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Translating the Genome in Time and Space: Specialized Ribosomes, RNA Regulons, and RNA-Binding Proteins
Abstract
A central question in cell and developmental biology is how the information encoded in the genome is differentially interpreted to generate a diverse array of cell types. A growing body of research on posttranscriptional gene regulation is revealing that both global protein synthesis rates and the translation of specific mRNAs are highly specialized in different cell types. How this exquisite translational regulation is achieved is the focus of this review. Two levels of regulation are discussed: the translation machinery and cis-acting elements within mRNAs. Recent evidence shows that the ribosome itself directs how the genome is translated in time and space and reveals surprising functional specificity in individual components of the core translation machinery. We are also just beginning to appreciate the rich regulatory information embedded in the untranslated regions of mRNAs, which direct the selective translation of transcripts. These hidden RNA regulons may interface with a myriad of RNA-binding proteins and specialized translation machinery to provide an additional layer of regulation to how transcripts are spatiotemporally expressed. Understanding this largely unexplored world of translational codes hardwired in the core translation machinery is an exciting new research frontier fundamental to our understanding of gene regulation, organismal development, and evolution.
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“This is characterized by the striated muscle-specific paralog RPL3L, which is prevalent in resting tissue. Following hypertrophic overload, RPL3L expression plummets and is replaced by the ubiquitous isoform RPL3.”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [187]
In the citing paper
“Rather than altering mRNA selectivity for contractile proteins, this paralog switch enables the RPL3-containing ribosomes to physically anchor to mitochondria, maximizing the local ATP supply required to sustain the massive energetic cost of hypertrophy [187,189].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [187]
In the citing paper
“More recent work, however, has proposed that variation in ribosomal protein composition and rRNA modification patterns may generate ribosome populations with distinct translational preferences [186,187].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [187]
Citations
Cites
An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs
Kozak, M. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.20.8125 · Cited by 5,090
Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets
Sonenberg, N., & Hinnebusch, A. G. (2009) · Cell · doi:10.1016/j.cell.2009.01.042 · Cited by 3,304
Direct analysis of protein complexes using mass spectrometry
Link, A. J., Eng, J. K., Schieltz, D. M., Carmack, E., Mize, G. J., Morris, D. R., Garvik, B. M., & Yates, J. R. (1999) · Nature Biotechnology · doi:10.1038/10890 · Cited by 2,218
Ingolia, N. T., Lareau, L. F., & Weissman, J. S. (2011) · Cell · doi:10.1016/j.cell.2011.10.002 · Cited by 2,187
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132
FMRP Stalls Ribosomal Translocation on mRNAs Linked to Synaptic Function and Autism
Darnell, J. C., Van Driesche, S. J., Zhang, C., Hung, K. Y. S., Mele, A., Fraser, C. E., Stone, E. F., Chen, C., Fak, J. J., Chi, S. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.013 · Cited by 2,072
Pelletier, J., & Sonenberg, N. (1988) · Nature · doi:10.1038/334320a0 · Cited by 1,953
The Cell as a Collection of Protein Machines: Preparing the Next Generation of Molecular Biologists
Alberts, B. (1998) · Cell · doi:10.1016/s0092-8674(00)80922-8 · Cited by 1,411
Translational control in stress and apoptosis
Holčı́k, M., & Sonenberg, N. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1618 · Cited by 1,409
CCAAT/enhancer-binding proteins: structure, function and regulation
Ramji, D. P., & Foka, P. (2002) · Biochemical Journal · doi:10.1042/bj20020508 · Cited by 1,404
Jang, S. K., Kräusslich, H., Nicklin, M. J. H., Duke, G. M., Palmenberg, A. C., & Wimmer, E. (1988) · Journal of Virology · doi:10.1128/jvi.62.8.2636-2643.1988 · Cited by 1,390
The translational landscape of mTOR signalling steers cancer initiation and metastasis
Hsieh, A. C., Liu, Y., Edlind, M. P., Ingolia, N. T., Janes, M. R., Sher, A., Shi, E. Y., Stumpf, C. R., Christensen, C., Bonham, M. J., et al. (2012) · Nature · doi:10.1038/nature10912 · Cited by 1,313
Brown, V., Jin, P., Ceman, S., Darnell, J. C., O'Donnell, W. T., Tenenbaum, S. A., Jin, X., Feng, Y., Wilkinson, K. D., Keene, J. D., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00568-2 · Cited by 1,109
A SMALL PARTICULATE COMPONENT OF THE CYTOPLASM
Palade, G. E. (1955) · The Journal of Cell Biology · doi:10.1083/jcb.1.1.59 · Cited by 1,014
Garlick, P. J., McNurlan, M. A., & Preedy, V. R. (1980) · Biochemical Journal · doi:10.1042/bj1920719 · Cited by 974
Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
Darnell, J. C., Jensen, K. B., Jin, P., Brown, V., Warren, S. T., & Darnell, R. B. (2001) · Cell · doi:10.1016/s0092-8674(01)00566-9 · Cited by 952
Dendritic Protein Synthesis, Synaptic Plasticity, and Memory
Sutton, M. A., & Schuman, E. M. (2006) · Cell · doi:10.1016/j.cell.2006.09.014 · Cited by 938
Calvo, S. E., Pagliarini, D. J., & Mootha, V. K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810916106 · Cited by 914
Genome-wide probing of RNA structure reveals active unfolding of mRNA structures in vivo
Rouskin, S., Zubradt, M., Stefan Washietl, A., Kellis, M., & Weissman, J. S. (2013) · Nature · doi:10.1038/nature12894 · Cited by 862
Wilkinson, K. A., Merino, E. J., & Weeks, K. M. (2006) · Nature Protocols · doi:10.1038/nprot.2006.249 · Cited by 775
In vivo genome-wide profiling of RNA secondary structure reveals novel regulatory features
Ding, Y., Tang, Y., Kwok, C. K., Zhang, Y., Bevilacqua, P. C., & Assmann, S. M. (2014) · Nature · doi:10.1038/nature12756 · Cited by 775
Structural imprints in vivo decode RNA regulatory mechanisms
Spitale, R. C., Flynn, R. A., Zhang, Q. C., Crisalli, P., Lee, B., Jung, J., Kuchelmeister, H. Y., Batista, P. J., Torre, E. A., Kool, E. T., et al. (2015) · Nature · doi:10.1038/nature14263 · Cited by 760
Upstream Open Reading Frames as Regulators of mRNA Translation
Morris, D. R., & Geballe, A. P. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.23.8635-8642.2000 · Cited by 736
How Common Are Extraribosomal Functions of Ribosomal Proteins?
Warner, J. R., & McIntosh, K. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.03.006 · Cited by 735
Specialized ribosomes: a new frontier in gene regulation and organismal biology
Xue, S., & Barna, M. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3359 · Cited by 730
Self-citationUnusual Resistance of Peptidyl Transferase to Protein Extraction Procedures
Noller, H. F., Hoffarth, V., & Zimniak, L. (1992) · Science · doi:10.1126/science.1604315 · Cited by 728
Haematopoietic stem cells require a highly regulated protein synthesis rate
Signer, R. A. J., Magee, J. A., Salic, A., & Morrison, S. J. (2014) · Nature · doi:10.1038/nature13035 · Cited by 674
Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasisPreprint
Ruvinsky, I., Sharon, N., Lerer, T., Cohen, H., Stolovich-Rain, M., Nir, T., Dor, Y., Zisman, P., & Meyuhas, O. (2005) · Genes & Development · doi:10.1101/gad.351605 · Cited by 668
Ribosome-Mediated Specificity in Hox mRNA Translation and Vertebrate Tissue Patterning
Kondrashov, N., Pusic, A. D., Stumpf, C. R., Shimizu, K., Hsieh, A. C., Xue, S., Ishijima, J., Shiroishi, T., & Barna, M. (2011) · Cell · doi:10.1016/j.cell.2011.03.028 · Cited by 619
Self-citationHigh-Resolution View of the Yeast Meiotic Program Revealed by Ribosome Profiling
Brar, G. A., Yassour, M., Friedman, N., Regev, A., Ingolia, N. T., & Weissman, J. S. (2012) · Science · doi:10.1126/science.1215110 · Cited by 533
Gene Expression Regulation by Upstream Open Reading Frames and Human Disease
Barbosa, C., Peixeiro, I., & Romão, L. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003529 · Cited by 525
The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif
Schaeffer, C., Bardoni, B., Mandel, J., Ehresmann, B., Ehresmann, C., & Moine, H. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.4803 · Cited by 471
Cellular IRES-mediated translation
Komar, A. A., & Hatzoglou, M. (2011) · Cell Cycle · doi:10.4161/cc.10.2.14472 · Cited by 455
Keersmaecker, K. D., Atak, Z. K., Li, N., Vicente, C., Patchett, S., Girardi, T., Gianfelici, V., Geerdens, E., Clappier, E., Porcu, M., et al. (2012) · Nature Genetics · doi:10.1038/ng.2508 · Cited by 445
Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin
Liu, J., Xu, Y., Stoleru, D., & Salic, A. N. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111561108 · Cited by 440
Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly
Ceci, M., Gaviraghi, C., Gorrini, C., Sala, L. A., Offenhäuser, N., Marchisio, P. C., & Biffo, S. (2003) · Nature · doi:10.1038/nature02160 · Cited by 437
Many Ribosomal Protein Genes Are Cancer Genes in Zebrafish
Amsterdam, A., Sadler, K. C., Lai, K., Farrington, S. M., Bronson, R. T., Lees, J. A., & Hopkins, N. H. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020139 · Cited by 427
Impaired Control of IRES-Mediated Translation in X-Linked Dyskeratosis Congenita
Yoon, A., Peng, G., Brandenburg, Y., Zollo, O., Xu, W. G., Rego, E. M., & Ruggero, D. (2006) · Science · doi:10.1126/science.1123835 · Cited by 423
Translational control of C/EBP alpha and C/EBP beta isoform expressionPreprint
Calkhoven, C. F., Mueller, C. G., & Leutz, A. (2000) · University of Groningen research database (University of Groningen / Centre for Information Technology) · doi:10.1101/gad.14.15.1920 · Cited by 399
Inactivation of Conserved C. elegans Genes Engages Pathogen- and Xenobiotic-Associated Defenses
Melo, J. A., & Ruvkun, G. (2012) · Cell · doi:10.1016/j.cell.2012.02.050 · Cited by 398
The ribosomal protein genes and Minute loci of Drosophila melanogaster
Marygold, S. J., Roote, J., Reuter, G., Lambertsson, A., Ashburner, M., Millburn, G. H., Harrison, P. M., Yu, Z., Kenmochi, N., Kaufman, T. C., et al. (2007) · Genome Biology · doi:10.1186/gb-2007-8-10-r216 · Cited by 385
Differential Requirements for eIF4E Dose in Normal Development and Cancer
Truitt, M., Conn, C. S., Shi, Z., Pang, X., Tokuyasu, T. A., Coady, A. M., Seo, Y., Barna, M., & Ruggero, D. (2015) · Cell · doi:10.1016/j.cell.2015.05.049 · Cited by 383
Self-citationCell Cycle–Regulated Modification of the Ribosome by a Variant Multiubiquitin Chain
Spence, J. L., Gali, R. R., Dittmar, G., Sherman, F., Karin, M., & Finley, D. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00011-8 · Cited by 382
Proliferation, But Not Growth, Blocked by Conditional Deletion of 40 S Ribosomal Protein S6
Volarević, S., Stewart, M. J., Ledermann, B., Zilbermann, F., Terracciano, L., Montini, E., Grompe, M., Kozma, S. C., & Thomas, G. (2000) · Science · doi:10.1126/science.288.5473.2045 · Cited by 372
Ribosomal mutations cause p53-mediated dark skin and pleiotropic effects
McGowan, K. A., Li, J. Z., Park, C. Y., Beaudry, V. G., Tabor, H. K., Sabnis, A. J., Zhang, W., Fuchs, H., de Angelis, M. H., Myers, R., et al. (2008) · Nature Genetics · doi:10.1038/ng.188 · Cited by 363
Gradi, A., Svitkin, Y. V., Imataka, H., & Sonenberg, N. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.19.11089 · Cited by 358
A p53-dependent mechanism underlies macrocytic anemia in a mouse model of human 5q– syndrome
Barlow, J. L., Drynan, L. F., Hewett, D. R., Holmes, L. R., Lorenzo-Abalde, S., Lane, A. L., Jolin, H. E., Pannell, R., Middleton, A. J., Wong, S. H., et al. (2009) · Nature Medicine · doi:10.1038/nm.2063 · Cited by 349
Rack1, a Receptor for Activated Protein Kinase C, Interacts with Integrin β Subunit
Liliental, J., & Chang, D. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.2379 · Cited by 346
Mazumder, B., Sampath, P., Seshadri, V., Maitra, R. K., DiCorleto, P. E., & Fox, P. L. (2003) · Cell · doi:10.1016/s0092-8674(03)00773-6 · Cited by 344
Levy, S., Avni, D., Hariharan, N., Perry, R. P., & Meyuhas, O. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3319 · Cited by 344
Neuronal Transcriptome of Aplysia: Neuronal Compartments and Circuitry
Moroz, L. L., Edwards, J. R., Puthanveettil, S. V., Kohn, A. B., Ha, T. J., Heyland, A., Knudsen, B., Sahni, A., Yu, F., Liu, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.052 · Cited by 330
ELAV/Hu proteins inhibit p27 translation via an IRES element in the p27 5′UTR
Kullmann, M., Göpfert, U., Siewe, B., & Hengst, L. (2002) · Genes & Development · doi:10.1101/gad.248902 · Cited by 327
Identification and Characterization of a Novel Cell Cycle–Regulated Internal Ribosome Entry Site
Cornelis, S., Bruynooghe, Y., Denecker, G., Huffel, S. V., Tinton, S. A., & Beyaert, R. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80239-7 · Cited by 326
Structurally Distinct, Stage-Specific Ribosomes Occur in Plasmodium
Gunderson, J. H., Sogin, M. L., Woollett, G. R., Hollingdale, M. R., de la Cruz, V. F., Waters, A. P., & McCutchan, T. F. (1987) · Science · doi:10.1126/science.3672135 · Cited by 325
RNA regulons in Hox 5′ UTRs confer ribosome specificity to gene regulation
Xue, S., Tian, S., Fujii, K., Kladwang, W., Das, R., & Barna, M. (2014) · Nature · doi:10.1038/nature14010 · Cited by 319
Self-citationFleischer, T. C., Weaver, C. M., McAfee, K. J., Jennings, J. L., & Link, A. J. (2006) · Genes & Development · doi:10.1101/gad.1422006 · Cited by 308
A new internal-ribosome-entry-site motif potentiates XIAP- mediated cytoprotection
Holčı́k, M., Lefebvre, C. A., Yeh, C., Chow, T. Y.-K., & Korneluk, R. G. (1999) · Nature Cell Biology · doi:10.1038/11109 · Cited by 302
Sampath, P., Pritchard, D. K., Pabon, L., Reinecke, H., Schwartz, S. M., Morris, D. R., & Murry, C. E. (2008) · Cell Stem Cell · doi:10.1016/j.stem.2008.03.013 · Cited by 277
Viral IRES RNA structures and ribosome interactions.
Kieft, J. (2008) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2008.04.007 · Cited by 272
Ribosomal Protein s15 Phosphorylation Mediates LRRK2 Neurodegeneration in Parkinson’s Disease
Martin, I., Kim, J. W., Lee, B. D., Kang, H. C., Xu, J.-C., Jia, H., Stankowski, J., Kim, M.-S., Zhong, J., Kumar, M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.064 · Cited by 265
Fragile X Mental Retardation Protein Regulates Translation by Binding Directly to the Ribosome
Chen, E., Sharma, M. R., Shi, X., Agrawal, R. K., & Joseph, S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.023 · Cited by 253
Transmembrane Receptor DCC Associates with Protein Synthesis Machinery and Regulates Translation
Tcherkezian, J., Brittis, P. A., Thomas, F., Roux, P. P., & Flanagan, J. G. (2010) · Cell · doi:10.1016/j.cell.2010.04.008 · Cited by 248
uAUG and uORFs in human and rodent 5′untranslated mRNAs
Iacono, M., Mignone, F., & Pesole, G. (2005) · Gene · doi:10.1016/j.gene.2004.11.041 · Cited by 244
Gingras, A., Svitkin, Y. V., Belsham, G. J., Pause, A., & Sonenberg, N. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5578 · Cited by 238
The ribosomal basis of diamond-blackfan anemia: mutation and database update
Boria, I., Garelli, E., Gazda, H. T., Aspesi, A., Quarello, P., Pavesi, E., Ferrante, D., Meerpohl, J. J., Kartal, M., Da Costa, L., et al. (2010) · Human Mutation · doi:10.1002/humu.21383 · Cited by 233
3 The Minute Genes in Drosophila and Their Molecular Functions
Lambertsson, A. (1998) · Advances in genetics · doi:10.1016/s0065-2660(08)60142-x · Cited by 231
Cellular Differences in Protein Synthesis Regulate Tissue Homeostasis
Buszczak, M., Signer, R. A. J., & Morrison, S. J. (2014) · Cell · doi:10.1016/j.cell.2014.09.016 · Cited by 224
LIN28A Is a Suppressor of ER-Associated Translation in Embryonic Stem Cells
Cho, J., Chang, H., Kwon, S. C., Kim, B., Kim, Y., Choe, J., Ha, M., Kim, Y. K., & Kim, V. N. (2012) · Cell · doi:10.1016/j.cell.2012.10.019 · Cited by 223
Two internal ribosome entry sites mediate the translation of p53 isoforms
Ray, P. S., Grover, R., & Das, S. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400623 · Cited by 207
Ribosomal Protein SA Haploinsufficiency in Humans with Isolated Congenital Asplenia
Bolze, A., Mahlaoui, N., Byun, M., Turner, B., Trede, N. S., Ellis, S. R., Abhyankar, A., Itan, Y., Patin, É., Brebner, S., et al. (2013) · Science · doi:10.1126/science.1234864 · Cited by 199
RACK1 Controls IRES-Mediated Translation of Viruses
Majzoub, K., Hafirassou, M. L., Meignin, C., Goto, A., Marzi, S., Fedorova, A. A., Verdier, Y., Vinh, J., Hoffmann, J. A., Martin, F., et al. (2014) · Cell · doi:10.1016/j.cell.2014.10.041 · Cited by 195
Changes in rRNA transcription influence proliferation and cell fate within a stem cell lineage
Zhang, Q., Shalaby, N. A., & Buszczak, M. (2014) · Science · doi:10.1126/science.1246384 · Cited by 192
Identification of the 40 S ribosomal protein S6 phosphorylation sites induced by cycloheximide.
Krieg, J., Hofsteenge, J., & Thomas, G. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37981-x · Cited by 190
Bellodi, C., Kopmar, N. E., & Ruggero, D. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.83 · Cited by 177
Anderson, S. J., Lauritsen, J. P. H., Hartman, M. G., Foushee, A. M. D., Lefebvre, J. M., Shinton, S. A., Gerhardt, B., Hardy, R. R., Oravecz, T., & Wiest, D. L. (2007) · Immunity · doi:10.1016/j.immuni.2007.04.012 · Cited by 173
Lee, A. S.-Y., Burdeinick-Kerr, R., & Whelan, S. P. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216454109 · Cited by 169
Watson, K. L., Konrad, K. D., Woods, D. F., & Bryant, P. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.23.11302 · Cited by 165
p53 represses ribosomal gene transcription
Budde, A., & Grummt, I. (1999) · Oncogene · doi:10.1038/sj.onc.1202402 · Cited by 157
Direct Link between RACK1 Function and Localization at the Ribosome In Vivo
Coyle, S. M., Gilbert, W. V., & Doudna, J. A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01718-08 · Cited by 157
Degenhardt, R. F., & Bonham‐Smith, P. C. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.107.111799 · Cited by 156
Bellodi, C., McMahon, M. E., Contreras, A., Juliano, D., Kopmar, N. E., Nakamura, T., Maltby, D. A., Burlingame, A. L., Savage, S. A., Shimamura, A., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.04.030 · Cited by 154
Ribosomal proteins of Escherichia coli II. Proteins from the 30 s subunit
Moore, P. B., Traut, R. R., Noller, H. F., Pearson, P., & Delius, H. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90420-8 · Cited by 145
Stoichiometric measurements of 30S and 50S ribosomal proteins from Escherichia coli
Weber, H. (1972) · Molecular and General Genetics MGG · doi:10.1007/bf00333861 · Cited by 144
Introns within Ribosomal Protein Genes Regulate the Production and Function of Yeast Ribosomes
Parenteau, J., Durand, M., Morin, G., Gagnon, J., Lucier, J., Wellinger, R. J., Chabot, B., & Elela, S. A. (2011) · Cell · doi:10.1016/j.cell.2011.08.044 · Cited by 144
SYNTHESIS OF PROTEIN IN THE PANCREAS
Allfrey, V. G., Daly, M. M., & Mirsky, A. E. (1953) · The Journal of General Physiology · doi:10.1085/jgp.37.2.157 · Cited by 142
Ferreyra, M. L. F., Pezza, A., Biarc, J., Burlingame, A. L., & Casati, P. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.157057 · Cited by 139
Importin 7 and Exportin 1 Link c-Myc and p53 to Regulation of Ribosomal Biogenesis
Golomb, L., Bublik, D. R., Wilder, S., Nevo, R., Kiss, V., Grabusic, K., Volarevic, S., & Oren, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.11.022 · Cited by 137
Panić, L., Tamarut, S., Sticker-Jantscheff, M., Barkić, M., Solter, D., Uzelac, M., Grabušić, K., & Volarević, S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00751-06 · Cited by 135
Yang, D.-Q., Halaby, M. J., & Zhang, Y. (2006) · Oncogene · doi:10.1038/sj.onc.1209483 · Cited by 134
Ribosomes and translation in plant developmental control
Horiguchi, G., Lijsebettens, M. V., Candela, H., Micol, J. L., & Tsukaya, H. (2012) · Plant Science · doi:10.1016/j.plantsci.2012.04.008 · Cited by 127
Zeidan, Q., Wang, Z., Maio, A. D., & Hart, G. W. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-11-0941 · Cited by 126
Ribosome heterogeneity: another level of complexity in bacterial translation regulation
Byrgazov, K., Vesper, O., & Moll, I. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.01.009 · Cited by 123
A two-dimensional mutate-and-map strategy for non-coding RNA structure
Kladwang, W., VanLang, C. C., Cordero, P., & Das, R. (2011) · Nature Chemistry · doi:10.1038/nchem.1176 · Cited by 121
Sonja, B. A. U. M., Bittins, M., Frey, S., & Seedorf, M. (2004) · Biochemical Journal · doi:10.1042/bj20031962 · Cited by 114
Ribosomal Protein Gene Knockdown Causes Developmental Defects in Zebrafish
Uechi, T., Nakajima, Y., Nakao, A., Torihara, H., Chakraborty, A., Inoue, K., & Kenmochi, N. (2006) · PLoS ONE · doi:10.1371/journal.pone.0000037 · Cited by 113
Kaberdina, A. C., Szaflarski, W., Nierhaus, K. H., & Moll, I. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.014 · Cited by 111
Mass spectrometric analysis of the human 40S ribosomal subunit: Native and HCV IRES‐bound complexes
Yu, Y., Ji, H., Doudna, J. A., & Leary, J. A. (2005) · Protein Science · doi:10.1110/ps.041293005 · Cited by 108
Mutations in the Drosophila Gene Encoding Ribosomal Protein S6 Cause Tissue Overgrowth
Stewart, M. J., & Denell, R. E. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2524-2535.1993 · Cited by 104
Control of Hematopoietic Stem Cell Emergence by Antagonistic Functions of Ribosomal Protein Paralogs
Zhang, Y., Duc, A. E., Rao, S., Sun, X., Bilbee, A. N., Rhodes, M. R., Li, Q., Kappes, D. J., Rhodes, J., & Wiest, D. L. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.01.018 · Cited by 101
Whittle, C. A., & Krochko, J. E. (2009) · The Plant Cell · doi:10.1105/tpc.109.068411 · Cited by 101
C/EBPβ ΔuORF mice—a genetic model for uORF-mediated translational control in mammalsPreprint
Wethmar, K., Bégay, V., Smink, J. J., Zaragoza, K., Wiesenthal, V., Dörken, B., Calkhoven, C. F., & Leutz, A. (2010) · Genes & Development · doi:10.1101/gad.557910 · Cited by 99
Ribosomal Proteins of E. coli: Stoichiometry and Implications for Ribosome StructurePreprint
Traut, R. R., Delius, H., Ahmad‐Zadeh, C., Bickle, T. A., Pearson, P., & Tissieres, A. (1969) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1969.034.01.007 · Cited by 96
Control of Cyclin-Dependent Kinase Inhibitor p27 Expression by Cap-Independent Translation
Miskimins, W. K., Wang, G., Hawkinson, M., & Miskimins, R. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.15.4960-4967.2001 · Cited by 95
Odintsova, T. I., Müller, E., Ivanov, A. V., Egorov, T. A., Bienert, R., Vladimirov, S. N., Kostka, S., Otto, A., Wittmann‐Liebold, B., & Karpova, G. G. (2003) · Journal of Protein Chemistry · doi:10.1023/a:1025068419698 · Cited by 93
Barkić, M., Crnomarković, S., Grabušić, K., Bogetić, I., Panić, L., Tamarut, S., Brdovčak, M. C., Jerić, I., Vidak, S., & Volarević, S. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01588-08 · Cited by 92
The ribosomal protein RACK1 is required for microRNA function in both C. elegans and humans
Jannot, G., Bajan, S., Giguère, N. J., Bouasker, S., Banville, I., Piquet, S., Hutvágner, G., & Simard, M. J. (2011) · EMBO Reports · doi:10.1038/embor.2011.66 · Cited by 89
Physical and Functional Heterogeneity of E. coli RibosomesPreprint
Kurland, C. G., Voynow, P., HARDY, S. J. S., Randall, L. L., & Lutter, L. C. (1969) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1969.034.01.006 · Cited by 86
Lopes, A. M., Miguel, R. N., Sargent, C. A., Ellis, P. J. I., Amorim, A., & Affara, N. A. (2010) · BMC Molecular Biology · doi:10.1186/1471-2199-11-33 · Cited by 83
Sugihara, Y., Honda, H., Iida, T., Morinaga, T., Hino, S., Okajima, T., Matsuda, T., & Nadano, D. (2010) · Journal of Proteome Research · doi:10.1021/pr9008964 · Cited by 83
Lai, K., Amsterdam, A., Farrington, S., Bronson, R. T., Hopkins, N., & Lees, J. A. (2009) · Developmental Dynamics · doi:10.1002/dvdy.21815 · Cited by 81
Inhibition of CCAAT/Enhancer-binding Protein α and β Translation by Upstream Open Reading Frames
Lincoln, A. J., Monczak, Y., Williams, S. C., & Johnson, P. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9552 · Cited by 81
Spatial mapping of the neurite and soma proteomes reveals a functional Cdc42/Rac regulatory network
Pertz, O. C., Wang, Y., Yang, F., Wang, W., Gay, L. J., Gristenko, M. A., Clauss, T. R., Anderson, D. J., Liu, T., Auberry, K. J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706545105 · Cited by 79
Global growth deficiencies in mice lacking the ribosomal protein HIP/RPL29
Kirn‐Safran, C. B., Oristian, D., Focht, R. J., Parker, S. G., Vivian, J. L., & Carson, D. D. (2006) · Developmental Dynamics · doi:10.1002/dvdy.21046 · Cited by 78
Volta, V., Beugnet, A., Gallo, S., Magri, L., Brina, D., Pesce, E., Calamita, P., Sanvito, F., & Biffo, S. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1215-y · Cited by 76
Marygold, S. J., Coelho, C. M. A., & Leevers, S. J. (2004) · Genetics · doi:10.1534/genetics.104.034124 · Cited by 75
Characterization and Analysis of the Composition and Dynamics of the Mammalian Riboproteome
Reschke, M., Clohessy, J. G., Seitzer, N., Goldstein, D. P., Breitkopf, S. B., Schmolze, D. B., Ala, U., Asara, J. M., Beck, A. H., & Pandolfi, P. P. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.014 · Cited by 69
Mutation in ribosomal protein L21 underlies hereditary hypotrichosis simplex
Zhou, C., Zang, D., Jin, Y., Wu, H., Liu, Z., Du, J., & Zhang, J. (2011) · Human Mutation · doi:10.1002/humu.21503 · Cited by 67
Heterogeneity of ribosomal populations in Escherichia coli cells grown in different media
Deusser, E. (1972) · Molecular and General Genetics MGG · doi:10.1007/bf00333862 · Cited by 63
Török, I., Herrmann, D., Kiss, I., Tick, G., Speer, G., Schmitt, R., & Mechler, B. M. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.2308 · Cited by 57
Watkins‐Chow, D. E., Cooke, J., Pidsley, R., Edwards, A., Slotkin, R., Leeds, K. E., Mullen, R., Baxter, L. L., Campbell, T. G., Salzer, M. C., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003094 · Cited by 57
Deusser, E., & Wittmann, H. G. (1972) · Nature · doi:10.1038/238269a0 · Cited by 54
RPLP1, a Crucial Ribosomal Protein for Embryonic Development of the Nervous System
Perucho, L., Artero‐Castro, A., Llobet, S. G., y Cajal, S. R., LLeonart, M. E., & Wang, Z. (2014) · PLoS ONE · doi:10.1371/journal.pone.0099956 · Cited by 50
The ribosome – a macromolecular machine par excellence
Frank, J. (2000) · Chemistry & Biology · doi:10.1016/s1074-5521(00)00127-7 · Cited by 42
Bickle, T. A., Howard, G. A., & Traut, R. R. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43745-9 · Cited by 36
Rpl27a mutation in the sooty foot ataxia mouse phenocopies high p53 mouse models
Terzian, T., Dumble, M. L., Arbab, F., Christina Thaller, B., Donehower, L. A., Lozano, G., Justice, M. J., Roop, D. R., & Box, N. F. (2011) · The Journal of Pathology · doi:10.1002/path.2891 · Cited by 29
Ghosh, A., Rideout, E. J., & Grewal, S. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004750 · Cited by 26
RAMAGOPAL, S. (1991) · Biochemistry and Cell Biology · doi:10.1139/o91-040 · Cited by 21
Variation of ribosomal proteins with bacterial growth rate
Milne, A., Mak, W., & Wong, J. T.-F. (1975) · Journal of Bacteriology · doi:10.1128/jb.122.1.89-92.1975 · Cited by 20
Research works printed but not linked: 2
- Bridges CB, 1923, The Third-Chromosome Group of Mutant Characters of
- 10.1128/MCB.13.4.2524 · DOI
Cited by
Sorted by citations
Ribosome biogenesis in cancer: new players and therapeutic avenues
Pelletier, J., Thomas, G., & Volarević, S. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.104 · Cited by 837
Sloan, K. E., Warda, A. S., Sharma, S., Entian, K.-D., Lafontaine, D. L. J., & Bohnsack, M. T. (2017) · RNA Biology · doi:10.1080/15476286.2016.1259781 · Cited by 707
Heterogeneous Ribosomes Preferentially Translate Distinct Subpools of mRNAs Genome-wide
Shi, Z., Fujii, K., Kovary, K. M., Genuth, N. R., Röst, H. L., Teruel, M. N., & Barna, M. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.021 · Cited by 671
Self-citationLocal translation in neurons: visualization and function
Holt, C., Martin, K. C., & Schuman, E. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0263-5 · Cited by 463
The discovery of ribosome heterogeneity and its implications for gene regulation and organismal life
Genuth, N. R., & Barna, M. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.018 · Cited by 511
Self-citation
Metadata
- Authors
- Shi, Z., & Barna, M.
- Affiliations
- Stanford University (US)
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2015-11-13
- Volume
- 31
- Issue
- 1
- Pages
- 31-54
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2132392209
- Cited by
- 205
- References
- 130
- Citations by year
- 2026: 6 · 2025: 20 · 2024: 16 · 2023: 17 · 2022: 14 · 2021: 21 · 2020: 24 · 2019: 22 · 2018: 31 · 2017: 17 · 2016: 14 · 2015: 2
- FWCI
- 2.07
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (DP2OD008509)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- translational regulation, post-transcriptional regulation, specialized ribosomes, RNA-binding proteins, cis-regulatory elements, mRNA untranslated regions, cell type-specific translation, spatiotemporal gene expression, cell differentiation
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Ribosomes, RNA, RNA, Messenger, Protein Biosynthesis, RNA-Binding Proteins, Genome, Regulon
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