When SUMO met splicing
Spliceosomal proteins have been revealed as SUMO conjugation targets. Moreover, we have reported that many of these are in a SUMO-conjugated form when bound to a pre-mRNA substrate during a splicing reaction. We demonstrated that SUMOylation of Prp3 (PRPF3), a component of the U4/U6 di-snRNP, is req...
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_15476286_v15_n6_p689_Pozzi |
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todo:paper_15476286_v15_n6_p689_Pozzi2023-10-03T16:23:11Z When SUMO met splicing Pozzi, B. Mammi, P. Bragado, L. Giono, L.E. Srebrow, A. post-translational modifications spliceosome Splicing SR proteins SRSF1 SUMO conjugation SUMO protein nuclear protein PRPF3 protein, human RNA splicing factor small nuclear ribonucleoprotein SUMO 1 protein Article conjugation human protein processing RNA splicing spliceosome animal genetics metabolism physiology RNA splicing sumoylation Animals Humans Nuclear Proteins Ribonucleoprotein, U4-U6 Small Nuclear RNA Splicing RNA Splicing Factors SUMO-1 Protein Sumoylation Spliceosomal proteins have been revealed as SUMO conjugation targets. Moreover, we have reported that many of these are in a SUMO-conjugated form when bound to a pre-mRNA substrate during a splicing reaction. We demonstrated that SUMOylation of Prp3 (PRPF3), a component of the U4/U6 di-snRNP, is required for U4/U6•U5 tri-snRNP formation and/or recruitment to active spliceosomes. Expanding upon our previous results, we have shown that the splicing factor SRSF1 stimulates SUMO conjugation to several spliceosomal proteins. Given the relevance of the splicing process, as well as the complex and dynamic nature of its governing machinery, the spliceosome, the molecular mechanisms that modulate its function represent an attractive topic of research. We posit that SUMO conjugation could represent a way of modulating spliceosome assembly and thus, splicing efficiency. How cycles of SUMOylation/de-SUMOylation of spliceosomal proteins become integrated throughout the highly choreographed spliceosomal cycle awaits further investigation. © 2018, © 2018 Informa UK Limited, trading as Taylor & Francis Group. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_15476286_v15_n6_p689_Pozzi |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
post-translational modifications spliceosome Splicing SR proteins SRSF1 SUMO conjugation SUMO protein nuclear protein PRPF3 protein, human RNA splicing factor small nuclear ribonucleoprotein SUMO 1 protein Article conjugation human protein processing RNA splicing spliceosome animal genetics metabolism physiology RNA splicing sumoylation Animals Humans Nuclear Proteins Ribonucleoprotein, U4-U6 Small Nuclear RNA Splicing RNA Splicing Factors SUMO-1 Protein Sumoylation |
| spellingShingle |
post-translational modifications spliceosome Splicing SR proteins SRSF1 SUMO conjugation SUMO protein nuclear protein PRPF3 protein, human RNA splicing factor small nuclear ribonucleoprotein SUMO 1 protein Article conjugation human protein processing RNA splicing spliceosome animal genetics metabolism physiology RNA splicing sumoylation Animals Humans Nuclear Proteins Ribonucleoprotein, U4-U6 Small Nuclear RNA Splicing RNA Splicing Factors SUMO-1 Protein Sumoylation Pozzi, B. Mammi, P. Bragado, L. Giono, L.E. Srebrow, A. When SUMO met splicing |
| topic_facet |
post-translational modifications spliceosome Splicing SR proteins SRSF1 SUMO conjugation SUMO protein nuclear protein PRPF3 protein, human RNA splicing factor small nuclear ribonucleoprotein SUMO 1 protein Article conjugation human protein processing RNA splicing spliceosome animal genetics metabolism physiology RNA splicing sumoylation Animals Humans Nuclear Proteins Ribonucleoprotein, U4-U6 Small Nuclear RNA Splicing RNA Splicing Factors SUMO-1 Protein Sumoylation |
| description |
Spliceosomal proteins have been revealed as SUMO conjugation targets. Moreover, we have reported that many of these are in a SUMO-conjugated form when bound to a pre-mRNA substrate during a splicing reaction. We demonstrated that SUMOylation of Prp3 (PRPF3), a component of the U4/U6 di-snRNP, is required for U4/U6•U5 tri-snRNP formation and/or recruitment to active spliceosomes. Expanding upon our previous results, we have shown that the splicing factor SRSF1 stimulates SUMO conjugation to several spliceosomal proteins. Given the relevance of the splicing process, as well as the complex and dynamic nature of its governing machinery, the spliceosome, the molecular mechanisms that modulate its function represent an attractive topic of research. We posit that SUMO conjugation could represent a way of modulating spliceosome assembly and thus, splicing efficiency. How cycles of SUMOylation/de-SUMOylation of spliceosomal proteins become integrated throughout the highly choreographed spliceosomal cycle awaits further investigation. © 2018, © 2018 Informa UK Limited, trading as Taylor & Francis Group. |
| format |
JOUR |
| author |
Pozzi, B. Mammi, P. Bragado, L. Giono, L.E. Srebrow, A. |
| author_facet |
Pozzi, B. Mammi, P. Bragado, L. Giono, L.E. Srebrow, A. |
| author_sort |
Pozzi, B. |
| title |
When SUMO met splicing |
| title_short |
When SUMO met splicing |
| title_full |
When SUMO met splicing |
| title_fullStr |
When SUMO met splicing |
| title_full_unstemmed |
When SUMO met splicing |
| title_sort |
when sumo met splicing |
| url |
http://hdl.handle.net/20.500.12110/paper_15476286_v15_n6_p689_Pozzi |
| work_keys_str_mv |
AT pozzib whensumometsplicing AT mammip whensumometsplicing AT bragadol whensumometsplicing AT gionole whensumometsplicing AT srebrowa whensumometsplicing |
| _version_ |
1807320603764457472 |