The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
RNA Chemical Proteomics Reveals the N6-Methyladenosine (m6A)-Regulated Protein–RNA Interactome
Abstract
Epitranscriptomic RNA modifications can regulate mRNA function; however, there is a major gap in our understanding of the biochemical mechanisms mediating their effects. Here, we develop a chemical proteomics approach relying upon photo-cross-linking with synthetic diazirine-containing RNA probes and quantitative proteomics to profile RNA-protein interactions regulated by N 6 -methyladenosine (m 6 A), the most abundant internal modification in eukaryotic RNA. In addition to identifying YTH domain-containing proteins and ALKBH5, known interactors of this modification, we find that FMR1 and LRPPRC, two proteins associated with human disease, "read" this modification. Surprisingly, we also find that m 6 A disrupts RNA binding by the stress granule proteins G3BP1/2, USP10, CAPRIN1, and RBM42. Our work provides a general strategy for interrogating the interactome of RNA modifications and reveals the biochemical mechanisms underlying m 6 A function in the cell.
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“HNRNPA2B1 is known to act as a reader of m6A in the nucleus, where it regulates chromatin state and transcription”
From Interaction of tau with HNRNPA2B1 and N6-methyladenosine RNA mediates the progression of tauopathy (2021) · cites this paper as Arguello et al., 2017
Citations
Cites
N6-methyladenosine-dependent regulation of messenger RNA stability
Wang, X., Lu, Z., Gomez, A., Hon, G. C., Yue, Y., Han, D., Fu, Y., Parisien, M., Dai, Q., Jia, G., et al. (2014) · Nature · doi:10.1038/nature12730 · Cited by 4,558
Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons
Meyer, K. D., Saletore, Y., Zumbo, P., Elemento, O., Mason, C. E., & Jaffrey, S. R. (2012) · Cell · doi:10.1016/j.cell.2012.05.003 · Cited by 4,223
N6-Methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO
Jia, G., Fu, Y., Zhao, X., Dai, Q., Zheng, G., Yang, Y., Yi, C., Lindahl, T., Pan, T., Yang, Y.-G., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.687 · Cited by 4,106
ALKBH5 Is a Mammalian RNA Demethylase that Impacts RNA Metabolism and Mouse Fertility
Zheng, G., Dahl, J. A., Niu, Y., Fedorcsak, P., Huang, C.-M., Li, C. J., Vågbø, C. B., Shi, Y., Wang, W.-L., Song, S.-H., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.015 · Cited by 3,550
N6-methyladenosine Modulates Messenger RNA Translation Efficiency
Wang, X., Zhao, B. S., Roundtree, I. A., Lu, Z., Han, D., Ma, H., Weng, X., Chen, K., Shi, H., & He, C. (2015) · Cell · doi:10.1016/j.cell.2015.05.014 · Cited by 3,483
Nuclear m6A Reader YTHDC1 Regulates mRNA Splicing
Xiao, W., Adhikari, S., Dahal, U., Chen, Y.-S., Hao, Y.-J., Sun, B.-F., Sun, H.-Y., Li, A., Ping, X.-L., Lai, W.-Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.012 · Cited by 2,054
A census of human RNA-binding proteins
Gerstberger, S., Hafner, M., & Tuschl, T. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3813 · Cited by 2,032
YTHDF3 facilitates translation and decay of N6-methyladenosine-modified RNA
Shi, H., Wang, X., Lu, Z., Zhao, B. S., Ma, H., Hsu, P. J., Liu, C., & He, C. (2017) · Cell Research · doi:10.1038/cr.2017.15 · Cited by 1,815
HITS-CLIP yields genome-wide insights into brain alternative RNA processing
Licatalosi, D. D., Mele, A., Fak, J. J., Ule, J., Kayikci, M., Chi, S. W., Clark, T. A., Schweitzer, A. C., Blume, J. E., Wang, X., et al. (2008) · Nature · doi:10.1038/nature07488 · Cited by 1,352
FMRP targets distinct mRNA sequence elements to regulate protein expression
Ascano, M., Mukherjee, N., Bandaru, P., Miller, J. B., Nusbaum, J. D., Corcoran, D. L., Langlois, C., Munschauer, M., Dewell, S., Hafner, M., et al. (2012) · Nature · doi:10.1038/nature11737 · Cited by 701
Epitranscriptome sequencing technologies: decoding RNA modifications
Li, X., Xiong, X., & Yi, C. (2017) · Nature Methods · doi:10.1038/nmeth.4110 · Cited by 447
Research works printed but not linked: 15
- 10.1093/nar/gkq1028 · DOI · Paper page
- 10.1038/nature11112 · DOI · Paper page
- 10.1016/j.cell.2010.03.009 · DOI · Paper page
- 10.1016/j.bmc.2011.06.066 · DOI · Paper page
- Kauer J. C., 1986, J. Biol. Chem., 261, 10695, 10.1016/S0021-9258(18)67441-1 · DOI · Paper page
- 10.1038/nchembio.1654 · DOI · Paper page
- 10.1038/cr.2014.152 · DOI · Paper page
- 10.1261/rna.2136010 · DOI
- 10.1093/hmg/9.6.901 · DOI · Paper page
- 10.1016/j.tibs.2013.07.004 · DOI · Paper page
- 10.1111/j.1365-2443.2008.01256.x · DOI
- 10.1083/jcb.201508028 · DOI · Paper page
- 10.1016/j.molcel.2014.03.023 · DOI · Paper page
- 10.1038/emboj.2011.392 · DOI · Paper page
- 10.1038/nsmb.3462 · DOI · Paper page
Cited by
m 6 A RNA methylation: from mechanisms to therapeutic potential
He, P. C., & He, C. (2021) · The EMBO Journal · doi:10.15252/embj.2020105977 · Cited by 786
The RNA modification N6-methyladenosine as a novel regulator of the immune system
Shulman, Z., & Stern-Ginossar, N. (2020) · Nature Immunology · doi:10.1038/s41590-020-0650-4 · Cited by 426
The m6A epitranscriptome: transcriptome plasticity in brain development and function
Livneh, I., Moshitch-Moshkovitz, S., Amariglio, N., Rechavi, G., & Dominissini, D. (2020) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0244-z · Cited by 330
The role of m6A modification in physiology and disease
Yang, C., Hu, Y., Zhou, B., Bao, Y., Li, Z., Gong, C., Yang, H., Wang, S., & Xiao, Y. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-03143-z · Cited by 200
Interaction of tau with HNRNPA2B1 and N6-methyladenosine RNA mediates the progression of tauopathy
Jiang, L., Lin, W., Zhang, C., Ash, P. E. A., Verma, M., Kwan, J., van Vliet, E., Yang, Z., Cruz, A. L., Boudeau, S., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.038 · Cited by 177
Metadata
- Authors
- Arguello, A. E., DeLiberto, A. N., & Kleiner, R. E.
- Affiliations
- Department of Chemistry, Princeton University, Princeton, New Jersey 08544, United States
- ORCID
- Kleiner, Ralph E.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2017-11-20
- Volume
- 139
- Issue
- 48
- Pages
- 17249-17252
- ISSN
- 0002-7863
- 1520-5126
- Cited by
- 254
- References
- 11
- Language
- en
- Funders
- Princeton University
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