Arnon, T. I., Markel, G. & Mandelboim, O. Tumor and viral recognition by natural killer cells receptors. Semin. Cancer Biol. 16, 348–358 (2006).
Gasser, S., Orsulic, S., Brown, E. J. & Raulet, D. H. The DNA damage pathway regulates innate immune system ligands of the NKG2D receptor. Nature 436, 1186–1190 (2005).
Jost, S. & Altfeld, M. Control of human viral infections by natural killer cells. Annu. Rev. Immunol. 31, 163–194 (2013).
Moffett-King, A. Natural killer cells and pregnancy. Nat. Rev. Immunol. 2, 656–663 (2002).
Lanier, L. L. NK cell recognition. Annu. Rev. Immunol. 23, 225–274 (2005).
Long, E. O., Sik Kim, H., Liu, D., Peterson, M. E. & Rajagopalan, S. Controlling natural killer cell responses: integration of signals for activation and inhibition. Annu. Rev. Immunol. 31, 227–258 (2013).
Brodin, P., Lakshmikanth, T., Johansson, S., Karre, K. & Hoglund, P. The strength of inhibitory input during education quantitatively tunes the functional responsiveness of individual natural killer cells. Blood 113, 2434–2441 (2009).
Joncker, N. T., Fernandez, N. C., Treiner, E., Vivier, E. & Raulet, D. H. NK cell responsiveness is tuned commensurate with the number of inhibitory receptors for self-MHC class I: the rheostat model. J. Immunol. 182, 4572–4580 (2009).
Raulet, D. H. & Vance, R. E. Self-tolerance of natural killer cells. Nat. Rev. Immunol. 6, 520–531 (2006).
Raulet, D. H., Gasser, S., Gowen, B. G., Deng, W. & Jung, H. Regulation of ligands for the NKG2D activating receptor. Annu. Rev. Immunol. 31, 413–441 (2013).
Champsaur, M. & Lanier, L. L. Effect of NKG2D ligand expression on host immune responses. Immunol. Rev. 235, 267–285 (2010).
Groh, V. et al. Cell stress-regulated human major histocompatibility complex class I gene expressed in gastrointestinal epithelium. Proc. Natl Acad. Sci. USA 93, 12445–12450 (1996).
Groh, V. et al. Costimulation of CD8alphabeta T cells by NKG2D via engagement by MIC induced on virus-infected cells. Nat. Immunol. 2, 255–260 (2001).
Raulet, D. H. & Guerra, N. Oncogenic stress sensed by the immune system: role of natural killer cell receptors. Nat. Rev. Immunol. 9, 568–580 (2009).
Kasahara, M., Watanabe, Y., Sumasu, M. & Nagata, T. A family of MHC class I-like genes located in the vicinity of the mouse leukocyte receptor complex. Proc. Natl Acad. Sci. USA 99, 13687–13692 (2002).
Kasahara, M. & Yoshida, S. Immunogenetics of the NKG2D ligand gene family. Immunogenetics 64, 855–867 (2012).
Venkataraman, G. M., Suciu, D., Groh, V., Boss, J. M. & Spies, T. Promoter region architecture and transcriptional regulation of the genes for the MHC class I-related chain A and B ligands of NKG2D. J. Immunol. 178, 961–969 (2007).
Stern-Ginossar, N. et al. Human microRNAs regulate stress-induced immune responses mediated by the receptor NKG2D. Nat. Immunol. 9, 1065–1073 (2008).
Nachmani, D., Lankry, D., Wolf, D. G. & Mandelboim, O. The human cytomegalovirus microRNA miR-UL112 acts synergistically with a cellular microRNA to escape immune elimination. Nat. Immunol. 11, 806–813 (2010).
Tsukerman, P. et al. MiR-10b downregulates the stress-induced cell surface molecule MICB, a critical ligand for cancer cell recognition by natural killer cells. Cancer Res. 72, 5463–5472 (2012).
Muller-McNicoll, M. & Neugebauer, K. M. How cells get the message: dynamic assembly and function of mRNA-protein complexes. Nat. Rev. Genet. 14, 275–287 (2013).
Glisovic, T., Bachorik, J. L., Yong, J. & Dreyfuss, G. RNA-binding proteins and post-transcriptional gene regulation. FEBS Lett. 582, 1977–1986 (2008).
Martin, K. C. & Ephrussi, A. mRNA localization: gene expression in the spatial dimension. Cell 136, 719–730 (2009).
Moore, M. J. & Proudfoot, N. J. Pre-mRNA processing reaches back to transcription and ahead to translation. Cell 136, 688–700 (2009).
Sonenberg, N. & Hinnebusch, A. G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136, 731–745 (2009).
Lukong, K. E., Chang, K. W., Khandjian, E. W. & Richard, S. RNA-binding proteins in human genetic disease. Trends Genet. 24, 416–425 (2008).
Hammerle, M. et al. Post-transcriptional destabilization of the liver-specific long non-coding RNA HULC by the IGF2 mRNA-binding protein 1 (IGF2BP1). Hepatology. 58, 1703–1712 (2013).
Dayton, A. I. Matrin 3 and HIV Rev regulation of mRNA. Retrovirology 8, 62 (2011).
Jones, K., Timchenko, L. & Timchenko, N. A. The role of CUGBP1 in age-dependent changes of liver functions. Ageing Res. Rev. 11, 442–449 (2012).
Kim, H. H. & Gorospe, M. GU-rich RNA: expanding CUGBP1 function, broadening mRNA turnover. Mol. Cell 29, 151–152 (2008).
Miki, T. S. & Grosshans, H. The multifunctional RNase XRN2. Biochem. Soc. Trans. 41, 825–830 (2013).
Srikantan, S. & Gorospe, M. HuR function in disease. Front Biosci. (Landmark Ed) 17, 189–205 (2012).
Weber, A. et al. The FUSE binding proteins FBP1 and FBP3 are potential c-myc regulators in renal, but not in prostate and bladder cancer. BMC Cancer 8, 369 (2008).
Peritz, T. et al. Immunoprecipitation of mRNA-protein complexes. Nat. Protoc. 1, 577–580 (2006).
Le, H. T., Sorrell, A. M. & Siddle, K. Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation. PloS ONE 7, e33140 (2012).
Moore, M. J. From birth to death: the complex lives of eukaryotic mRNAs. Science 309, 1514–1518 (2005).
Mukherjee, N. et al. Integrative regulatory mapping indicates that the RNA-binding protein HuR couples pre-mRNA processing and mRNA stability. Mol. Cell 43, 327–339 (2011).
Ray, D. et al. A compendium of RNA-binding motifs for decoding gene regulation. Nature 499, 172–177 (2013).
Edwards, J. et al. Sequence determinants for the tandem recognition of UGU and CUG rich RNA elements by the two N--terminal RRMs of CELF1. Nucleic Acids Res. 39, 8638–8650 (2011).
Hafner, M. et al. Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP. Cell 141, 129–141 (2010).
Tang, K. F. et al. Induction of MHC class I-related chain B (MICB) by 5-aza-2′-deoxycytidine. Biochem. Biophys. Res. Commun. 370, 578–583 (2008).
Kim, H. H., Abdelmohsen, K. & Gorospe, M. Regulation of HuR by DNA damage response kinases. J. Nucleic Acids 2010, 981487 (2010).
Matsuoka, S. et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science 316, 1160–1166 (2007).
Abdelmohsen, K. & Gorospe, M. Posttranscriptional regulation of cancer traits by HuR. Wiley Interdiscip. Rev. RNA 1, 214–229 (2010).
Lee, J. E. & Cooper, T. A. Pathogenic mechanisms of myotonic dystrophy. Biochem. Soc. Trans. 37, 1281–1286 (2009).
Schoser, B. & Timchenko, L. Myotonic dystrophies 1 and 2: complex diseases with complex mechanisms. Curr. Genomics 11, 77–90 (2010).
Christiansen, J., Kolte, A. M., Hansen, T. & Nielsen, F. C. IGF2 mRNA-binding protein 2: biological function and putative role in type 2 diabetes. J. Mol. Endocrinol. 43, 187–195 (2009).
Srikantan, S., Tominaga, K. & Gorospe, M. Functional interplay between RNA-binding protein HuR and microRNAs. Curr. Protein Pept. Sci. 13, 372–379 (2012).
Stern-Ginossar, N. et al. Host immune system gene targeting by a viral miRNA. Science 317, 376–381 (2007).
Nachmani, D., Stern-Ginossar, N., Sarid, R. & Mandelboim, O. Diverse herpesvirus microRNAs target the stress-induced immune ligand MICB to escape recognition by natural killer cells. Cell Host Microbe 5, 376–385 (2009).