Characterization of a novel posttranslational modification in polypyrimidine tract-binding proteins by SUMO1
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Polypyrimidine tract-binding protein 1 (PTBP1) and its brainspecifichomologue, PTBP2, are associated with pre-mRNAs andinfluence pre-mRNA processing, as well as mRNA metabolismand transport. They play important roles in neural differentiationand glioma development. In our study, we detected theexpression of the two proteins in glioma cells and predicted thatthey may be sumoylated using SUMOplot analyses. Weconfirmed that PTBP1 and PTBP2 can be modified by SUMO1with co-immunoprecipitation experiments using 293ET cellstransiently co-expressing SUMO1 and either PTBP1 or PTBP2. We also found that SUMO1 modification of PTBP2 wasenhanced by Ubc9 (E2). The mutation of the sumoylation site(Lys137) of PTBP2 markedly inhibited its modification bySUMO1. Interestingly, in T98G glioma cells, the level ofsumoylated PTBP2 was reduced compared to that of normal braincells. Overall, this study shows that PTBP2 is posttranslationallymodified by SUMO1.
Abstract
Polypyrimidine tract-binding protein 1 (PTBP1) and its brainspecifichomologue, PTBP2, are associated with pre-mRNAs andinfluence pre-mRNA processing, as well as mRNA metabolismand transport. They play important roles in neural differentiationand glioma development. In our study, we detected theexpression of the two proteins in glioma cells and predicted thatthey may be sumoylated using SUMOplot analyses. Weconfirmed that PTBP1 and PTBP2 can be modified by SUMO1with co-immunoprecipitation experiments using 293ET cellstransiently co-expressing SUMO1 and either PTBP1 or PTBP2. We also found that SUMO1 modification of PTBP2 wasenhanced by Ubc9 (E2). The mutation of the sumoylation site(Lys137) of PTBP2 markedly inhibited its modification bySUMO1. Interestingly, in T98G glioma cells, the level ofsumoylated PTBP2 was reduced compared to that of normal braincells. Overall, this study shows that PTBP2 is posttranslationallymodified by SUMO1.
참고문헌 (21)
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