Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells

被引：59
作者：
Ohashi, S
Kanai, M
Hanai, S
Uchiumi, F
Maruta, H
Tanuma, S
Miwa, M
机构：
[1] Univ Tsukuba, Inst Basic Med Sci, Dept Biochem & Mol Oncol, Tsukuba, Ibaraki 3058575, Japan
[2] Tokyo Univ Sci, Fac Pharmaceut Sci, Dept Biochem, Noda, Chiba 2788501, Japan
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 307卷 / 04期
基金：
日本学术振兴会;
关键词：
PARG; PARP; poly(ADP-ribosyl)ation; poly(ADP-ribose); cell cycle; centrosomes;
D O I：
10.1016/S0006-291X(03)01272-5
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Posttranslational modification plays important roles in a range of cellular functions. Poly(ADP-ribosyl)ation influences DNA repair, transcription, centrosome duplication, and chromosome stability. Poly(ADP-ribose) attached to acceptor proteins should be properly hydrolyzed by poly(ADP-ribose) glycohydrolase (PARG). However the subcellular localization and the role of PARG have not been well characterized. Here, we transiently expressed GFP- or Myc-tagged human PARG in mammalian cells and revealed that the subcellular distribution of human PARG changes dramatically during the cell cycle. GFP-hPARG is found almost exclusively in the nucleus during interphase. During mitosis, most GFP-hPARG protein localizes to the cytoplasm and hardly any GFP-hPARG protein is found associated with the chromosomes. Furthermore, we found that GFP-hPARG localizes to the centrosomes during mitosis. Our findings suggest that shuttling of PARG between nucleus and cytoplasm and proper control of poly(ADP-ribose) metabolism throughout the cell cycle may play an important role in regulating cell cycle progression and centrosome duplication. (C) 2003 Elsevier Inc. All rights reserved.
引用
收藏
页码：915 / 921
页数：7
相关论文
共 29 条
[1]   DISSECTION OF ADP-RIBOSE POLYMER SYNTHESIS INTO INDIVIDUAL STEPS OF INITIATION, ELONGATION, AND BRANCHING [J].
ALVAREZGONZALEZ, R ;
MENDOZAALVAREZ, H .
BIOCHIMIE, 1995, 77 (06) :403-407
[2]   Molecular heterogeneity and regulation of poly(ADP-ribose)glycohydrolase [J].
Amé, JC ;
Jacobson, EL ;
Jacobson, MK .
MOLECULAR AND CELLULAR BIOCHEMISTRY, 1999, 193 (1-2) :75-81
[3]   PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression [J].
Augustin, A ;
Spenlehauer, C ;
Dumond, H ;
Murcia, JMD ;
Piel, M ;
Schmit, AC ;
Apiou, F ;
Vonesch, JL ;
Kock, M ;
Bornens, M ;
de Murcia, G .
JOURNAL OF CELL SCIENCE, 2003, 116 (08) :1551-1562
[4]   MODE OF ACTION OF POLY(ADP-RIBOSE) GLYCOHYDROLASE [J].
BROCHU, G ;
DUCHAINE, C ;
THIBEAULT, L ;
LAGUEUX, J ;
SHAH, GM ;
POIRIER, GG .
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 1994, 1219 (02) :342-350
[5]   PURIFICATION OF POLY(ADP-RIBOSE) GLYCOHYDROLASE AND DETECTION OF ITS ISOFORMS BY A ZYMOGRAM FOLLOWING ONE-DIMENSIONAL OR 2-DIMENSIONAL ELECTROPHORESIS [J].
BROCHU, G ;
SHAH, GM ;
POIRIER, GG .
ANALYTICAL BIOCHEMISTRY, 1994, 218 (02) :265-272
[6]   Tankyrase is a Golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles [J].
Chi, NW ;
Lodish, HF .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (49) :38437-38444
[7]   Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions [J].
D'Amours, D ;
Desnoyers, S ;
D'Silva, I ;
Poirier, GG .
BIOCHEMICAL JOURNAL, 1999, 342 :249-268
[8]   BRCA1 is associated with the centrosome during mitosis [J].
Hsu, LC ;
White, RL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (22) :12983-12988
[9]   TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression [J].
Kaminker, PG ;
Kim, SH ;
Taylor, RD ;
Zebarjadian, Y ;
Funk, WD ;
Morin, GB ;
Yaswen, P ;
Campisi, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (38) :35891-35899
[10]   Poly(ADP-ribose) polymerase localizes to the centrosomes and chromosomes [J].
Kanai, M ;
Uchida, M ;
Hanai, S ;
Uematsu, N ;
Uchida, K ;
Miwa, M .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 278 (02) :385-389
123