Abstract
Splicing is functionally coupled to transcription, linking the rate of RNA polymerase II (Pol II) elongation and the ability of splicing factors to recognize splice sites (ss) of various strengths. In most cases, slow Pol II elongation allows weak splice sites to be recognized, leading to higher inclusion of alternative exons. Using CFTR alternative exon 9 (E9) as a model, we show here that slowing down elongation can also cause exon skipping by promoting the recruitment of the negative factor ETR-3 onto the UG-repeat at E9 3' splice site, which displaces the constitutive splicing factor U2AF65 from the overlapping polypyrimidine tract. Weakening of E9 5' ss increases ETR-3 binding at the 3' ss and subsequent E9 skipping, whereas strengthening of the 5' ss usage has the opposite effect. This indicates that a delay in the cotranscriptional emergence of the 5' ss promotes ETR-3 recruitment and subsequent inhibition of E9 inclusion.
MeSH Terms
Alternative Splicing
Binding Sites
CELF Proteins
Caco-2 Cells
Cystic Fibrosis Transmembrane Conductance Regulator/genetics,metabolism
Exons
HEK293 Cells
Humans
Models, Genetic
Nerve Tissue Proteins/metabolism
Nuclear Proteins/genetics,metabolism
RNA Polymerase II/metabolism
RNA Splice Sites/physiology
RNA-Binding Proteins/metabolism
Ribonucleoproteins/genetics,metabolism
Splicing Factor U2AF
Transcription, Genetic
Chemicals
CELF Proteins
CELF2 protein, human
CFTR protein, human
Nerve Tissue Proteins
Nuclear Proteins
RNA Splice Sites
RNA-Binding Proteins
Ribonucleoproteins
Splicing Factor U2AF
U2AF2 protein, human
Cystic Fibrosis Transmembrane Conductance Regulator
RNA Polymerase II
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Dujardin Gwendal
Laboratorio de Fisiología y Biología Molecular, Departamento de Fisiología, Biología Molecular y Celular, IFIBYNE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, C1428EHA Buenos Aires, Argentina; Inserm U1078-ECLA Team, Faculty of Medicine, 22 Avenue Camille Desmoulins, 29238 Brest Cedex 3, France.
Lafaille Celina
Laboratorio de Fisiología y Biología Molecular, Departamento de Fisiología, Biología Molecular y Celular, IFIBYNE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, C1428EHA Buenos Aires, Argentina.
de la Mata Manuel
Laboratorio de Fisiología y Biología Molecular, Departamento de Fisiología, Biología Molecular y Celular, IFIBYNE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, C1428EHA Buenos Aires, Argentina.
Marasco Luciano E
Laboratorio de Fisiología y Biología Molecular, Departamento de Fisiología, Biología Molecular y Celular, IFIBYNE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, C1428EHA Buenos Aires, Argentina.
Muñoz Manuel J
Laboratorio de Fisiología y Biología Molecular, Departamento de Fisiología, Biología Molecular y Celular, IFIBYNE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, C1428EHA Buenos Aires, Argentina.
Le Jossic-Corcos Catherine
Inserm U1078-ECLA Team, Faculty of Medicine, 22 Avenue Camille Desmoulins, 29238 Brest Cedex 3, France.
Corcos Laurent
Inserm U1078-ECLA Team, Faculty of Medicine, 22 Avenue Camille Desmoulins, 29238 Brest Cedex 3, France.
Kornblihtt Alberto R
Laboratorio de Fisiología y Biología Molecular, Departamento de Fisiología, Biología Molecular y Celular, IFIBYNE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, C1428EHA Buenos Aires, Argentina. Electronic address:
[email protected].