Promoter-Dependent Translation Controlled by p54nrb and hnRNPM during Myoblast Differentiation.
Fibroblast growth factor 1 (FGF1) is induced during myoblast differentiation at both transcriptional and translational levels. Here, we identify hnRNPM and p54nrb/NONO present in protein complexes bound to the FGF1 promoter and to the mRNA internal ribosome entry site (IRES). Knockdown or overexpression of these proteins indicate that they cooperate in activating IRES-dependent translation during myoblast differentiation, in a promoter-dependent manner. Importantly, mRNA transfection and promoter deletion experiments clearly demonstrate the impact of the FGF1 promoter on the activation of IRES-dependent translation via p54nrb and hnRNPM. Accordingly, knockdown of either p54 or hnRNPM also blocks endogenous FGF1 induction and myotube formation, demonstrating the physiological relevance of this mechanism and the role of these two proteins in myogenesis. Our study demonstrates the cooperative function of hnRNPM and p54nrb as regulators of IRES-dependent translation and indicates the involvement of a promoter-dependent mechanism.
TRADGENE, UPS (EA4554), Toulouse, France.
Nadera
N
Ainaoui
TRADGENE, UPS (EA4554), Toulouse, France.
Fransky
F
Hantelys
TRADGENE, UPS (EA4554), Toulouse, France.
Edith
E
Renaud-Gabardos
TRADGENE, UPS (EA4554), Toulouse, France.
Morgane
M
Bunel
UMR U1037-CRCT, Inserm, UPS, Toulouse, France.
Frédéric
F
Lopez
TRADGENE, UPS (EA4554), Toulouse, France.
Françoise
F
Pujol
UMR U1043-CPTP, Inserm, UPS, Toulouse, France.
Remi
R
Planes
UMR U1043-CPTP, Inserm, UPS, Toulouse, France.
Elmostafa
E
Bahraoui
UMR U5282-IPBS, CNRS, UPS, Toulouse, France.
Carole
C
Pichereaux
UMR U5282-IPBS, CNRS, UPS, Toulouse, France.
Odile
O
Burlet-Schiltz
UMR U1048-I2MC, Inserm, UPS, Toulouse, France.
Angelo
A
Parini
UMR U1048-I2MC, Inserm, UPS, Toulouse, France.
Barbara
B
Garmy-Susini
TRADGENE, UPS (EA4554), Toulouse, France.
Anne-Catherine
AC
Prats
D000818:Animals; D002454:Cell Differentiation; D002460:Cell Line; D049109:Cell Proliferation; D004268:DNA-Binding Proteins; D016220:Fibroblast Growth Factor 1 / Q000235:genetics*; D034761:Heterogeneous-Nuclear Ribonucleoprotein Group M / Q000235:genetics / Q000378:metabolism*; D000067556:Internal Ribosome Entry Sites; D051379:Mice; D032446:Myoblasts / Q000166:cytology* / Q000378:metabolism; D034521:Nuclear Matrix-Associated Proteins / Q000235:genetics / Q000378:metabolism*; D050810:Octamer Transcription Factors / Q000235:genetics / Q000378:metabolism*; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D014176:Protein Biosynthesis; D025941:Protein Interaction Mapping; D034622:RNA Interference; D034741:RNA, Small Interfering / Q000235:genetics; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*
D004268:DNA-Binding Proteins; C440104:HNRNPM protein, human; D034761:Heterogeneous-Nuclear Ribonucleoprotein Group M; D000067556:Internal Ribosome Entry Sites; C083214:NONO protein, human; D034521:Nuclear Matrix-Associated Proteins; D050810:Octamer Transcription Factors; D034741:RNA, Small Interfering; D016601:RNA-Binding Proteins; D016220:Fibroblast Growth Factor 1