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DJ-1 cooperates with PYCR1 in cell protection against oxidative stress.

Abstract：

:DJ-1, a product of the DJ-1/PARK7 gene, has been suggested to play various functions involved in transcriptional regulation, protease activity, anti-oxidative stress activity, and regulation of mitochondrial complex I. Such a variety of functions of DJ-1 are supposed to be realized through interactions with different partner proteins. Among the candidates for DJ-1-partner proteins detected in TOF-MAS analyses of the cellular proteins co-immunoprecipitated with DJ-1, we focused here pyrroline-5-carboxylate reductase 1, PYCR1, a final key enzyme for proline biosynthesis. DJ-1 directly bound to PYCR1 in vivo and in vitro. DJ-1 and PYCR1 colocalized in mitochondria, and both were suggested to be involved in regulation of mitochondrial membrane potential, but differently. DJ-1 enhanced the enzymatic activity of PYCR1 in vitro. The cells knocked down for DJ-1 and PYCR1 showed lower viability under oxidative stress conditions. No additive nor synergistic results were obtained for the cells that had been knocked down for both DJ-1 and PYCR1, suggesting that DJ-1 and PYCR1 are on the same pathway of anti-oxidative stress protection of the cells.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yasuda T,Kaji Y,Agatsuma T,Niki T,Arisawa M,Shuto S,Ariga H,Iguchi-Ariga SM

doi

10.1016/j.bbrc.2013.05.095

subject

Has Abstract

pub_date

2013-06-28 00:00:00

pages

289-94

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(13)00902-9

journal_volume

436

pub_type

杂志文章

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