The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Alternative 3′ UTRs act as scaffolds to regulate membrane protein localization
Open accessAbstract
About half of human genes use alternative cleavage and polyadenylation (ApA) to generate messenger RNA transcripts that differ in the length of their 3' untranslated regions (3' UTRs) while producing the same protein. Here we show in human cell lines that alternative 3' UTRs differentially regulate the localization of membrane proteins. The long 3' UTR of CD47 enables efficient cell surface expression of CD47 protein, whereas the short 3' UTR primarily localizes CD47 protein to the endoplasmic reticulum. CD47 protein localization occurs post-translationally and independently of RNA localization. In our model of 3' UTR-dependent protein localization, the long 3' UTR of CD47 acts as a scaffold to recruit a protein complex containing the RNA-binding protein HuR (also known as ELAVL1) and SET to the site of translation. This facilitates interaction of SET with the newly translated cytoplasmic domains of CD47 and results in subsequent translocation of CD47 to the plasma membrane via activated RAC1 (ref. 5). We also show that CD47 protein has different functions depending on whether it was generated by the short or long 3' UTR isoforms. Thus, ApA contributes to the functional diversity of the proteome without changing the amino acid sequence. 3' UTR-dependent protein localization has the potential to be a widespread trafficking mechanism for membrane proteins because HuR binds to thousands of mRNAs, and we show that the long 3' UTRs of CD44, ITGA1 and TNFRSF13C, which are bound by HuR, increase surface protein expression compared to their corresponding short 3' UTRs. We propose that during translation the scaffold function of 3' UTRs facilitates binding of proteins to nascent proteins to direct their transport or function--and this role of 3' UTRs can be regulated by ApA.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The 5′ and 3′ UTRs flanking the coding region regulate mRNA translation, half-life and subcellular localization10,14.”
From mRNA vaccines for infectious diseases: principles, delivery and clinical translation (2021) · cites this paper as [14]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890
The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90164-8 · Cited by 3,616
Role of CD47 as a Marker of Self on Red Blood Cells
Oldenborg, P., Zheleznyak, A., Fang, Y., Lagenaur, C. F., Gresham, H. D., & Lindberg, F. P. (2000) · Science · doi:10.1126/science.288.5473.2051 · Cited by 2,018
Mayr, C., & Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.06.016 · Cited by 1,613
Self-citationLocalization of ASH1 mRNA particles in living yeast.
Bertrand, E., Chartrand, P., Schaefer, M., Shenoy, S., Singer, R., & Long, R. M. (1998) · Molecules and Cells · doi:10.1016/s1097-2765(00)80143-4 · Cited by 1,597
CD47 Is Upregulated on Circulating Hematopoietic Stem Cells and Leukemia Cells to Avoid Phagocytosis
Jaiswal, S., Jamieson, C. H. M., Pang, W. W., Park, C. Y., Chao, M. P., Majeti, R., Traver, D. J., van Rooijen, N., & Weissman, I. L. (2009) · Cell · doi:10.1016/j.cell.2009.05.046 · Cited by 1,578
Sandberg, R., Neilson, J. R., Sarma, A., Sharp, P. A., & Burge, C. B. (2008) · Science · doi:10.1126/science.1155390 · Cited by 1,349
A New ER Trafficking Signal Regulates the Subunit Stoichiometry of Plasma Membrane KATP Channels
Zerangue, N., Schwappach, B., Jan, Y. N., & Jan, L. Y. (1999) · Neuron · doi:10.1016/s0896-6273(00)80708-4 · Cited by 1,025
Fan, X. C., & Steitz, J. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3448 · Cited by 866
Transcriptome-wide Analysis of Regulatory Interactions of the RNA-Binding Protein HuR
Lebedeva, S., Jens, M., Theil, K., Schwanhäusser, B., Selbach, M., Landthaler, M., & Rajewsky, N. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.008 · Cited by 716
Flagged first, then by citations
Research works printed but not linked: 1
- Frazier, W. A., Isenberg, J. S., Kaur, S. & Roberts, D. D. in UCSD Nature Molecule Pages (University of California, San Diego, 2010)
Cited by
Sorted by citations
Items 101–200 of 473
Blake, D., & Lynch, K. W. (2021) · Immunological Reviews · doi:10.1111/imr.13018 · Cited by 49
Shen, T., Li, H., Song, Y., Li, L., Lin, J., Wei, G., & Ni, T. (2019) · Aging · doi:10.18632/aging.101836 · Cited by 48
Pyko, J., Rosemann, J., Krauspe, V., Kappler, M., Eckert, A. W., Hämmerle, M., & Gutschner, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186835 · Cited by 49
Regulation and function of alternative polyadenylation in development and differentiation
Gallicchio, L., Olivares, G. H., Berry, C. W., & Fuller, M. T. (2023) · RNA Biology · doi:10.1080/15476286.2023.2275109 · Cited by 49
Hollerer, I., Curk, T., Haase, B., Beneš, V., Hauer, C., Neu‐Yilik, G., Bhuvanagiri, M., Hentze, M. W., & Kulozik, A. E. (2016) · RNA · doi:10.1261/rna.055657.115 · Cited by 49
Alternative Polyadenylation of Mammalian Transcripts Is Generally Deleterious, Not Adaptive
Xu, C., & Zhang, J. (2018) · Cell Systems · doi:10.1016/j.cels.2018.05.007 · Cited by 49
Chatrikhi, R., Mallory, M. J., Gazzara, M. R., Agosto, L. M., Zhu, W. S., Litterman, A. J., Ansel, K. M., & Lynch, K. W. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.022 · Cited by 47
Transcriptomic and proteomic signatures of stemness and differentiation in the colon crypt
Habowski, A. N., Flesher, J. L., Bates, J. M., Tsai, C., Martin, K., Zhao, R., Ganesan, A. K., Edwards, R. A., Shi, T., Wiley, H. S., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-01181-z · Cited by 49
Enhancers regulate 3′ end processing activity to control expression of alternative 3′UTR isoforms
Kwon, B., Fansler, M. M., Patel, N. D., Lee, J., Ma, W., & Mayr, C. (2022) · Nature Communications · doi:10.1038/s41467-022-30525-y · Cited by 47
Self-citationLü, W., Lee, S., Majumdar, S., Zhang, B., Sanfilippo, P., Joseph, B. J., Miura, P., Soller, M., & Lai, E. C. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.09.007 · Cited by 46
The transcriptional elongation rate regulates alternative polyadenylation in yeast
Geisberg, J. V., Moqtaderi, Z., & Struhl, K. (2020) · eLife · doi:10.7554/elife.59810 · Cited by 45
Neumann, D., Pillman, K. A., Dredge, B. K., Bert, A. G., Phillips, C. A., Lumb, R., Ramani, Y., Bracken, C. P., Hollier, B. G., Selth, L. A., et al. (2023) · RNA Biology · doi:10.1080/15476286.2023.2294222 · Cited by 45
de Bruin, R. G., van der Veer, E. P., Prins, J., Lee, D. H., Dane, M. J. C., Zhang, H., Roeten, M. K., Bijkerk, R., de Boer, H. C., Rabelink, T. J., et al. (2016) · Scientific Reports · doi:10.1038/srep21643 · Cited by 46
Engineered mRNA Delivery Systems for Biomedical Applications
Wang, J., Zhu, H., Gan, J., Liang, G., Li, L., & Zhao, Y. (2023) · Advanced Materials · doi:10.1002/adma.202308029 · Cited by 46
Mert, U., & Şanlioğlu, A. D. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2321-z · Cited by 48
Romo, L., Ashar-Patel, A., Pfister, E. L., & D, N. A. M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.009 · Cited by 47
ELAV/Hu RNA binding proteins determine multiple programs of neural alternative splicing
Lee, S., Wei, L., Zhang, B., Goering, R., Majumdar, S., Wen, J., Taliaferro, J. M., & Lai, E. C. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009439 · Cited by 46
Goering, R., Engel, K. L., Gillen, A. E., Fong, N., Bentley, D. L., & Taliaferro, J. M. (2021) · BMC Genomics · doi:10.1186/s12864-021-07781-1 · Cited by 45
RNA localization and co‐translational interactions control RAB13 GTPase function and cell migration
Moissoglu, K., Stueland, M., Gasparski, A. N., Wang, T., Jenkins, L. M., Hastings, M. L., & Mili, S. (2020) · The EMBO Journal · doi:10.15252/embj.2020104958 · Cited by 43
Structural determinants of co-translational protein complex assembly
Mallik, S., Venezian, J., Lobov, A., Heidenreich, M., Garcia-Seisdedos, H., Yeates, T. O., Shiber, A., & Levy, E. D. (2025) · Cell · doi:10.1016/j.cell.2024.11.013 · Cited by 42
Regulation of NGF Signaling by an Axonal Untranslated mRNA
Crerar, H., Scott-Solomon, E., Bodkin-Clarke, C., Andreassi, C., Hazbon, M., Logie, E., Cano‐Jaimez, M., Gaspari, M., Kuruvilla, R., & Riccio, A. (2019) · Neuron · doi:10.1016/j.neuron.2019.02.011 · Cited by 41
Alternative polyadenylation: An enigma of transcript length variation in health and disease
Mohanan, N. K., Shaji, F., Koshre, G. R., & Laishram, R. S. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1692 · Cited by 43
Epigenetics and the dynamics of chromatin during adenovirus infections
Lynch, K. L., Gooding, L. R., Garnett‐Benson, C., Ornelles, D. A., & Avgousti, D. C. (2019) · FEBS Letters · doi:10.1002/1873-3468.13697 · Cited by 40
Kucherenko, M. M., & Shcherbata, H. R. (2018) · Nature Communications · doi:10.1038/s41467-017-02757-w · Cited by 39
Bacterial 3′UTRs: A Useful Resource in Post-transcriptional Regulation
Menendez-Gil, P., & Toledo‐Arana, A. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.617633 · Cited by 42
Alternative Polyadenylation in Stem Cell Self-Renewal and Differentiation
Sommerkamp, P., Cabezas‐Wallscheid, N., & Trumpp, A. (2021) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2021.04.006 · Cited by 40
T cells at work: How post‐transcriptional mechanisms control T cell homeostasis and activation
Jurgens, A. P., Popović, B., & Wolkers, M. C. (2021) · European Journal of Immunology · doi:10.1002/eji.202049055 · Cited by 42
Alternative polyadenylation and RNA-binding proteins
Erson-Bensan, A. E. (2016) · Journal of Molecular Endocrinology · doi:10.1530/jme-16-0070 · Cited by 39
Fear extinction is regulated by the activity of long noncoding RNAs at the synapse
Liau, W., Zhao, Q., Bademosi, A. T., Gormal, R. S., Gong, H., Marshall, P. R., Periyakaruppiah, A., Madugalle, S. U., Zajaczkowski, E. L., Leighton, L. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43535-1 · Cited by 38
Ogorodnikov, A., Kargapolova, Y., & Danckwardt, S. (2016) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-016-1828-3 · Cited by 39
Understanding Neurodevelopmental Disorders: The Promise of Regulatory Variation in the 3′UTRome
Wanke, K. A., Devanna, P., & Vernes, S. C. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.11.006 · Cited by 42
Zhao, Z., Xu, Q., Wei, R., Wang, W., Ding, D., Yang, Y., Yao, J., Zhang, L., Hu, Y., Wei, G., et al. (2021) · Genome Research · doi:10.1101/gr.271627.120 · Cited by 40
C5orf30 is a negative regulator of tissue damage in rheumatoid arthritis
Muthana, M., Hawtree, S., Wilshaw, A., Linehan, E., Roberts, H., Khetan, S., Adeleke, G. E., Wright, F., Akil, M., Fearon, U., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1501947112 · Cited by 37
NAA10 polyadenylation signal variants cause syndromic microphthalmia
Johnston, J. J., Williamson, K. A., Chou, C. M., Sapp, J. C., Ansari, M., Chapman, H. M., Cooper, D. N., Dabir, T. A., Dudley, J. N., Holt, R. J., et al. (2019) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2018-105836 · Cited by 37
Yoon, Y., Klomp, J. A., Martín-Martín, I., Criscione, F., Calvo, E., Ribeiro, J. M. C., & Schmidt‐Ott, U. (2019) · eLife · doi:10.7554/elife.46711 · Cited by 37
Mutations in cis that affect mRNA synthesis, processing and translation
Roos, D., & de Boer, M. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166166 · Cited by 37
Zhou, R., Xiao, X., He, P., Zhao, Y., Xu, M., Zheng, X., Yang, R., Chen, S., Zhou, L., Zhang, D., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac167 · Cited by 38
DeeReCT-APA: Prediction of Alternative Polyadenylation Site Usage Through Deep Learning
Li, Z., Li, Y., Zhang, B., Li, Y., Long, Y., Zhou, J., Zou, X., Zhang, M., Hu, Y., Chen, W., et al. (2022) · Genomics, Proteomics & Bioinformatics · doi:10.1016/j.gpb.2020.05.004 · Cited by 37
Ziff, O. J., Harley, J., Wang, Y., Neeves, J., Tyzack, G. E., Ibrahim, F., Skehel, M. J., Chakrabarti, A. M., Kelly, G. P., & Patani, R. (2023) · Neuron · doi:10.1016/j.neuron.2023.06.019 · Cited by 36
Aberrant plasticity of peripheral sensory axons in a painful neuropathy
Hirai, T., Mulpuri, Y., Cheng, Y., Xia, Z., Li, W., Ruangsri, S., Spigelman, I., & Nishimura, I. (2017) · Scientific Reports · doi:10.1038/s41598-017-03390-9 · Cited by 36
Moqtaderi, Z., Geisberg, J. V., & Struhl, K. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.08.044 · Cited by 35
A survey on identification and quantification of alternative polyadenylation sites from RNA-seq data
Chen, M., Ji, G., Fu, H., Lin, Q., Ye, C., Ye, W., Su, Y., & Wu, X. (2019) · Briefings in Bioinformatics · doi:10.1093/bib/bbz068 · Cited by 35
The Role of Alternative Polyadenylation in the Regulation of Subcellular RNA Localization
Arora, A., Goering, R., Lo, H. G., Lo, J., Moffatt, C., & Taliaferro, J. M. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2021.818668 · Cited by 40
Recurrent tumor-specific regulation of alternative polyadenylation of cancer-related genes
Xue, Z., Warren, R. L., Gibb, E. A., MacMillan, D., Wong, J., Chiu, R., Hammond, S. A., Yang, C., Nip, K. M., Ennis, C. A., et al. (2018) · BMC Genomics · doi:10.1186/s12864-018-4903-7 · Cited by 33
mRNA-Based Vaccines and Mode of Action
Gergen, J., & Petsch, B. (2020) · Current topics in microbiology and immunology · doi:10.1007/82_2020_230 · Cited by 36
mRNA alternative polyadenylation (APA) in regulation of gene expression and diseases
Guo, S., & Lin, S. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.09.005 · Cited by 34
Ye, W., Lian, Q., Ye, C., & Wu, X. (2022) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2022.09.005 · Cited by 34
Davis, A. G., Johnson, D. T., Zheng, D., Wang, R., Jayne, N. D., Liu, M., Shin, J., Wang, L., Stoner, S. A., Zhou, J., et al. (2021) · Blood · doi:10.1182/blood.2020005693 · Cited by 32
Resistance to targeted therapies in acute myeloid leukemia
Mecklenbrauck, R., & Heuser, M. (2022) · Clinical & Experimental Metastasis · doi:10.1007/s10585-022-10189-0 · Cited by 31
Zhang, X., Zhang, S., Ma, L., Jiang, E., Xu, H., Chen, R., Yang, Q., Chen, H., Li, Z., & Lan, X. (2017) · Oncotarget · doi:10.18632/oncotarget.23260 · Cited by 31
The Role of cis- and trans-Acting RNA Regulatory Elements in Leukemia
Elcheva, I. A., & Spiegelman, V. S. (2020) · Cancers · doi:10.3390/cancers12123854 · Cited by 34
Splicing-accessible coding 3′UTRs control protein stability and interaction networks
Preußner, M., Gao, Q., Morrison, E., Herdt, O., Finkernagel, F., Schümann, M., Krause, E., Freund, C., Chen, W., & Heyd, F. (2020) · Genome biology · doi:10.1186/s13059-020-02102-3 · Cited by 29
Jobbins, A. M., Haberman, N., Artigas, N., Amourda, C., Paterson, H. A. B., Yu, S., Blackford, S. J. I., Montoya, A., Dore, M. H., Wang, Y.-F., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac165 · Cited by 32
A working model for condensate RNA-binding proteins as matchmakers for protein complex assembly
Chen, X., & Mayr, C. (2021) · RNA · doi:10.1261/rna.078995.121 · Cited by 29
Self-citationThe emerging roles of CFIm25 ( NUDT21/CPSF5 ) in human biology and disease
Masamha, C. P. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1757 · Cited by 28
The mRNA vaccine, a swift warhead against a moving infectious disease target
Mir, S., & Mir, M. A. (2024) · Expert Review of Vaccines · doi:10.1080/14760584.2024.2320327 · Cited by 28
Global analysis of regulatory divergence in the evolution of mouse alternative polyadenylation
Xiao, M., Zhang, B., Li, Y., Gao, Q., Sun, W., & Chen, W. (2016) · Molecular Systems Biology · doi:10.15252/msb.20167375 · Cited by 27
Structural–functional diversity of CD47 proteoforms
Zhang, T., Wang, F., Xu, L., & Yang, Y. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1329562 · Cited by 26
Local Translation in Nervous System Pathologies
Gamarra, M., de la Cruz, A., Blanco‐Urrejola, M., & Baleriola, J. (2021) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2021.689208 · Cited by 30
Lang, S., Nguyen, D., Bhadra, P., Jung, M., Helms, V., & Zimmermann, R. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.833540 · Cited by 29
Fernandes, N., & Buchan, J. R. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa352 · Cited by 26
The roles and mechanisms of coding and noncoding RNA variations in cancer
Kim, S. Y., Na, M. J., Yoon, S., Shin, E., Ha, J. W., Jeon, S., & Nam, S. W. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01307-x · Cited by 25
Mariella, E., Marotta, F., Grassi, E., Gilotto, S., & Provero, P. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00714 · Cited by 25
Endogenous p53 expression in human and mouse is not regulated by its 3′UTR
Mitschka, S., & Mayr, C. (2021) · eLife · doi:10.7554/elife.65700 · Cited by 26
Self-citationSpecific Features of RNA Polymerases I and III: Structure and Assembly
Turowski, T. W., & Boguta, M. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.680090 · Cited by 29
Jereb, S., Hwang, H., Otterloo, E. V., Govek, E., Fak, J. J., Yuan, Y., Hatten, M. E., & Darnell, R. B. (2018) · eLife · doi:10.7554/elife.34042 · Cited by 25
Pathogenic diversity of RNA variants and RNA variation-associated factors in cancer development
Yang, H. D., & Nam, S. W. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0429-6 · Cited by 25
Cong, L., Sugden, S., Leclair, P., Lim, C. J., Pham, T. N. Q., & Cohen, É. A. (2021) · mBio · doi:10.1128/mbio.01920-21 · Cited by 27
Regulation of neuronal RNA signatures by ELAV /Hu proteins
Hilgers, V. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1733 · Cited by 26
Ma, H., Cai, L., Lin, J., Zhou, K., & Li, Q. Q. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.866054 · Cited by 24
T-cells require post-transcriptional regulation for accurate immune responses
Salerno, F., & Wolkers, M. C. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150154 · Cited by 24
Application of genome editing techniques to regulate gene expression in crops
Dong, H. (2024) · BMC Plant Biology · doi:10.1186/s12870-024-04786-2 · Cited by 25
Regulation of gene expression by alternative polyadenylation in health and disease
Tian, B., Yu, S., & Zhang, Q. (2026) · Nature Reviews Genetics · doi:10.1038/s41576-025-00928-w · Cited by 23
RNA-biology ruling cancer progression? Focus on 3′UTRs and splicing
Erson-Bensan, A. E. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09884-9 · Cited by 23
RNAs as Regulators of Cellular Matchmaking
Fernandes, N., & Buchan, J. R. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.634146 · Cited by 24
mRNA delivery technologies: Toward clinical translation
Gómez-Aguado, I., Rodríguez-Castejón, J., Beraza-Millor, M., Rodríguez‐Gascón, A., del Pozo‐Rodríguez, A., & Solinís, M. Á. (2022) · International review of cytology · doi:10.1016/bs.ircmb.2022.04.010 · Cited by 23
Cao, M. C., & Scotter, E. L. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049418 · Cited by 25
Downregulation of apoptotic repressor AVEN exacerbates cardiac injury after myocardial infarction
Yu, P. F., Song, S., Zhang, X., Cui, S., Wei, G., Huang, Z., Zeng, L., Ni, T., & Sun, A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2302482120 · Cited by 24
Nuclear export is a limiting factor in eukaryotic mRNA metabolism
Müller, J. M., Moos, K., Baar, T., Maier, K. C., Žumer, K., & Tresch, A. (2024) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1012059 · Cited by 23
Sequence determinants as key regulators in gene expression of T cells
Nicolet, B. P., Zandhuis, N. D., Lattanzio, V. M., & Wolkers, M. C. (2021) · Immunological Reviews · doi:10.1111/imr.13021 · Cited by 23
RNA assemblages orchestrate complex cellular processes
Nielsen, F. C., Hansen, H. T., & Christiansen, J. (2016) · BioEssays · doi:10.1002/bies.201500175 · Cited by 22
Cao, M. C., Ryan, B., Wu, J., Curtis, M. A., Faull, R. L. M., Dragunow, M., & Scotter, E. L. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106245 · Cited by 23
Puzzling out nuclear pore complex assembly
Penzo, A., & Palancade, B. (2023) · FEBS Letters · doi:10.1002/1873-3468.14713 · Cited by 22
Sun, X., Nagahama, Y., Singh, S. K., Kozakai, Y., Nabeshima, H., Fukushima, K., Tanaka, H., Motooka, D., Fukui, E., Vivier, É., et al. (2024) · Immunity · doi:10.1016/j.immuni.2024.05.006 · Cited by 24
Dynamic landscape of alternative polyadenylation during retinal development
Hu, W., Li, S., Park, J. Y., Boppana, S., Ni, T., Li, M., Zhu, J., Tian, B., Xie, Z., & Xiang, M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2429-1 · Cited by 23
Combinatory RNA-Sequencing Analyses Reveal a Dual Mode of Gene Regulation by ADAR1 in Gastric Cancer
Cho, C. J., Jung, J., Jiang, L., Lee, E. J., Kim, D., Kim, B. S., Kim, H. S., Jung, H., Song, H.-J., Hwang, S. W., et al. (2018) · Digestive Diseases and Sciences · doi:10.1007/s10620-018-5081-9 · Cited by 22
Quantitative Proteomics Links the LRRC59 Interactome to mRNA Translation on the ER Membrane
Hannigan, M. M., Hoffman, A. M., Thompson, J. W., Zheng, T., & Nicchitta, C. V. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra120.002228 · Cited by 22
Bhadra, P., Schorr, S., Lerner, M., Nguyen, D., Dudek, J., Förster, F. G., Helms, V., Lang, S., & Zimmermann, R. (2021) · Molecules · doi:10.3390/molecules26123591 · Cited by 22
CRISPR-iPAS: a novel dCAS13-based method for alternative polyadenylation interference
Tian, S., Zhang, B., He, Y., Sun, Z., Li, J., Li, Y., Yi, H., Zhao, Y., Zou, X., Li, Y., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac108 · Cited by 21
Cacioppo, R., & Lindon, C. (2022) · Open Biology · doi:10.1098/rsob.220134 · Cited by 21
Mukherjee, S., Graber, J. H., & Moore, C. L. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1091403 · Cited by 21
Hu, Z., Li, M., Chen, Y., Chen, L., Han, Y., Chen, C., Lü, X., You, N., Lou, Y., Huang, Y., et al. (2024) · Science China Life Sciences · doi:10.1007/s11427-023-2495-x · Cited by 21
Regulators of alternative polyadenylation operate at the transition from mitosis to meiosis
Shan, L., Wu, C., Chen, D., Hou, L., Li, X., Wang, L., Chu, X., Hou, Y., & Wang, Z. (2017) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2016.12.007 · Cited by 21
Struebing, F. L., Wang, J., Li, Y., King, R., Mistretta, O. C., ENGLISH, A. W., & Geisert, E. E. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00354 · Cited by 21
Connections between 3′ end processing and DNA damage response: Ten years later
Murphy, M. R., & Kleiman, F. E. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1571 · Cited by 21
Gadd45α modulates aversive learning through post‐transcriptional regulation of memory‐related mRNAs
Rey, A. A., Karaulanov, E., Sharopov, S., Arab, K., Schäfer, A., Gierl, M. S., Guggenhuber, S., Brandes, C., Pennella, L., Gruhn, W. H., et al. (2019) · EMBO Reports · doi:10.15252/embr.201846022 · Cited by 20
Molecular Insights into mRNA Polyadenylation and Deadenylation
Liu, J., Lu, X., Zhang, S., Yuan, L., & Sun, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231910985 · Cited by 20
Castillo-Guzman, D., Hartono, S. R., Frederick, M. H., Sanz, L. A., Sereiva, T., & Chedin, F. L. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.08.130583 · Cited by 25
Cell surface RNA biology: new roles for RNA binding proteins
Porat, J., & Flynn, R. A. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.03.005 · Cited by 19
Novel immunotherapy for gastric cancer: targeting the CD47–SIRPα axis
Ooki, A., Osumi, H., Shimozaki, K., & Yamaguchi, K. (2025) · Cancer and Metastasis Reviews · doi:10.1007/s10555-025-10269-z · Cited by 19
Metadata
- Authors
- Berkovits, B. D., & Mayr, C.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Corresponding author
- Mayr, Christine
- ORCID
- Mayr, Christine
- Venue
- Nature
- Published
- 2015-04-20
- Volume
- 522
- Issue
- 7556
- Pages
- 363-367
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC4697748
- OpenAlex
- W1969412365
- Cited by
- 474
- References
- 39
- Citations by year
- 2026: 26 · 2025: 40 · 2024: 39 · 2023: 42 · 2022: 38 · 2021: 75 · 2020: 47 · 2019: 50 · 2018: 38 · 2017: 38 · 2016: 28 · 2015: 11
- FWCI
- 16.54
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Damon Runyon Cancer Research Foundation (DRR-24-13)
- National Cancer Institute (U01CA164190, P30CA008748)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- 3' untranslated region, CD47, membrane protein localization, HuR, Rac1, post-translational translocation, endoplasmic reticulum, cell surface expression, mRNA isoforms, alternative splicing, phagocytosis resistance, RNA-binding proteins, translational regulation, protein scaffolds
- MeSH terms
- ELAV-Like Protein 1, Cell Line, Cell Membrane, DNA-Binding Proteins, Endoplasmic Reticulum, Humans, Membrane Proteins, RNA, Messenger, Transcription Factors, Genes, Reporter, 3' Untranslated Regions, rac1 GTP-Binding Protein, Protein Transport, Polyadenylation, CD47 Antigen, ELAV Proteins, Histone Chaperones, RNA Isoforms
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review