Identifying the Mechanisms of α-Synuclein-Mediated Cytotoxicity in Parkinson’s Disease: New Insights from a Bioinformatics-Based Approach

References

• SotoC. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci.4(1), 49–60 (2003).
   PubMed Web of Science ®Google Scholar
• ChungCG, LeeH, LeeSB. Mechanisms of protein toxicity in neurodegenerative diseases. Cell. Mol. Life Sci.75(17), 3159–3180 (2018).
   PubMed Web of Science ®Google Scholar
• GangulyU, ChakrabartiSS, KaurU, MukherjeeA, ChakrabartiS. Alpha-synuclein, proteotoxicity and Parkinson’s disease: search for neuroprotective therapy. Curr. Neuropharmacol.16(7), 1086–1097 (2018).
   PubMed Web of Science ®Google Scholar
• StefanisL. α-Synuclein in Parkinson’s disease. Cold Spring Harb. Perspect. Med.2(2), a009399 (2012).
   PubMed Web of Science ®Google Scholar
• SurguchovA. Intracellular dynamics of synucleins: “here, there and everywhere”. Int. Rev. Cell Mol. Biol.320, 103–169 (2015).
   PubMed Web of Science ®Google Scholar
• GhiglieriV, CalabreseV, CalabresiP. Alpha- synuclein: from early synaptic dysfunction to neurodegeneration. Front. Neurol.9, 295 (2018).
   PubMed Web of Science ®Google Scholar
• GangulyU, GangulyA, SenOet al.Dopamine cytotoxicity on SH-SY5Y cells: involvement of α-synuclein and relevance in the neurodegeneration of sporadic Parkinson’s disease. Neurotox. Res.35(4), 898–907 (2019).
   PubMed Web of Science ®Google Scholar
• ZhangG, XiaY, WanFet al.New perspectives on roles of alpha-synuclein in Parkinson’s disease. Front. Aging Neurosci.10, 370 (2018).
   PubMedGoogle Scholar
• SmithWW, JiangH, PeiZet al.Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Human Mol. Genet.14(24), 3801–3811 (2005).
   PubMed Web of Science ®Google Scholar
• OrdonezDG, LeeMK, FeanyMB. α-Synuclein induces mitochondrial dysfunction through spectrin and the actin cytoskeleton. Neuron97(1), 108–124 (2018).
   PubMed Web of Science ®Google Scholar
• GallegosS, PachecoC, PetersC, OpazoCM, AguayoLG. Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson’s disease. Front. Neurosci.9, 59 (2015).
   PubMed Web of Science ®Google Scholar
• PfefferkornCM, JiangZ, JenniferC, LeeJC. Biophysics of α-synuclein membrane interactions. Biochim. Biophys. Acta1818(2), 162–171 (2012).
   PubMed Web of Science ®Google Scholar
• EmamzadehFN. Alpha-synuclein structure, functions, and interactions. J. Res. Med. Sci.21, 29 (2016).
   PubMed Web of Science ®Google Scholar
• SchnackC, DanzerKM, GillardonBHF. Protein array analysis of oligomerization-induced changes in alpha-synuclein protein–protein interactions points to an interference with Cdc42 effector proteins. Neuroscience154(4), 1450–1457 (2008).
   PubMed Web of Science ®Google Scholar
• JellingerKA. Interaction between α-synuclein and other proteins in neurodegenerative disorders. Sci. World J.11, 1893–1907 (2011).
   Google Scholar
• VenderovaK, ParkDS. Programmed cell death in Parkinson’s disease. Cold Spring Harb. Perspect. Med.2(8), a009365 (2012).
   PubMed Web of Science ®Google Scholar
• PerierC, BovéJ, VilaM. Mitochondria and programmed cell death in Parkinson’s disease: apoptosis and beyond. Antioxid. Redox Signal.16(9), 883–895 (2012).
   PubMed Web of Science ®Google Scholar
• BirA, SenO, AnandSet al.α-Synuclein induced mitochondrial dysfunction in isolated preparation and intact cells: implications in the pathogenesis of Parkinson’s disease. J. Neurochem.131(6), 868–877 (2014).
   PubMed Web of Science ®Google Scholar
• GangulyU, BanerjeeA, ChakrabartiSSet al.Interaction of α-synuclein and Parkin in iron toxicity on SH-SY5Y cells: implications in the pathogenesis of Parkinson’s disease. Biochem. J.477(6), 1109–1122 (2020).
   PubMed Web of Science ®Google Scholar
• DroitA, PoirierGG, HunterJM. Experimental and bioinformatic approaches for interrogating protein–protein interactions to determine protein function. J. Mol. Endocrinol.34(2), 263–280 (2005).
   PubMed Web of Science ®Google Scholar
• KuzmanovU, EmiliA. Protein–protein interaction networks: probing disease mechanisms using model systems. Genome Med.5(4), 37 (2013).
   PubMedGoogle Scholar
• PawsonT, NashP. Protein–protein interactions define specificity in signal transduction. Genes Dev.14(9), 1027–1047 (2000).
   PubMed Web of Science ®Google Scholar
• KolchW. Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions. Biochem. J.351(Pt 2), 289–305 (2000).
   PubMed Web of Science ®Google Scholar
• SzklarczykD, FranceschiniA, WyderSet al.STRING v10: protein–protein interaction networks, integrated over the tree of life. Nucleic Acids Res.43(Database Issue), D447–D452 (2015).
   PubMed Web of Science ®Google Scholar
• CamachoCJ, GatchellDW, KimuraSR, VajdaS. Scoring docked conformations generated by rigid-body protein–protein docking. Proteins40(3), 525–537 (2000).
   PubMed Web of Science ®Google Scholar
• WengZ, VajdaS, DelisiC. Prediction of protein complexes using empirical free energy functions. Protein Sci.5(4), 614–626 (1996).
   PubMed Web of Science ®Google Scholar
• HalperinI, MaB, WolfsonH, NussinovR. Principles of docking: an overview of search algorithms and a guide to scoring functions. Proteins47(4), 409–443 (2002).
   PubMed Web of Science ®Google Scholar
• KozakovD, HallDR, XiaBet al.The ClusPro web server for protein–protein docking. Nat. Protocols.12(2), 255–278 (2017).
   PubMed Web of Science ®Google Scholar
• TinaKG, BhadraR, SrinivasanN. PIC: protein interactions calculator. Nucleic Acids Res.35(Web server issue), W473–W476 (2007).
   PubMed Web of Science ®Google Scholar
• EmamzadehFN, SurguchovA. Parkinson’s disease: biomarkers, treatment, and risk factors. Front. Neurosci.12, 612 (2018).
   PubMed Web of Science ®Google Scholar
• DewsonG, KluckRM. Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis. J. Cell Sci.122(pt 16), 2801–2808 (2009).
   PubMed Web of Science ®Google Scholar
• LalierL, CartronP-F, OlivierCet al.Prostaglandins antagonistically control Bax activation during apoptosis. Cell Death Differen.18(3), 528–537 (2011).
   PubMed Web of Science ®Google Scholar
• BouilletP, StrasserA. BH3-only proteins – evolutionarily conserved proapoptotic Bcl-2 family members essential for initiating programmed cell death. J. Cell Sci.115(Pt 8), 1567–1574 (2002).
   PubMed Web of Science ®Google Scholar
• ChoiME, PriceDR, RyterSW, ChoiAMK. Necroptosis: a crucial pathogenic mediator of human disease. JCI Insight4(15), e128834 (2019).
   PubMed Web of Science ®Google Scholar