PTPN14 regulates Roquin2 stability by tyrosine dephosphorylation

References

• Nguyen, L.K, Muñoz-García J, Maccario H, et al. Switches, excitable responses and oscillations in the Ring1B/Bmi1 ubiquitination system. PLoS Comput Biol. 2011;7:e1002317.
   PubMed Web of Science ®Google Scholar
• Moeller HB, Praetorius J, Rutzler MR, et al. Phosphorylation of aquaporin-2 regulates its endocytosis and protein-protein interactions. Proc Natl Acad Sci U S A. 2010;107:502–507.
   PubMed Web of Science ®Google Scholar
• Hunter T. The age of crosstalk: phosphorylation, ubiquitination, and beyond. Mol Cell. 2007;28:730–738.
   PubMed Web of Science ®Google Scholar
• Skaar JR, Pagan JK, Pagano M. Mechanisms and function of substrate recruitment by F-box proteins. Nat Rev Mol Cell Biol. 2013;14:369–381.
   PubMed Web of Science ®Google Scholar
• Bassermann F, Eichner R, Pagano M. The ubiquitin proteasome system - implications for cell cycle control and the targeted treatment of cancer. Biochim Biophys Acta. 2014;1843:446–453.
   PubMed Web of Science ®Google Scholar
• Hershko A, Ciechanover A. The ubiquitin system. Annu Rev Biochem. 1998;67:425–479.
   PubMed Web of Science ®Google Scholar
• Choi J, Lee K, Ingvarsdottir K, et al. Loss of KLHL6 promotes diffuse large B-cell lymphoma growth and survival by stabilizing the mRNA decay factor roquin2. Nat Cell Biol. 2018;20:586–596.
   PubMed Web of Science ®Google Scholar
• Morin, R.D., Mendez-Lago M, Mungall AJ, et al. Frequent mutation of histone-modifying genes in non-Hodgkin lymphoma. Nature. 2011;476(7360):298.
   PubMed Web of Science ®Google Scholar
• Lohr JG, Stojanov P, Lawrence MS, et al. Discovery and prioritization of somatic mutations in diffuse large B-cell lymphoma (DLBCL) by whole-exome sequencing. Proc Natl Acad Sci U S A. 2012;109:3879–3884.
   PubMed Web of Science ®Google Scholar
• Idoia GR, Kremer Hovinga JA, Terrell DR, et al. CREBBP loss cooperates with BCL2 over-expression to promote lymphoma in mice. Blood. 2016;128:2175–2178.
   PubMedGoogle Scholar
• Reddy, A., Zhang J, Davis NS, et al. Genetic and functional drivers of diffuse large B cell lymphoma. Cell. 2017;171:481–494. e415.
   PubMed Web of Science ®Google Scholar
• Vinuesa CG, Cook MC, Angelucci C, et al. A RING-type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity. Nature. 2005;435:452–458.
   PubMed Web of Science ®Google Scholar
• Leppek K, Schott J, Reitter S, et al. Roquin promotes constitutive mRNA decay via a conserved class of stem-loop recognition motifs. Cell. 2013;153:869–881.
   PubMed Web of Science ®Google Scholar
• Schlundt A, Heinz GA, Janowski R, et al. Structural basis for RNA recognition in roquin-mediated post-transcriptional gene regulation. Nat Struct Mol Biol. 2014;21:671–678.
   PubMed Web of Science ®Google Scholar
• Tan D, Zhou M, Kiledjian M, et al. The ROQ domain of Roquin recognizes mRNA constitutive-decay element and double-stranded RNA. Nat Struct Mol Biol. 2014;21:679–685.
   PubMed Web of Science ®Google Scholar
• Smith AL, Nukina N, Masuda N, et al. Pez: a novel human cDNA encoding protein tyrosine phosphatase- and ezrin-like domains. Biochem Biophys Res Commun. 1995;209:959–965.
   PubMed Web of Science ®Google Scholar
• Wadham C, Gamble JR, Vadas MA, et al. The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin. Mol Biol Cell. 2003;14:2520–2529.
   PubMed Web of Science ®Google Scholar
• Wadham C, Gamble JR, Vadas MA, et al. Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation. J Cell Sci. 2000;113(Pt 17):3117–3123.
   PubMed Web of Science ®Google Scholar
• Zhang P, Giannini C, Sarkaria JN, et al. Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14. Oncogene. 2013;32:2087–2095.
   PubMed Web of Science ®Google Scholar
• Sjoblom T, Jones S, Wood LD, et al. The consensus coding sequences of human breast and colorectal cancers. Science. 2006;314:268–274.
   PubMed Web of Science ®Google Scholar
• Wang, Z., Shen D, Parsons DW, et al. Mutational analysis of the tyrosine phosphatome in colorectal cancers. Science. 2004;304:1164–1166.
   PubMed Web of Science ®Google Scholar
• Wang W, Gagliardini V, Raissig MT, et al. PTPN14 is required for the density-dependent control of YAP1. Genes Dev. 2012;26:1959–1971.
   PubMed Web of Science ®Google Scholar
• Liu X, Giannini C, Sarkaria JN, et al. PTPN14 interacts with and negatively regulates the oncogenic function of YAP. Oncogene. 2013;32:1266–1273.
   PubMed Web of Science ®Google Scholar
• Belle L, Ali N, Lonic A, et al. The tyrosine phosphatase PTPN14 (Pez) inhibits metastasis by altering protein trafficking. Sci Signal. 2015;8:ra18.
   PubMed Web of Science ®Google Scholar
• Mello SS, Valente LJ, Raj N, et al. A p53 super-tumor suppressor reveals a tumor suppressive p53-Ptpn14-Yap axis in pancreatic cancer. Cancer Cell. 2017;32:460–473. e466.
   PubMed Web of Science ®Google Scholar
• Heffetz D, Bushkin I, Dror R, et al. The insulinomimetic agents H2O2 and vanadate stimulate protein tyrosine phosphorylation in intact cells. J Biol Chem. 1990;265:2896–2902.
   PubMed Web of Science ®Google Scholar
• Secrist JP, Burns LA, Karnitz L, et al. Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events. J Biol Chem. 1993;268:5886–5893.
   PubMed Web of Science ®Google Scholar
• Seet BT, Dikic I, Zhou -M-M, et al. Reading protein modifications with interaction domains. Nat Rev Mol Cell Biol. 2006;7:473–483.
   PubMed Web of Science ®Google Scholar
• Sgromo A, Raisch T, Bawankar P, et al. A CAF40-binding motif facilitates recruitment of the CCR4-NOT complex to mRNAs targeted by Drosophila Roquin. Nat Commun. 2017;8:14307.
   PubMed Web of Science ®Google Scholar
• Warner JR. The economics of ribosome biosynthesis in yeast. Trends Biochem Sci. 1999;24:437–440.
   PubMed Web of Science ®Google Scholar
• Provost E, Weier CA, Leach SD. Multiple ribosomal proteins are expressed at high levels in developing zebrafish endoderm and are required for normal exocrine pancreas development. Zebrafish. 2013;10:161–169.
   PubMed Web of Science ®Google Scholar
• Pratama A, Ramiscal R, Silva D, et al. Roquin-2 shares functions with its paralog Roquin-1 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation. Immunity. 2013;38:669–680.
   PubMed Web of Science ®Google Scholar
• Ogata M, Takada T, Mori Y, et al. Effects of overexpression of PTP36, a putative protein tyrosine phosphatase, on cell adhesion, cell growth, and cytoskeletons in HeLa cells. J Biol Chem. 1999;274:12905–12909.
   PubMed Web of Science ®Google Scholar
• White EA, Munger K, Howley PM. High-risk human papillomavirus E7 proteins target PTPN14 for degradation. MBio. 2016;7.
   Web of Science ®Google Scholar
• Blanchetot C, Chagnon M, Dube N, et al. Substrate-trapping techniques in the identification of cellular PTP targets. Methods. 2005;35:44–53.
   PubMed Web of Science ®Google Scholar
• Satpathy S, Wagner SA, Beli P, et al. Systems-wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation. Mol Syst Biol. 2015;11:810.
   PubMed Web of Science ®Google Scholar
• Barretina J, Skaletsky H, Brown LG, et al. The cancer cell line encyclopedia enables predictive modelling of anticancer drug sensitivity. Nature. 2012;483:603–607.
   PubMed Web of Science ®Google Scholar
• Lenz G, Link E, Parish S, et al. Stromal gene signatures in large-B-cell lymphomas. N Engl J Med. 2008;359:2313–2323.
   PubMed Web of Science ®Google Scholar
• Kunder CA, Roncador G, Advani RH, et al. KLHL6 Is Preferentially Expressed in Germinal Center-Derived B-Cell Lymphomas. Am J Clin Pathol. 2017;148:465–476.
   PubMed Web of Science ®Google Scholar
• Meriranta L, Kremer Hovinga JA, Terrell DR, et al. Low expression and somatic mutations of the KLHL6 gene predict poor survival in patients with activated b-cell like diffuse large B-cell lymphoma. Blood. 2016;128:2175–2178.
   PubMed Web of Science ®Google Scholar
• Kuchay S, Duan S, Schenkein E, et al. FBXL2- and PTPL1-mediated degradation of p110-free p85beta regulatory subunit controls the PI(3)K signalling cascade. Nat Cell Biol. 2013;15:472–480.
   PubMed Web of Science ®Google Scholar
• Littlepage LE, Ruderman JV, Kato K, et al. Identification of a new APC/C recognition domain, the A box, which is required for the Cdh1-dependent destruction of the kinase Aurora-A during mitotic exit. Genes Dev. 2002;16:2274–2285.
   PubMed Web of Science ®Google Scholar
• Song L, Rape M, Vasta V, et al. Substrate-specific regulation of ubiquitination by the anaphase-promoting complex. Cell Cycle. 2011;10:52–56.
   PubMed Web of Science ®Google Scholar
• Gunawardana J, Harris SR, Croucher NJ, et al. Recurrent somatic mutations of PTPN1 in primary mediastinal B cell lymphoma and Hodgkin lymphoma. Nat Genet. 2014;46:329–335.
   PubMed Web of Science ®Google Scholar
• Ying J, Li H, Cui Y, et al. Epigenetic disruption of two proapoptotic genes MAPK10/JNK3 and PTPN13/FAP-1 in multiple lymphomas and carcinomas through hypermethylation of a common bidirectional promoter. Leukemia. 2006;20:1173–1175.
   PubMed Web of Science ®Google Scholar
• Ramiscal RR, Bowman CA, Russell DA, et al. Attenuation of AMPK signaling by ROQUIN promotes T follicular helper cell formation. Elife. 2015;4:e08698.
   PubMed Web of Science ®Google Scholar
• Maruyama T, Araki T, Kawarazaki Y, et al. Roquin-2 promotes ubiquitin-mediated degradation of ASK1 to regulate stress responses. Sci Signal. 2014;7:ra8.
   PubMed Web of Science ®Google Scholar
• Ying M, Shao X, Jing H, et al. Ubiquitin-dependent degradation of CDK2 drives the therapeutic differentiation of AML by targeting PRDX2. Blood. 2018;131:2698–2711.
   PubMed Web of Science ®Google Scholar
• Florens L, Washburn MP. Proteomic analysis by multidimensional protein identification technology. Methods Mol Biol. 2006;328:159–175.
   PubMedGoogle Scholar
• Washburn MP, Wolters D, Yates JR. 3rd Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol. 2001;19:242–247.
   PubMed Web of Science ®Google Scholar
• McDonald WH, Ohi R, Miyamoto DT, et al. Comparison of three directly coupled HPLC MS/MS strategies for identification of proteins from complex mixtures: single-dimension LC-MS/MS, 2-phase MudPIT, and 3-phase MudPIT. Int J Mass Spectrom. 2002;219:245–251.
   Web of Science ®Google Scholar
• Eng JK, McCormack AL, Yates JR. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom. 1994;5:976–989.
   PubMed Web of Science ®Google Scholar
• Tabb DL, McDonald WH, Yates JR. 3rd DTASelect and contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res. 2002;1:21–26.
   PubMed Web of Science ®Google Scholar
• Florens L, Carozza M, Swanson S, et al. Analyzing chromatin remodeling complexes using shotgun proteomics and normalized spectral abundance factors. Methods. 2006;40:303–311.
   PubMed Web of Science ®Google Scholar
• Paoletti AC, Parmely TJ, Tomomori-Sato C, et al. Quantitative proteomic analysis of distinct mammalian Mediator complexes using normalized spectral abundance factors. Proc Natl Acad Sci U S A. 2006;103:18928–18933.
   PubMed Web of Science ®Google Scholar
• Zybailov B, Mosley AL, Sardiu ME, et al. Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae. J Proteome Res. 2006;5:2339–2347.
   PubMed Web of Science ®Google Scholar