134. Holcik M, Gordon BW, Korneluk RG. The internal ribosome entry site-mediated translation of antiapoptotic protein XIAP is modulated by the heterogeneous nuclear ribonucleoproteins C1 and C2. *Mol Cell Biol* (2003) 23(1):280–8. doi:10.1128/MCB.23.1.280-288.2003

135. Schepens B, Tinton SA, Bruynooghe Y, Parthoens E, Haegman M, Beyaert R, et al. A role for hnRNP C1/C2 and Unr in internal initiation of translation during mitosis. *EMBO J* (2007) 26(1):158–69. doi:10.1038/sj.emboj.7601468

136. Lee EK, Kim HH, Kuwano Y, Abdelmohsen K, Srikantan S, Subaran SS, et al. hnRNP C promotes APP translation by competing with FMRP for APP mRNA recruitment to P bodies. *Nat Struct Mol Biol* (2010) 17(6):732–9. doi:10.1038/nsmb.1815

137. Beaudoin ME, Poirel VJ, Krushel LA. Regulating amyloid precursor protein synthesis through an internal ribosomal entry site. *Nucleic Acids Res* (2008) 36(21):e6835–47. doi:10.1093/nar/gkn792

138. Kim JH, Paek KY, Choi K, Kim TD, Hahm B, Kim KT, et al. Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner. *Mol Cell Biol* (2003) 23(2):708–20. doi:10.1128/MCB.23.2.708-720.2003

139. Fung PA, Labrecque R, Pederson T. RNA-dependent phosphorylation of a nuclear RNA binding protein. *Proc Natl Acad Sci U S A* (1997) 94(4):1064–8. doi:10.1073/pnas.94.4.1064

140. Phillips K, Kedersha N, Shen L, Blackshear PJ, Anderson P. Arthritis suppressor genes TIA-1 and TTP dampen the expression of tumor necrosis factor alpha, cyclooxygenase 2, and inflammatory arthritis. *Proc Natl Acad Sci U S A* (2004) 101(7):2011–6. doi:10.1073/pnas.0400148101

141. Dixon DA, Balch GC, Kedersha N, Anderson P, Zimmerman GA, Beauchamp RD, et al. Regulation of cyclooxygenase-2 expression by the translational silencer TIA-1. *J Exp Med* (2003) 198(3):475–81. doi:10.1084/jem.20030616

142. Kawai T, Lal A, Yang X, Galban S, Mazan-Mamczarz K, Gorospe M. Translational control of cytochrome c by RNA-binding proteins TIA-1 and HuR. *Mol Cell Biol* (2006) 26(8):3295–307. doi:10.1128/MCB.26.8.3295-3307.2006

143. Damgaard CK, Lykke-Andersen J. Translational coregulation of 5'TOP mRNAs by TIA-1 and TIAR. *Genes Dev* (2011) 25(19):2057–68. doi:10.1101/gad.17355911

144. Zhang T, Kruys V, Huez G, Gueydan C. AU-rich element-mediated translational control: complexity and multiple activities of trans-activating factors. *Biochem Soc Trans* (2002) 30(Pt 6):952–8. doi:10.1042/bst0300952

145. Wilkinson MF, Shyu AB. Multifunctional regulatory proteins that control gene expression in both the nucleus and the cytoplasm. *Bioessays* (2001) 23(9):775–87. doi:10.1002/bies.1113

146. Tian Q, Taupin J, Elledge S, Robertson M, Anderson P. Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis. *J Exp Med* (1995) 182(3):865–74. doi:10.1084/jem.182.3.865

147. Izquierdo JM, Valcarcel J. Fas-activated serine/threonine kinase (FAST K) synergizes with TIA-1/TIAR proteins to regulate Fas alternative splicing. *J Biol Chem* (2007) 282(3):1539–43. doi:10.1074/jbc.C600198200

148. Bachmann M, Pfeifer K, Schroder HC, Muller WE. Characterization of the autoantigen La as a nucleic acid-dependent ATPase/dATPase with melting properties. *Cell* (1990) 60(1):85–93. doi:10.1016/0092-8674(90)90718-T

149. Huhn P, Pruijn GJ, van Venrooij WJ, Bachmann M. Characterization of the autoantigen La (SS-B) as a dsRNA unwinding enzyme. *Nucleic Acids Res* (1997) 25(2):410–6. doi:10.1093/nar/25.2.410

150. Martino L, Pennell S, Kelly G, Bui TT, Kotik-Kogan O, Smerdon SJ, et al. Analysis of the interaction with the hepatitis C virus mRNA reveals an alternative mode of RNA recognition by the human La protein. *Nucleic Acids Res* (2012) 40(3):1381–94. doi:10.1093/nar/gkr890

151. Kuehnert J, Sommer G, Zierk AW, Fedarovich A, Brock A, Fedarovich D, et al. Novel RNA chaperone domain of RNA-binding protein La is regulated by AKT phosphorylation. *Nucleic Acids Res* (2015) 43(1):581–94. doi:10.1093/nar/gku1309

152. Svitkin YV, Meerovitch K, Lee HS, Dholakia JN, Kenan DJ, Agol VI, et al. Internal translation initiation on poliovirus RNA: further characterization of La function in poliovirus translation in vitro. *J Virol* (1994) 68(3):1544–50.

153. Svitkin YV, Pause A, Sonenberg N. La autoantigen alleviates translational repression by the 5' leader sequence of the human immunodeficiency virus type 1 mRNA. *J Virol* (1994) 68(11):7001–7.

154. Pudi R, Srinivasan P, Das S. La protein binding at the GCAC site near the initiator AUG facilitates the ribosomal assembly on the hepatitis C virus RNA to influence internal ribosome entry site-mediated translation. *J Biol Chem* (2004) 279(29):29879–88. doi:10.1074/jbc.M403417200

155. Schwartz EI, Intine RV, Maraia RJ. CK2 is responsible for phosphorylation of human La protein serine-366 and can modulate rpL37 5'-terminal oligopyrimidine mRNA metabolism. *Mol Cell Biol* (2004) 24(21):9580–91. doi:10.1128/MCB.24.21.9580-9591.2004

156. Brenet F, Socci ND, Sonenberg N, Holland EC. Akt phosphorylation of La regulates specific mRNA translation in glial progenitors. *Oncogene* (2009) 28(1):128–39. doi:10.1038/onc.2008.376

157. Intine RV, Dundr M, Vassilev A, Schwartz E, Zhao Y, Zhao Y, et al. Nonphosphorylated human La antigen interacts with nucleolin at nucleolar sites involved in rRNA biogenesis. *Mol Cell Biol* (2004) 24(24):10894–904. doi:10.1128/MCB.24.24.10894-10904.2004

158. Adachi T, Motojima S, Hirata A, Fukuda T, Makino S. Eosinophil viability-enhancing activity in sputum from patients with bronchial asthma. *Am J Respir Crit Care Med* (1995) 151:618–23. doi:10.1164/ajrccm.151.3_Pt_1.618

159. Corrigan CJ, Hamid Q, North J, Barkans J, Moqbel R, Durham S, et al. Peripheral blood CD4 but not CD8 T-lymphocytes in patients with exacerbation of asthma transcribe and translate messenger RNA encoding cytokines which prolong eosinophil survival in the context of a Th2-type pattern: effect of glucocorticoid therapy. *Am J Respir Cell Mol Biol* (1995) 12:567–78. doi:10.1165/ajrcmb.12.5.7742019

160. Schneider T, van Velzen D, Moqbel R, Issekutz AC. Kinetics and quantitation of eosinophil and neutrophil recruitment to allergic lung inflammation in a brown Norway rat model. *Am J Respir Cell Mol Biol* (1997) 17(6):702–12. doi:10.1165/ajrcmb.17.6.2849

161. Walker C, Bauer W, Braun RK, Menz G, Braun P, Schwarz F, et al. Activated T cells and cytokines in bronchoalveolar lavages from patients with various lung diseases associated with eosinophilia. *Am J Respir Crit Care Med* (1994) 150:1038–48. doi:10.1164/ajrccm.150.4.7921434

162. Shaver JR, Zangrilli JG, Cho SK, Cirelli RA, Pollice M, Hastie AT, et al. Kinetics of the development and recovery of the lung from IgE-mediated inflammation: dissociation of pulmonary eosinophilia, lung injury, and eosinophil-active cytokines. *Am J Respir Crit Care Med* (1997) 155(2):442–8. doi:10.1164/ajrccm.155.2.9032176

163. Yamashita N, Tashimo H, Ishida H, Kaneko F, Nakano J, Kato H, et al. Attenuation of airway hyperresponsiveness in a murine asthma model by neutralization of granulocyte-macrophage colony-stimulating factor (GM-CSF). *Cell Immunol* (2002) 219(2):92–7. doi:10.1016/S0008-8749(02)00565-8

164. Ohkawara Y, Lei XF, Stampfli MR, Marshall JS, Xing Z, Jordana M. Cytokine and eosinophil responses in the lung, peripheral blood, and bone marrow compartments in a murine model of allergen-induced airways inflammation. *Am J Respir Cell Mol Biol* (1997) 16:510–20. doi:10.1165/ajrcmb.16.5.9160833

165. Lei XF, Ohkawara Y, Stampfli MR, Gauldie J, Croitoru K, Jordana M, et al. Compartmentalized transgene expression of granulocyte-macrophage colony-stimulating factor (GM-CSF) in mouse lung enhances allergic airways inflammation. *Clin Exp Immunol* (1998) 113(2):157–65. doi:10.1046/j.1365-2249.1998.00652.x

166. Park CS, Choi YS, Ki SY, Moon SH, Jeong SW, Uh ST, et al. Granulocyte macrophage colony-stimulating factor is the main cytokine enhancing survival of eosinophils in asthmatic airways. *Eur Respir J* (1998) 12(4):872–8. doi:10.1183/09031936.98.12040872

167. Moqbel R, Hamid Q, Ying S, Barkans J, Hartnell A, Tsicopoulos A, et al. Expression of mRNA and immunoreactivity for the granulocyte/macrophage colony-stimulating factor in activated human eosinophils. *J Exp Med* (1991) 174(3):749–52. doi:10.1084/jem.174.3.749

168. Gauvreau GM, O'Byrne PM, Moqbel R, Velazquez J, Watson RM, Howie KJ, et al. Enhanced expression of GM-CSF in differentiating eosinophils of atopic and atopic asthmatic subjects. *Am J Respir Cell Mol Biol* (1998) 19(1):55–62. doi:10.1165/ajrcmb.19.1.2871

169. Ohkawara Y, Lim KG, Xing Z, Glibetic M, Nakano K, Dolovich J, et al. CD40 expression by human peripheral blood eosinophils. *J Clin Invest* (1996) 97(7):1761–6. doi:10.1172/JCI118603

170. Kim JT, Gleich GJ, Kita H. Roles of CD9 molecules in survival and activation of human eosinophils. *J Immunol* (1997) 159(2):926–33.
134. Holcik M, Gordon BW, Korneluk RG. The internal ribosome entry site-mediated translation of antiapoptotic protein XIAP is modulated by the heterogeneous nuclear ribonucleoproteins C1 and C2. *Mol Cell Biol* (2003) 23(1):280–8. doi:10.1128/MCB.23.1.280-288.2003

135. Schepens B, Tinton SA, Bruynooghe Y, Parthoens E, Haegman M, Beyaert R, et al. A role for hnRNP C1/C2 and Unr in internal initiation of translation during mitosis. *EMBO J* (2007) 26(1):158–69. doi:10.1038/sj.emboj.7601468

136. Lee EK, Kim HH, Kuwano Y, Abdelmohsen K, Srikantan S, Subaran SS, et al. hnRNP C promotes APP translation by competing with FMRP for APP mRNA recruitment to P bodies. *Nat Struct Mol Biol* (2010) 17(6):732–9. doi:10.1038/nsmb.1815

137. Beaudoin ME, Poirel VJ, Krushel LA. Regulating amyloid precursor protein synthesis through an internal ribosomal entry site. *Nucleic Acids Res* (2008) 36(21):e6835–47. doi:10.1093/nar/gkn792

138. Kim JH, Paek KY, Choi K, Kim TD, Hahm B, Kim KT, et al. Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner. *Mol Cell Biol* (2003) 23(2):708–20. doi:10.1128/MCB.23.2.708-720.2003

139. Fung PA, Labrecque R, Pederson T. RNA-dependent phosphorylation of a nuclear RNA binding protein. *Proc Natl Acad Sci U S A* (1997) 94(4):1064–8. doi:10.1073/pnas.94.4.1064

140. Phillips K, Kedersha N, Shen L, Blackshear PJ, Anderson P. Arthritis suppressor genes TIA-1 and TTP dampen the expression of tumor necrosis factor alpha, cyclooxygenase 2, and inflammatory arthritis. *Proc Natl Acad Sci U S A* (2004) 101(7):2011–6. doi:10.1073/pnas.0400148101

141. Dixon DA, Balch GC, Kedersha N, Anderson P, Zimmerman GA, Beauchamp RD, et al. Regulation of cyclooxygenase-2 expression by the translational silencer TIA-1. *J Exp Med* (2003) 198(3):475–81. doi:10.1084/jem.20030616

142. Kawai T, Lal A, Yang X, Galban S, Mazan-Mamczarz K, Gorospe M. Translational control of cytochrome c by RNA-binding proteins TIA-1 and HuR. *Mol Cell Biol* (2006) 26(8):3295–307. doi:10.1128/MCB.26.8.3295-3307.2006

143. Damgaard CK, Lykke-Andersen J. Translational coregulation of 5'TOP mRNAs by TIA-1 and TIAR. *Genes Dev* (2011) 25(19):2057–68. doi:10.1101/gad.17355911

144. Zhang T, Kruys V, Huez G, Gueydan C. AU-rich element-mediated translational control: complexity and multiple activities of trans-activating factors. *Biochem Soc Trans* (2002) 30(Pt 6):952–8. doi:10.1042/bst0300952

145. Wilkinson MF, Shyu AB. Multifunctional regulatory proteins that control gene expression in both the nucleus and the cytoplasm. *Bioessays* (2001) 23(9):775–87. doi:10.1002/bies.1113

146. Tian Q, Taupin J, Elledge S, Robertson M, Anderson P. Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis. *J Exp Med* (1995) 182(3):865–74. doi:10.1084/jem.182.3.865

147. Izquierdo JM, Valcarcel J. Fas-activated serine/threonine kinase (FAST K) synergizes with TIA-1/TIAR proteins to regulate Fas alternative splicing. *J Biol Chem* (2007) 282(3):1539–43. doi:10.1074/jbc.C600198200

148. Bachmann M, Pfeifer K, Schroder HC, Muller WE. Characterization of the autoantigen La as a nucleic acid-dependent ATPase/dATPase with melting properties. *Cell* (1990) 60(1):85–93. doi:10.1016/0092-8674(90)90718-T

149. Huhn P, Pruijn GJ, van Venrooij WJ, Bachmann M. Characterization of the autoantigen La (SS-B) as a dsRNA unwinding enzyme. *Nucleic Acids Res* (1997) 25(2):410–6. doi:10.1093/nar/25.2.410

150. Martino L, Pennell S, Kelly G, Bui TT, Kotik-Kogan O, Smerdon SJ, et al. Analysis of the interaction with the hepatitis C virus mRNA reveals an alternative mode of RNA recognition by the human La protein. *Nucleic Acids Res* (2012) 40(3):1381–94. doi:10.1093/nar/gkr890

151. Kuehnert J, Sommer G, Zierk AW, Fedarovich A, Brock A, Fedarovich D, et al. Novel RNA chaperone domain of RNA-binding protein La is regulated by AKT phosphorylation. *Nucleic Acids Res* (2015) 43(1):581–94. doi:10.1093/nar/gku1309

152. Svitkin YV, Meerovitch K, Lee HS, Dholakia JN, Kenan DJ, Agol VI, et al. Internal translation initiation on poliovirus RNA: further characterization of La function in poliovirus translation in vitro. *J Virol* (1994) 68(3):1544–50.

153. Svitkin YV, Pause A, Sonenberg N. La autoantigen alleviates translational repression by the 5' leader sequence of the human immunodeficiency virus type 1 mRNA. *J Virol* (1994) 68(11):7001–7.

154. Pudi R, Srinivasan P, Das S. La protein binding at the GCAC site near the initiator AUG facilitates the ribosomal assembly on the hepatitis C virus RNA to influence internal ribosome entry site-mediated translation. *J Biol Chem* (2004) 279(29):29879–88. doi:10.1074/jbc.M403417200

155. Schwartz EI, Intine RV, Maraia RJ. CK2 is responsible for phosphorylation of human La protein serine-366 and can modulate rpL37 5'-terminal oligopyrimidine mRNA metabolism. *Mol Cell Biol* (2004) 24(21):9580–91. doi:10.1128/MCB.24.21.9580-9591.2004

156. Brenet F, Socci ND, Sonenberg N, Holland EC. Akt phosphorylation of La regulates specific mRNA translation in glial progenitors. *Oncogene* (2009) 28(1):128–39. doi:10.1038/onc.2008.376

157. Intine RV, Dundr M, Vassilev A, Schwartz E, Zhao Y, Zhao Y, et al. Nonphosphorylated human La antigen interacts with nucleolin at nucleolar sites involved in rRNA biogenesis. *Mol Cell Biol* (2004) 24(24):10894–904. doi:10.1128/MCB.24.24.10894-10904.2004

158. Adachi T, Motojima S, Hirata A, Fukuda T, Makino S. Eosinophil viability-enhancing activity in sputum from patients with bronchial asthma. *Am J Respir Crit Care Med* (1995) 151:618–23. doi:10.1164/ajrccm.151.3_Pt_1.618

159. Corrigan CJ, Hamid Q, North J, Barkans J, Moqbel R, Durham S, et al. Peripheral blood CD4 but not CD8 T-lymphocytes in patients with exacerbation of asthma transcribe and translate messenger RNA encoding cytokines which prolong eosinophil survival in the context of a Th2-type pattern: effect of glucocorticoid therapy. *Am J Respir Cell Mol Biol* (1995) 12:567–78. doi:10.1165/ajrcmb.12.5.7742019

160. Schneider T, van Velzen D, Moqbel R, Issekutz AC. Kinetics and quantitation of eosinophil and neutrophil recruitment to allergic lung inflammation in a brown Norway rat model. *Am J Respir Cell Mol Biol* (1997) 17(6):702–12. doi:10.1165/ajrcmb.17.6.2849

161. Walker C, Bauer W, Braun RK, Menz G, Braun P, Schwarz F, et al. Activated T cells and cytokines in bronchoalveolar lavages from patients with various lung diseases associated with eosinophilia. *Am J Respir Crit Care Med* (1994) 150:1038–48. doi:10.1164/ajrccm.150.4.7921434

162. Shaver JR, Zangrilli JG, Cho SK, Cirelli RA, Pollice M, Hastie AT, et al. Kinetics of the development and recovery of the lung from IgE-mediated inflammation: dissociation of pulmonary eosinophilia, lung injury, and eosinophil-active cytokines. *Am J Respir Crit Care Med* (1997) 155(2):442–8. doi:10.1164/ajrccm.155.2.9032176

163. Yamashita N, Tashimo H, Ishida H, Kaneko F, Nakano J, Kato H, et al. Attenuation of airway hyperresponsiveness in a murine asthma model by neutralization of granulocyte-macrophage colony-stimulating factor (GM-CSF). *Cell Immunol* (2002) 219(2):92–7. doi:10.1016/S0008-8749(02)00565-8

164. Ohkawara Y, Lei XF, Stampfli MR, Marshall JS, Xing Z, Jordana M. Cytokine and eosinophil responses in the lung, peripheral blood, and bone marrow compartments in a murine model of allergen-induced airways inflammation. *Am J Respir Cell Mol Biol* (1997) 16:510–20. doi:10.1165/ajrcmb.16.5.9160833

165. Lei XF, Ohkawara Y, Stampfli MR, Gauldie J, Croitoru K, Jordana M, et al. Compartmentalized transgene expression of granulocyte-macrophage colony-stimulating factor (GM-CSF) in mouse lung enhances allergic airways inflammation. *Clin Exp Immunol* (1998) 113(2):157–65. doi:10.1046/j.1365-2249.1998.00652.x

166. Park CS, Choi YS, Ki SY, Moon SH, Jeong SW, Uh ST, et al. Granulocyte macrophage colony-stimulating factor is the main cytokine enhancing survival of eosinophils in asthmatic airways. *Eur Respir J* (1998) 12(4):872–8. doi:10.1183/09031936.98.12040872

167. Moqbel R, Hamid Q, Ying S, Barkans J, Hartnell A, Tsicopoulos A, et al. Expression of mRNA and immunoreactivity for the granulocyte/macrophage colony-stimulating factor in activated human eosinophils. *J Exp Med* (1991) 174(3):749–52. doi:10.1084/jem.174.3.749

168. Gauvreau GM, O'Byrne PM, Moqbel R, Velazquez J, Watson RM, Howie KJ, et al. Enhanced expression of GM-CSF in differentiating eosinophils of atopic and atopic asthmatic subjects. *Am J Respir Cell Mol Biol* (1998) 19(1):55–62. doi:10.1165/ajrcmb.19.1.2871

169. Ohkawara Y, Lim KG, Xing Z, Glibetic M, Nakano K, Dolovich J, et al. CD40 expression by human peripheral blood eosinophils. *J Clin Invest* (1996) 97(7):1761–6. doi:10.1172/JCI118603

170. Kim JT, Gleich GJ, Kita H. Roles of CD9 molecules in survival and activation of human eosinophils. *J Immunol* (1997) 159(2):926–33.
171. Levi-Schaffer F, Temkin V, Malamud V, Feld S, Zilberman Y. Mast cells enhance eosinophil survival in vitro: role of TNF-alpha and granulocyte-macrophage colony-stimulating factor. *J Immunol* (1998) 160(11):5554-62.

172. Esnault S, Malter JS. Granulocyte macrophage-colony-stimulating factor mRNA is stabilized in airway eosinophils and peripheral blood eosinophils activated by TNF-alpha plus fibronectin. *J Immunol* (2001) 166(7):4658-63. doi:10.4049/jimmunol.166.7.4658

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174. Hoontrakoon R, Chu HW, Gardai SJ, Wenzel SE, McDonald P, Fadok VA, et al. Interleukin-15 inhibits spontaneous apoptosis in human eosinophils via autocrine production of granulocyte macrophage-colony stimulating factor and nuclear factor-kappaB activation. *Am J Respir Cell Mol Biol* (2002) 26(4):404-12. doi:10.1165/ajrcmb.26.4.4517

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**Conflict of Interest Statement:** The authors declare no conflict of interest other than an issued patent on the use of Pin1 as a drug target to treat eosinophilia.

The reviewer KWG and the handling editor declared their shared affiliation, and the handling editor states that the process nevertheless met the standards of a fair and objective review.

Copyright © 2017 Esnault, Shen and Malter. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
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196. Liu LY, Sedgwick JB, Bates ME, Vrtis RF, Gern JE, Kita H, et al. Decreased expression of membrane IL-5R alpha on human eosinophils: II. IL-5 down-modulates its receptor via a proteinase-mediated process. *J Immunol* (2002) 169(11):6459-66. doi:10.4049/jimmunol.169.11.6459

197. Gregory B, Kirchem A, Phipps S, Gevaert P, Pridgeon C, Rankin SM, et al. Differential regulation of human eosinophil IL-3, IL-5, and GM-CSF receptor alpha-chain expression by cytokines: IL-3, IL-5, and GM-CSF down-regulate IL-5 receptor alpha expression with loss of IL-5 responsiveness, but up-regulate IL-3 receptor alpha expression. *J Immunol* (2003) 170(11):5359-66. doi:10.4049/jimmunol.170.11.5359

198. Johansson MW, Kelly EA, Busse WW, Jarjour NN, Mosher DF. Up-regulation and activation of eosinophil integrins in blood and airway after segmental lung antigen challenge. *J Immunol* (2008) 180(11):7622-35. doi:10.4049/jimmunol.180.11.7622

199. Chauvin C, Koka V, Nouschi A, Mieulet V, Hoareau-Aveilla C, Dreazen A, et al. Ribosomal protein S6 kinase activity controls the ribosome biogenesis transcriptional program. *Oncogene* (2014) 33(4):474-83. doi:10.1038/onc.2012.606

200. Sapkota GP, Cummings L, Newell FS, Armstrong C, Bain J, Frodin M, et al. BI-D1870 is a specific inhibitor of the p90 RSK (ribosomal S6 kinase) isoforms in vitro and in vivo. *Biochem J* (2007) 401(1):29-38. doi:10.1042/BJ20061088

201. Anjum R, Blenis J. The RSK family of kinases: emerging roles in cellular signalling. *Nat Rev Mol Cell Biol* (2008) 9(10):747-58. doi:10.1038/nrm2509

**Conflict of Interest Statement:** The authors declare no conflict of interest other than an issued patent on the use of Pin1 as a drug target to treat eosinophilia.

The reviewer KWG and the handling editor declared their shared affiliation, and the handling editor states that the process nevertheless met the standards of a fair and objective review.

Copyright © 2017 Esnault, Shen and Malter. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.