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Parkinson disease protein 7

Definition:

Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Has been described as a protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. But this function is rebuted by other works. As a protein deglycase, repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin. Able to remove the glycations and restore histone 3, histone glycation disrupts both local and global chromatin architecture by altering histone-DNA interactions as well as histone acetylation and ubiquitination levels. Displays a very low glyoxalase activity that may reflect its deglycase activity. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells. In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity. In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity).

References:

[1]. Ju-young Lee, et al. Human DJ-1 and its homologs are novel glyoxalases. Hum Mol Genet. 2012 Jul 15;21(14):3215-25. [Content Brief]

[2]. Takahiro Taira, et al. DJ-1 has a role in antioxidative stress to prevent cell death. EMBO Rep. 2004 Feb;5(2):213-8. [Content Brief]

[3]. Aya Sekito, et al. DJ-1 interacts with HIPK1 and affects H2O2-induced cell death. Free Radic Res. 2006 Feb;40(2):155-65. [Content Brief]

[4]. Eunsung Junn, et al. Mitochondrial localization of DJ-1 leads to enhanced neuroprotection. J Neurosci Res. 2009 Jan;87(1):123-9. [Content Brief]

[5]. Gilbert Richarme, et al. Guanine glycation repair by DJ-1/Park7 and its bacterial homologs. Science. 2017 Jul 14;357(6347):208-211. [Content Brief]

[6]. Y Shinbo, et al. Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities. Cell Death Differ. 2006 Jan;13(1):96-108. [Content Brief]

[7]. Gilbert Richarme, et al. Parkinsonism-associated protein DJ-1 is a bona fide deglycase. Biochem Biophys Res Commun. 2017 Jan 29;483(1):387-391. [Content Brief]

[8]. Beisha Tang, et al. Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease. Hum Mol Genet. 2006 Jun 1;15(11):1816-25. [Content Brief]

[9]. Hui Xiong, et al. Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation. J Clin Invest. 2009 Mar;119(3):650-60. [Content Brief]

[10]. Kazuya Honbou, et al. The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease. J Biol Chem. 2003 Aug 15;278(33):31380-4. [Content Brief]

[11]. Qingfei Zheng, et al. Reversible histone glycation is associated with disease-related changes in chromatin architecture. Nat Commun. 2019 Mar 20;10(1):1289. [Content Brief]

[12]. Shoshana Shendelman, et al. DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol. 2004 Nov;2(11):e362. [Content Brief]

[13]. D Nagakubo, et al. DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras. Biochem Biophys Res Commun. 1997 Feb 13;231(2):509-13. [Content Brief]

[14]. Noriyuki Matsuda, et al. Parkinson's disease-related DJ-1 functions in thiol quality control against aldehyde attack in vitro. Sci Rep. 2017 Oct 9;7(1):12816. [Content Brief]

[15]. Benny Björkblom, et al. Parkinson disease protein DJ-1 binds metals and protects against metal-induced cytotoxicity. J Biol Chem. 2013 Aug 2;288(31):22809-20. [Content Brief]

[16]. R Sean McNally, et al. DJ-1 enhances cell survival through the binding of Cezanne, a negative regulator of NF-kappaB. J Biol Chem. 2011 Feb 11;286(6):4098-106. [Content Brief]

[17]. Jue Chen, et al. Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage. Hum Mol Genet. 2010 Jun 15;19(12):2395-408. [Content Brief]

[18]. Daniel H Pfaff, et al. Evidence Against a Role for the Parkinsonism-associated Protein DJ-1 in Methylglyoxal Detoxification. J Biol Chem. 2017 Jan 13;292(2):685-690. [Content Brief]

[19]. K Takahashi, et al. DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor. J Biol Chem. 2001 Oct 5;276(40):37556-63. [Content Brief]

[20]. Sun-Joo Lee, et al. Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain. J Biol Chem. 2003 Nov 7;278(45):44552-9. [Content Brief]

[21]. James J Galligan, et al. Methylglyoxal-derived posttranslational arginine modifications are abundant histone marks. Proc Natl Acad Sci U S A. 2018 Sep 11;115(37):9228-9233. [Content Brief]

[22]. Guido Krebiehl, et al. Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1. PLoS One. 2010 Feb 23;5(2):e9367. [Content Brief]

[23]. Tamara Advedissian, et al. The Parkinsonism-associated protein DJ-1/Park7 prevents glycation damage in human keratinocyte. Biochem Biophys Res Commun. 2016 Apr 22;473(1):87-91. [Content Brief]

[24]. Kwang Soo Kim, et al. DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes. Hum Mol Genet. 2013 Dec 1;22(23):4805-17. [Content Brief]

[25]. Mark A Wilson, et al. The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease. Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9256-61. [Content Brief]

[26]. Marcel P van der Brug, et al. RNA binding activity of the recessive parkinsonism protein DJ-1 supports involvement in multiple cellular pathways. Proc Natl Acad Sci U S A. 2008 Jul 22;105(29):10244-9. [Content Brief]

[27]. Rosa M Canet-Avilés, et al. The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):9103-8. [Content Brief]

[28]. Casey M Clements, et al. DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15091-6. [Content Brief]

[29]. Anna Andreeva, et al. The apparent deglycase activity of DJ-1 results from the conversion of free methylglyoxal present in fast equilibrium with hemithioacetals and hemiaminals. J Biol Chem. 2019 Dec 6;294(49):18863-18872. [Content Brief]

[30]. Gilbert Richarme, et al. Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues. J Biol Chem. 2015 Jan 16;290(3):1885-97. [Content Brief]

[31]. Takeshi Niki, et al. DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex. Mol Cancer Res. 2003 Feb;1(4):247-61. [Content Brief]

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