-3159 (2007).
    • (2007) Hum Mol Genet , vol.16 , pp. 3149-3159
    • Kashima, T.1    Rao, N.2    David, C.J.3    Manley, J.L.4
  • 40
    • 0028289188 scopus 로고
    • Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors
    • Kohtz, J. D. et al. Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors. Nature 368, 119-124 (1994).
    • (1994) Nature , vol.368 , pp. 119-124
    • Kohtz, J.D.1
  • 41
    • 0031042396 scopus 로고    scopus 로고
    • Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing
    • Xiao, S. H. & Manley, J. L. Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev 11, 334-344 (1997).
    • (1997) Genes Dev , vol.11 , pp. 334-344
    • Xiao, S.H.1    Manley, J.L.2
  • 42
    • 0032493734 scopus 로고    scopus 로고
    • A serine/arginine-rich domain in the human U1 70k protein is necessary and sufficient for ASF/SF2 binding
    • Cao, W. H. & Garcia-Blanco, M. A. A serine/arginine-rich domain in the human U1 70k protein is necessary and sufficient for ASF/SF2 binding. J Biol Chem 273, 20629-20635 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 20629-20635
    • Cao, W.H.1    Garcia-Blanco, M.A.2
  • 43
    • 79957784833 scopus 로고    scopus 로고
    • Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1-70K snRNP protein determines early spliceosome assembly
    • Cho, S. Y. et al. Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1-70K snRNP protein determines early spliceosome assembly. Proc Natl Acad Sci USA 108, 8233-8238 (2011).
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 8233-8238
    • Cho, S.Y.1
  • 44
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., Krummel, B. & Saiki, R. K. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res 16, 7351-7367 (1988).
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 45
    • 0031829201 scopus 로고    scopus 로고
    • Myasthenic syndromes in Turkish kinships due to mutations in the acetylcholine receptor
    • Ohno, K. et al. Myasthenic syndromes in Turkish kinships due to mutations in the acetylcholine receptor. Ann Neurol 44, 234-241 (1998).
    • (1998) Ann Neurol , vol.44 , pp. 234-241
    • Ohno, K.1
  • 46
    • 0033636518 scopus 로고    scopus 로고
    • Functional association of U2 snRNP with the ATP-independent spliceosomal complex e
    • Das, R., Zhou, Z. & Reed, R. Functional association of U2 snRNP with the ATP-independent spliceosomal complex E. Mol Cell 5, 779-787 (2000).
    • (2000) Mol Cell , vol.5 , pp. 779-787
    • Das, R.1    Zhou, Z.2    Reed, R.3
  • 47
    • 84871436996 scopus 로고    scopus 로고
    • Evolutionary dynamics of gene and isoform regulation in Mammalian tissues
    • Merkin, J., Russell, C., Chen, P. & Burge, C. B. Evolutionary dynamics of gene and isoform regulation in Mammalian tissues. Science 338, 1593-1599 (2012).
    • (2012) Science , vol.338 , pp. 1593-1599
    • Merkin, J.1    Russell, C.2    Chen, P.3    Burge, C.B.4
  • 48
    • 65449136284 scopus 로고    scopus 로고
    • TopHat: Discovering splice junctions with RNA-Seq
    • Trapnell, C., Pachter, L. & Salzberg, S. L. TopHat: discovering splice junctions with RNA-Seq. Bioinformatics 25, 1105-1111 (2009).
    • (2009) Bioinformatics , vol.25 , pp. 1105-1111
    • Trapnell, C.1    Pachter, L.2    Salzberg, S.L.3
  • 49
    • 77952123055 scopus 로고    scopus 로고
    • Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation
    • Trapnell, C. et al. Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation. Nat Biotechnol 28, 511-515 (2010).
    • (2010) Nat Biotechnol , vol.28 , pp. 511-515
    • Trapnell, C.1
  • 50
    • 78649714014 scopus 로고    scopus 로고
    • Analysis and design of RNA sequencing experiments for identifying isoform regulation
    • Katz, Y., Wang, E. T., Airoldi, E. M. & Burge, C. B. Analysis and design of RNA sequencing experiments for identifying isoform regulation. Nat Methods 7, 1009-1015 (2010).
    • (2010) Nat Methods , vol.7 , pp. 1009-1015
    • Katz, Y.1    Wang, E.T.2    Airoldi, E.M.3    Burge, C.B.4
  • 51
    • 0031921640 scopus 로고    scopus 로고
    • Statistical features of human exons and their flanking regions
    • Zhang, M. Q. Statistical features of human exons and their flanking regions. Hum Mol Genet 7, 919-932 (1998).
    • (1998) Hum Mol Genet , vol.7 , pp. 919-932
    • Zhang, M.Q.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.