The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1 (original) (raw)
Faccio, L. et al. Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia. J. Biol. Chem.275, 2581–2588 (2000). ArticleCAS Google Scholar
Gray, C. W. et al. Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response. Eur. J. Biochem.267, 5699–5710 (2000). ArticleCAS Google Scholar
Hegde, R. et al. Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein–caspase interaction. J. Biol. Chem.277, 432–438 (2002). ArticleCAS Google Scholar
Martins, L. M. et al. The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif. J. Biol. Chem.277, 439–444 (2002). ArticleCAS Google Scholar
Suzuki, Y. et al. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell8, 613–621 (2001). ArticleCAS Google Scholar
Verhagen, A. M. et al. HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins. J. Biol. Chem.277, 445–454 (2002). ArticleCAS Google Scholar
Martins, L. M. et al. Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi. J. Biol. Chem.278, 49417–49427 (2003). ArticleCAS Google Scholar
Yang, Q. H., Church-Hajduk, R., Ren, J., Newton, M. L. & Du, C. Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis. Genes Dev.17, 1487–1496 (2003). ArticleCAS Google Scholar
Jones, J. M. et al. Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice. Nature425, 721–727 (2003). ArticleCAS Google Scholar
Martins, L. M. et al. Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Mol. Cell. Biol.24, 9848–9862 (2004). ArticleCAS Google Scholar
Spiess, C., Beil, A. & Ehrmann, M. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell97, 339–347 (1999). ArticleCAS Google Scholar
Walsh, N. P., Alba, B. M., Bose, B., Gross, C. A. & Sauer, R. T. OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell113, 61–71 (2003). ArticleCAS Google Scholar
Strauss, K. M. et al. Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease. Hum. Mol. Genet.14, 2099–2111 (2005). ArticleCAS Google Scholar
Cilenti, L. et al. Regulation of HAX-1 anti-apoptotic protein by Omi/HtrA2 protease during cell death. J. Biol. Chem.279, 50295–50301 (2004). ArticleCAS Google Scholar
Valente, E. M. et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science304, 1158–1160 (2004). ArticleCAS Google Scholar
Bonifati, V. et al. Early-onset parkinsonism associated with PINK1 mutations: frequency, genotypes, and phenotypes. Neurology65, 87–95 (2005). ArticleCAS Google Scholar
Hatano, Y. et al. Novel PINK1 mutations in early-onset parkinsonism. Ann. Neurol.56, 424–427 (2004). ArticleCAS Google Scholar
Li, Y. et al. Clinicogenetic study of PINK1 mutations in autosomal recessive early-onset parkinsonism. Neurology64, 1955–1957 (2005). ArticleCAS Google Scholar
Rogaeva, E. et al. Analysis of the PINK1 gene in a large cohort of cases with Parkinson disease. Arch. Neurol.61, 1898–1904 (2004). Article Google Scholar
Rohe, C. F. et al. Homozygous PINK1 C-terminus mutation causing early-onset parkinsonism. Ann. Neurol.56, 427–431 (2004). ArticleCAS Google Scholar
Obenauer, J. C., Cantley, L. C. & Yaffe, M. B. Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res.31, 3635–3641 (2003). ArticleCAS Google Scholar
Kuma, Y. et al. BIRB796 inhibits all p38 MAPK isoforms in vitro and in vivo. J. Biol. Chem.280, 19472–19479 (2005). ArticleCAS Google Scholar
Chandel, N. S. et al. Mitochondrial reactive oxygen species trigger hypoxia-induced transcription. Proc. Natl Acad. Sci. USA95, 11715–11720 (1998). ArticleCAS Google Scholar
Li, W. et al. Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. Nature Struct. Biol.9, 436–441 (2002). ArticleCAS Google Scholar
Wilken, C., Kitzing, K., Kurzbauer, R., Ehrmann, M. & Clausen, T. Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease. Cell117, 483–494 (2004). ArticleCAS Google Scholar
Greenamyre, J. T. & Hastings, T. G. Biomedicine. Parkinson's—divergent causes, convergent mechanisms. Science304, 1120–1122 (2004). ArticleCAS Google Scholar
Paisan-Ruiz, C. et al. Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease. Neuron44, 595–600 (2004). ArticleCAS Google Scholar
Ramirez, A. et al. Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase. Nature Genet.38, 1184–1191 (2006). ArticleCAS Google Scholar
Zimprich, A. et al. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron44, 601–607 (2004). ArticleCAS Google Scholar
Beilina, A. et al. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc. Natl Acad. Sci. USA102, 5703–5708 (2005). ArticleCAS Google Scholar
Silvestri, L. et al. Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum. Mol. Genet.14, 3477–3492 (2005). ArticleCAS Google Scholar
Sim, C. H. et al. C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1. Hum. Mol. Genet.15, 3251–3262 (2006). ArticleCAS Google Scholar
Harper, S. J. & Wilkie, N. MAPKs: new targets for neurodegeneration. Expert Opin. Ther. Targets7, 187–200 (2003). ArticleCAS Google Scholar
Pridgeon, J. W., Olzmann, J. A., Chin, L. S. & Li, L. PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLOS Biol.5, e172 (2007). Article Google Scholar
Young, J. C. & Hartl, F. U. A stress sensor for the bacterial periplasm. Cell113, 1–2 (2003). ArticleCAS Google Scholar
Abou-Sleiman, P. M. et al. A heterozygous effect for PINK1 mutations in Parkinson's disease? Ann. Neurol.60, 414–419 (2006). ArticleCAS Google Scholar
Gandhi, S. et al. PINK1 protein in normal human brain and Parkinson's disease. Brain129, 1720–1731 (2006). ArticleCAS Google Scholar
Vyas, S. et al. Differentiation-dependent sensitivity to apoptogenic factors in PC12 cells. J. Biol. Chem.279, 30983–30993 (2004). ArticleCAS Google Scholar
Evan, G. I., Lewis, G. K., Ramsay, G. & Bishop, J. M. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol.5, 3610–3616 (1985). ArticleCAS Google Scholar
Garner, A. P., Weston, C. R., Todd, D. E., Balmanno, K. & Cook, S. J. ΔMEKK3:ER* activation induces a p38α/β2-dependent cell cycle arrest at the G2 checkpoint. Oncogene21, 8089–8104 (2002). ArticleCAS Google Scholar
Rytomaa, M., Lehmann, K. & Downward, J. Matrix detachment induces caspase-dependent cytochrome c release from mitochondria: inhibition by PKB/Akt but not Raf signalling. Oncogene19, 4461–4468 (2000). ArticleCAS Google Scholar
Abraham, V. C., Taylor, D. L. & Haskins, J. R. High content screening applied to large-scale cell biology. Trends Biotechnol.22, 15–22 (2004). ArticleCAS Google Scholar