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Proteomic Investigations Reveal a Role for RNA Processing Factor THRAP3 in the DNA Damage Response
Open accessAbstract
Summary The regulatory networks of the DNA damage response (DDR) encompass many proteins and posttranslational modifications. Here, we use mass spectrometry-based proteomics to analyze the systems-wide response to DNA damage by parallel quantification of the DDR-regulated phosphoproteome, acetylome and proteome. We show that phosphorylation-dependent signaling networks are regulated more strongly compared to acetylation. Among the phosphorylated proteins identified are many putative substrates of DNA-PK, ATM and ATR kinases, but a majority of phosphorylated proteins do not share the ATM/ATR/DNA-PK target consensus, suggesting an important role of downstream kinases in amplifying DDR signals. We show that the splicing-regulator phosphatase PPM1G is recruited to sites of DNA damage, while the splicing-associated protein THRAP3 is excluded from these regions. Moreover, THRAP3 depletion causes cellular hypersensitivity to DNA damaging agents, thus suggesting an important link between RNA metabolism and DNA repair. Our results broaden the knowledge of DNA damage signaling networks and identify novel components of the DDR.
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Metadata
- Authors
- Beli, P., Lukashchuk, N., Wagner, S. A., Weinert, B. T., Olsen, J. V., Baskcomb, L., Mann, M., Jackson, S. P., & Choudhary, C.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2012-04
- Volume
- 46
- Issue
- 2
- Pages
- 212-225
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1998163656
- Cited by
- 330
- References
- 57
- FWCI
- 11.27
- Type
- journal article
- Language
- en
- Open access
- bronze
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