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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Crystal Structure of Filamentous Aggregates of Human DJ-1 Formed in an Inorganic Phosphate-dependent Manner

Cited 8 times inthomson ciCited 8 times inthomson ci
Title
Crystal Structure of Filamentous Aggregates of Human DJ-1 Formed in an Inorganic Phosphate-dependent Manner
Author
Cha, Sun-ShinIl Jung, HaJeon, HyesungAn, Young JunKim, In-KwonYun, SangukAhn, Hyun JinChung, Kwang ChulLee, Sang HeeSuh, Pann-GhillKang, Sa-Ouk
Keywords
FAMILIAL PARKINSONS-DISEASE; MULTIPLE SYSTEM ATROPHY; OXIDATIVE STRESS; DROSOPHILA DJ-1; ALPHA-SYNUCLEIN; PROTEIN DJ-1; CELL-DEATH; FERTILITY; L166P; INACTIVATION
Issue Date
200812
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.283, no.49, pp.34069 - 34075
Abstract
Mutations in the DJ-1 gene have been implicated in the autosomal recessive early onset parkinsonism. DJ-1 is a soluble dimeric protein with critical roles in response to oxidative stress and in neuronal maintenance. However, several lines of evidence suggest the existence of a nonfunctional aggregated form of DJ-1 in the brain of patients with some neurodegenerative diseases. Here, we show that inorganic phosphate, an important anion that exhibits elevated levels in patients with Parkinson disease, transforms DJ-1 into filamentous aggregates. According to the 2.4-A crystal structure, DJ-1 dimers are linearly stacked through Pi-mediated interactions to form protofilaments, which are then bundled into a filamentous assembly.
URI
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DOI
http://dx.doi.org/10.1074/jbc.M804243200
ISSN
0021-9258
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