FADD phosphorylation contributes to development of renal fibrosis by accelerating epithelial-mesenchymal transition

References

• Chinnaiyan AM, O’Rourke K, Tewari M, et al. FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis. Cell. 1995;81:505–512.
   PubMed Web of Science ®Google Scholar
• Zhang J, Winoto A. A mouse fas-associated protein with homology to the human mort1/FADD protein is essential for fas-induced apoptosis. Mol Cell Biol. 1996;16:2756–2763.
   PubMed Web of Science ®Google Scholar
• Lee EW, Seo J, Jeong M, et al. The roles of FADD in extrinsic apoptosis and necroptosis. BMB Rep. 2012;45:496–508.
   PubMed Web of Science ®Google Scholar
• Welz PS, Wullaert A, Vlantis K, et al. FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation. Nature. 2011;477:330–334. DOI:10.1038/nature10273.
   PubMed Web of Science ®Google Scholar
• Bonnet MC, Preukschat D, Welz PS, et al. The adaptor protein FADD protects epidermal keratinocytes from necroptosis in vivo and prevents skin inflammation. Immunity. 2011;35:572–582. DOI:10.1016/j.immuni.2011.08.014.
   PubMed Web of Science ®Google Scholar
• Pyo JO, Jang MH, Kwon YK, et al. Essential roles of Atg5 and FADD in autophagic cell death: dissection of autophagic cell death into vacuole formation and cell death. J Biol Chem. 2005;280:20722–20729. DOI:10.1074/jbc.M413934200.
   PubMed Web of Science ®Google Scholar
• He L, Ren Y, Zheng Q, et al. Fas-associated protein with death domain (FADD) regulates autophagy through promoting the expression of ras homolog enriched in brain (Rheb) in human breast adenocarcinoma cells. Oncotarget. 2016;7:24572–24584. DOI:10.18632/oncotarget.8249.
   PubMedGoogle Scholar
• Kabra NH, Kang C, Hsing LC, et al. T cell-specific FADD-deficient mice: fADD is required for early T cell development. Proc Natl Acad Sci U S A. 2001;98:6307–6312.
   PubMed Web of Science ®Google Scholar
• Hua ZC, Sohn SJ, Kang C, et al. A function of fas-associated death domain protein in cell cycle progression localized to a single amino acid at its C-terminal region. Immunity. 2003;18:513–521.
   PubMed Web of Science ®Google Scholar
• Matsuyoshi S, Shimada K, Nakamura M, et al. FADD phosphorylation is critical for cell cycle regulation in breast cancer cells. Br J Cancer. 2006;94:532–539.
   PubMed Web of Science ®Google Scholar
• Imtiyaz HZ, Zhou X, Zhuang H, et al. The death domain of FADD is essential for embryogenesis, lymphocyte development, and proliferation. J Biol Chem. 2009;284:9917–9926. DOI:10.1074/jbc.M900249200.
   PubMed Web of Science ®Google Scholar
• Thomas LR, Henson A, Reed JC, et al. Direct binding of fas-associated death domain (FADD) to the tumor necrosis factor-related apoptosis-inducing ligand receptor DR5 is regulated by the death effector domain of FADD. J Biol Chem. 2004;279:32780–32785.
   PubMed Web of Science ®Google Scholar
• Shimada K, Nakamura M, Ishida E, et al. Molecular roles of MAP kinases and FADD phosphorylation in prostate cancer. Histol Histopathol. 2006;21:415–422.
   PubMed Web of Science ®Google Scholar
• Yao C, Zhuang H, Cheng W, et al. FADD phosphorylation impaired islet morphology and function. J Cell Physiol. 2015;230:1448–1456. DOI:10.1002/jcp.24885.
   PubMed Web of Science ®Google Scholar
• Yao C, Zhuang H, Du P, et al. Role of fas-associated death domain-containing protein (FADD) phosphorylation in regulating glucose homeostasis: from proteomic discovery to physiological validation. Mol Cell Proteomics. 2013;12:2689–2700. DOI:10.1074/mcp.M113.029306.
   PubMed Web of Science ®Google Scholar
• Balachandran S, Thomas E, Barber GN. A FADD-dependent innate immune mechanism in mammalian cells. Nature. 2004;432:401–405.
   PubMed Web of Science ®Google Scholar
• Balachandran S, Venkataraman T, Fisher PB, et al. Fas-associated death domain-containing protein-mediated antiviral innate immune signaling involves the regulation of Irf7. J Immunol. 2007;178:2429–2439.
   PubMed Web of Science ®Google Scholar
• Tourneur L, Chiocchia G. FADD: a regulator of life and death. Trends Immunol. 2010;31:260–269.
   PubMed Web of Science ®Google Scholar
• Drakos E, Leventaki V, Atsaves V, et al. Expression of serine 194-phosphorylated fas-associated death domain protein correlates with proliferation in B-cell non-Hodgkin lymphomas. Hum Pathol. 2011;42:1117–1124. DOI:10.1016/j.humpath.2010.11.002.
   PubMed Web of Science ®Google Scholar
• Alappat EC, Feig C, Boyerinas B, et al. Phosphorylation of FADD at serine 194 by CKIalpha regulates its nonapoptotic activities. Mol Cell. 2005;19:321–332. DOI:10.1016/j.molcel.2005.06.024.
   PubMed Web of Science ®Google Scholar
• Ramos-Miguel A, Garcia-Fuster MJ, Callado LF, et al. Phosphorylation of FADD (Fas-associated death domain protein) at serine 194 is increased in the prefrontal cortex of opiate abusers: relation to mitogen activated protein kinase, phosphoprotein enriched in astrocytes of 15 kDa, and Akt signaling pathways involved in neuroplasticity. Neuroscience. 2009;161:23–38. DOI:10.1016/j.neuroscience.2009.03.028.
   PubMed Web of Science ®Google Scholar
• Schock SN, Young JA, He TH, et al. Deletion of FADD in macrophages and granulocytes results in RIP3- and MyD88-dependent systemic inflammation. PLoS One. 2015;10:e0124391.
   PubMed Web of Science ®Google Scholar
• Grgic I, Campanholle G, Bijol V, et al. Targeted proximal tubule injury triggers interstitial fibrosis and glomerulosclerosis. Kidney Int. 2012;82:172–183. DOI:10.1038/ki.2012.20.
   PubMed Web of Science ®Google Scholar
• Thiery JP, Acloque H, Huang RY, et al. Epithelial-mesenchymal transitions in development and disease. Cell. 2009;139:871–890.
   PubMed Web of Science ®Google Scholar
• Cannito S, Novo E, di Bonzo LV, et al. Epithelial-mesenchymal transition: from molecular mechanisms, redox regulation to implications in human health and disease. Antioxid Redox Signal. 2010;12:1383–1430. DOI:10.1089/ars.2009.2737.
   PubMed Web of Science ®Google Scholar
• Huen SC, Cantley LG. Macrophages in renal injury and repair. Annu Rev Physiol. 2017;79:449–469.
   PubMed Web of Science ®Google Scholar
• Ferenbach D, Kluth DC, Hughes J. Inflammatory cells in renal injury and repair. Seminars in nephrology. Semin Nephrol. 2007;27:250–259.
   PubMed Web of Science ®Google Scholar
• Damian M, Porteus MH. A crisper look at genome editing: rNA-guided genome modification. Mol Ther. 2013;21:720–722.
   PubMed Web of Science ®Google Scholar
• Zhuang H, Wang X, Zha D, et al. FADD is a key regulator of lipid metabolism. EMBO Mol Med. 2016;8:895–918. DOI:10.15252/emmm.201505924.
   PubMed Web of Science ®Google Scholar
• Scaffidi C, Volkland J, Blomberg I, et al. Phosphorylation of FADD/MORT1 at serine 194 and association with a 70-kDa cell cycle-regulated protein kinase. J Immunol. 2000;164:1236–1242. DOI:10.4049/jimmunol.164.3.1236.
   PubMed Web of Science ®Google Scholar
• Ma Y, Liu H, Tu-Rapp H, et al. Fas ligation on macrophages enhances IL-1R1-toll-like receptor 4 signaling and promotes chronic inflammation. Nat Immunol. 2004;5:380–387. DOI:10.1038/ni1054.
   PubMed Web of Science ®Google Scholar
• Bannerman DD, Tupper JC, Kelly JD, et al. The fas-associated death domain protein suppresses activation of NF-kappa B by LPS and IL-1 beta. J Clin Invest. 2002;109:419–425.
   PubMed Web of Science ®Google Scholar
• Ranjan K, Pathak C. FADD regulates NF-kappaB activation and promotes ubiquitination of cFLIPL to induce apoptosis. Sci Rep. 2016;6:22787.
   PubMed Web of Science ®Google Scholar
• Eid S, Maalouf R, Jaffa AA, et al. 20-HETE and EETs in diabetic nephropathy: a novel mechanistic pathway. PLoS One. 2013;8:e70029. DOI:10.1371/journal.pone.0070029.
   PubMed Web of Science ®Google Scholar
• Nieto MA. Epithelial-mesenchymal transitions in development and disease: old views and new perspectives. Int J Dev Biol. 2009;53:1541–1547.
   PubMed Web of Science ®Google Scholar