Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress

Li, Hong Mei; Niki, Takeshi; Taira, Takahiro; Iguchi‐Ariga, Sanae M.M.; Ariga, Hiroyoshi

doi:10.1080/10715760500260348

Cited by 148 publications

(113 citation statements)

References 43 publications

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“…2A). As described previously [1,26,28], DJ-1 was located both in the nucleus and cytoplasm and some portions of DJ-1 were colocalized with mitochondria under a non-stress condition (See merged figure in which green (DJ-1) and red (mitochondria) were turned yellow.). To clearly see mitochondria-resident proteins, NIH3T3 cells on cover glasses were heated to inactivate antigenecity of cytoplasmic proteins and then stained with anti-DJ-1 and anti-NDUFS3 antibodies.…”

Section: Identification Of Subunits Of Mitochondrial Complex I As Dj-mentioning

confidence: 58%

“…DJ-1 is located both in the cytoplasm and nucleus [1] and has recently been shown to be located in mitochondria [11,[24][25][26]. It has also been reported that some parts of DJ-1 were translocated into mitochondria after cells had been subjected to oxidative stress to protect cells from oxidative stress-induced cell death [27][28][29][30]. The exact localization of DJ-1 in mitochondria, inner membrane, outer membrane or intermembrane space, is, however, still not clear, and the characteristics and function of mitochondria-resident DJ-1 are still not known.…”

Section: Introductionmentioning

confidence: 99%

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DJ-1 binds to mitochondrial complex I and maintains its activity

Hayashi

Ishimori

Takahashi-Niki

et al. 2009

Biochemical and Biophysical Research Communications

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167

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Parkinson's disease (PD) is caused by neuronal cell death, and oxidative stress and mitochondrial dysfunction are thought to be responsible for onset of PD. DJ-1, a causative gene product of a familial form of Parkinson's disease, PARK7, plays roles in transcriptional regulation and anti-oxidative stress. The possible mitochondrial function of DJ-1 has been proposed, but its exact function remains unclear. In this study, we found that DJ-1 directly bound to NDUFA4 and ND1, nuclear and mitochondrial DNA-encoding subunits of mitochondrial complex I, respectively, and was co-localized with complex I and that complex I activity was reduced in DJ-1-knockdown NIH3T3 and HEK293cells. These findings suggest that DJ-1 is an integral mitochondrial protein and that DJ-1 plays a role in maintenance of mitochondrial complex I activity.

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Section: Identification Of Subunits Of Mitochondrial Complex I As Dj-mentioning

confidence: 58%

Section: Introductionmentioning

confidence: 99%

DJ-1 binds to mitochondrial complex I and maintains its activity

Hayashi

Ishimori

Takahashi-Niki

et al. 2009

Biochemical and Biophysical Research Communications

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167

118

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“…DJ-1 is a dimeric protein and has some structural similarities with heat-shock proteins (45). Deletion and a point mutation (L166P) of DJ-1 that disrupts normal dimer formation are responsible for the onset of familiar Parkinson's disease (46).…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization of an oocyte factor required for development of porcine nuclear transfer embryos

Miyamoto

Nagai²,

Kitamura³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Nuclear reprogramming of differentiated cells can be induced by oocyte factors. Despite numerous attempts, these factors and mechanisms responsible for successful reprogramming remain elusive. Here, we identify one such factor, necessary for the development of nuclear transfer embryos, using porcine oocyte extracts in which some reprogramming events are recapitulated. After incubating somatic nuclei in oocyte extracts from the metaphase II stage, the oocyte proteins that were specifically and abundantly incorporated into the nuclei were identified by mass spectrometry. Among 25 identified proteins, we especially focused on a multifunctional protein, DJ-1. DJ-1 is present at a high concentration in oocytes from the germinal vesicle stage until embryos at the fourcell stage. Inhibition of DJ-1 function compromises the development of nuclear transfer embryos but not that of fertilized embryos. Microarray analysis of nuclear transfer embryos in which DJ-1 function is inhibited shows perturbed expression of P53 pathway components. In addition, embryonic arrest of nuclear transfer embryos injected with anti-DJ-1 antibody is rescued by P53 inhibition. We conclude that DJ-1 is an oocyte factor that is required for development of nuclear transfer embryos. This study presents a means for identifying natural reprogramming factors in mammalian oocytes and a unique insight into the mechanisms underlying reprogramming by nuclear transfer.oocyte extract and proteomics | reprogramming in mammalian oocytes E mbryonic cells differentiate into specific types of cells as development progresses. Once differentiated, the reversion of a differentiated cell state to an original undifferentiated state is strictly inhibited in normal development. However, it has been experimentally shown that differentiated nuclei can be returned to an undifferentiated embryonic state after nuclear transfer (NT) to enucleated eggs or oocytes (1, 2). Such experiments provide an opportunity to reprogram somatic cells as a means to prepare undifferentiated cells, which may be differentiated into any kinds of cells for cell-replacement therapy. Recently, nuclear reprogramming technology has been expanded by the production of induced pluripotent stem (iPS) cells (3). iPS cells can be obtained by overexpressing specific sets of transcription factors such as Oct4, Sox2, Klf4, and c-myc in cultured cells. The processes leading to establishment of iPS cell lines are being carefully examined and we are begining to understand how somatic cells acquire pluripotency by this method (4-6). The mechanisms leading to pluripotency may be different between iPS cells and NT embryos because somatic nuclei transferred into unfertilized metaphase II (MII) oocytes must undergo early embryonic development before the inner cell mass (ICM) can give rise to pluripotent embryonic stem (ES) cells. In addition, the molecules and mechanisms that induce somatic cell reprogramming are expected to be different between iPS cells and NT embryos (7,8). A recent study has shown that nuclear t...

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“…Furthermore, we have reported that DJ-1 activated TH and DDC through direct binding to TH and DDC in an oxidative status of DJ-1-dependent manner [24] and that human DJ-1 activates TH gene expression in cultured human dopaminergic cells [15]. DJ-1 is preferentially localized in the cytoplasm and nucleus [7] and a portion of DJ-1 is localized in the mitochondria [22,[25][26][27] and synapse [28].…”

Section: Introductionmentioning

confidence: 99%

Stimulation of vesicular monoamine transporter 2 activity by DJ-1 in SH-SY5Y cells

Ishikawa

Tanaka

Takahashi-Niki

et al. 2012

Biochemical and Biophysical Research Communications

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Loss-of-functional mutation in the DJ-1 gene causes a subset of familial Parkinson's disease. The mechanism underlying DJ-1-related selective vulnerability in the dopaminergic pathway is, however, not known. Dopamine is synthesized by two enzymes and then packed into synaptic vesicles by vesicular monoamine transporter 2 (VMAT2). In this study, we found that knockdown of DJ-1 expression reduced the levels of mRNA and protein of VMAT2, resulting in reduced VMAT2 activity. Co-immunoprecipitation and pull-down experiments revealed that DJ-1 directly bound to VMAT2, and DJ-1 was co-localized with VMAT2 in cells. Furthermore, ectopic expression of wild-type DJ-1, but not that of L166P, M26I and C106S mutants of DJ-1, increased mRNA and protein levels of VMAT2 and VMAT2 activity. Since VMAT2 and a portion of DJ-1 are localized in the synaptic membrane, these results suggest that DJ-1, but not pathogenically mutated DJ-1, stimulates VMAT2 activity in the synapse by transactivation of the VMAT gene and by direct binding to VMAT2 and that cysteine 106 is necessary for the stimulating activity of DJ-1 toward VMAT2.

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Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress

Cited by 148 publications

References 43 publications

DJ-1 binds to mitochondrial complex I and maintains its activity

DJ-1 binds to mitochondrial complex I and maintains its activity

Identification and characterization of an oocyte factor required for development of porcine nuclear transfer embryos

Stimulation of vesicular monoamine transporter 2 activity by DJ-1 in SH-SY5Y cells

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