Journal
CELL REPORTS
Volume 25, Issue 3, Pages 726-+Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2018.09.041
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Funding
- National Ataxia Foundation (Young Investigator Research Grant 2017), United States
- NIH, United States [P30CA125123]
- Howard Hughes Medical Institute, United States
- NIH/National Institute of Neurological Disorders and Stroke (NIH/NINDS), United States [2R37NS027699]
- Baylor College of Medicine IDDRC, United States [U54HD083092]
- Cancer Prevention Research Institute of Texas [RP170387]
- Houston endowment, United States
- NIH/National Institute of Aging (NIH/NIA), United States [AG05733902]
- NIH/National Institute of General Medical Sciences (NIH/NIGMS), United States [GM12003302]
- P30 Digestive Disease Center support grant, United States [NIDDK-DK56338]
- P30 Cancer Center support grant at Baylor College of Medicine, United States [NCI-CA125123]
- Huffington foundation, United States
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RNA splicing entails the coordinated interaction of more than 150 proteins in the spliceosome, one of the most complex of the cell's molecular machines. We previously discovered that the RNA-binding motif protein 17 (RBM17), a component of the spliceosome, is essential for survival and cell maintenance. Here, we find that it interacts with the spliceosomal factors U2SURP and CHERP and that they reciprocally regulate each other's stability, both in mouse and in human cells. Individual knockdown of each of the three proteins induces overlapping changes in splicing and gene expression of transcripts enriched for RNA-processing factors. Our results elucidate the function of RBM17, U2SURP, and CHERP and link the activity of the spliceosome to the regulation of downstream RNA-binding proteins. These data support the hypothesis that, beyond driving constitutive splicing, spliceosomal factors can regulate alternative splicing of specific targets.
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