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Antagonistic regulation of alpha-actinin alternative splicing by CELF proteins and polypyrimidine tract binding protein.
RNA. 2003 Apr; 9(4):443-56.RNA

Abstract

The alpha-actinin gene has a pair of alternatively spliced exons. The smooth muscle (SM) exon is repressed in most cell types by polypyrimidine tract binding protein (PTB). CELF (CUG-BP and ETR3-like factors) family proteins, splicing regulators whose activities are altered in myotonic dystrophy, were found to coordinately regulate selection of the two alpha-actinin exons. CUG-BP and ETR3 activated the SM exon, and along with CELF4 they were also able to repress splicing of the NM (nonmuscle) exon both in vivo and in vitro. Activation of SM exon splicing was associated with displacement of PTB from the polypyrimidine tract by binding of CUG-BP at adjacent sites. Our data provides direct evidence for the activity of CELF proteins as both activators and repressors of splicing within a single-model system of alternative splicing, and suggests a model whereby alpha-actinin alternative splicing is regulated by synergistic and antagonistic interactions between members of the CELF and PTB families.

Authors+Show Affiliations

Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

12649496

Citation

Gromak, Natalia, et al. "Antagonistic Regulation of Alpha-actinin Alternative Splicing By CELF Proteins and Polypyrimidine Tract Binding Protein." RNA (New York, N.Y.), vol. 9, no. 4, 2003, pp. 443-56.
Gromak N, Matlin AJ, Cooper TA, et al. Antagonistic regulation of alpha-actinin alternative splicing by CELF proteins and polypyrimidine tract binding protein. RNA. 2003;9(4):443-56.
Gromak, N., Matlin, A. J., Cooper, T. A., & Smith, C. W. (2003). Antagonistic regulation of alpha-actinin alternative splicing by CELF proteins and polypyrimidine tract binding protein. RNA (New York, N.Y.), 9(4), 443-56.
Gromak N, et al. Antagonistic Regulation of Alpha-actinin Alternative Splicing By CELF Proteins and Polypyrimidine Tract Binding Protein. RNA. 2003;9(4):443-56. PubMed PMID: 12649496.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Antagonistic regulation of alpha-actinin alternative splicing by CELF proteins and polypyrimidine tract binding protein. AU - Gromak,Natalia, AU - Matlin,Arianne J, AU - Cooper,Thomas A, AU - Smith,Christopher W J, PY - 2003/3/22/pubmed PY - 2003/5/7/medline PY - 2003/3/22/entrez SP - 443 EP - 56 JF - RNA (New York, N.Y.) JO - RNA VL - 9 IS - 4 N2 - The alpha-actinin gene has a pair of alternatively spliced exons. The smooth muscle (SM) exon is repressed in most cell types by polypyrimidine tract binding protein (PTB). CELF (CUG-BP and ETR3-like factors) family proteins, splicing regulators whose activities are altered in myotonic dystrophy, were found to coordinately regulate selection of the two alpha-actinin exons. CUG-BP and ETR3 activated the SM exon, and along with CELF4 they were also able to repress splicing of the NM (nonmuscle) exon both in vivo and in vitro. Activation of SM exon splicing was associated with displacement of PTB from the polypyrimidine tract by binding of CUG-BP at adjacent sites. Our data provides direct evidence for the activity of CELF proteins as both activators and repressors of splicing within a single-model system of alternative splicing, and suggests a model whereby alpha-actinin alternative splicing is regulated by synergistic and antagonistic interactions between members of the CELF and PTB families. SN - 1355-8382 UR - https://www.unboundmedicine.com/medline/citation/12649496/Antagonistic_regulation_of_alpha_actinin_alternative_splicing_by_CELF_proteins_and_polypyrimidine_tract_binding_protein_ DB - PRIME DP - Unbound Medicine ER -