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

Sayaka Ohashi; Masayuki Kanai; Shuji Hanai; Fumiaki Uchiumi; Hideharu Maruta; Sei Ichi Tanuma; Masanao Miwa

doi:10.1016/S0006-291X(03)01272-5

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

Sayaka Ohashi, Masayuki Kanai, Shuji Hanai, Fumiaki Uchiumi, Hideharu Maruta, Sei Ichi Tanuma, Masanao Miwa

Research output: Contribution to journal › Article › peer-review

61 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	915-921
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	307
Issue number	4
DOIs	https://doi.org/10.1016/S0006-291X(03)01272-5
Publication status	Published - 8 Aug 2003

Keywords

Cell cycle
Centrosomes
PARG
PARP
Poly(ADP-ribose)
Poly(ADP-ribosyl)ation

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10.1016/S0006-291X(03)01272-5

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title = "Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells",

abstract = "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.",

keywords = "Cell cycle, Centrosomes, PARG, PARP, Poly(ADP-ribose), Poly(ADP-ribosyl)ation",

author = "Sayaka Ohashi and Masayuki Kanai and Shuji Hanai and Fumiaki Uchiumi and Hideharu Maruta and Tanuma, \{Sei Ichi\} and Masanao Miwa",

note = "Funding Information: We are grateful to Dr. T. Urano, Nagoya University, for human breast carcinoma cell line, MDA-435 cells. We thank E. Sugihara, Y. Nogi, and A. Kabayama for precious comments and technical assistance. This work was supported in part by Grant-in-Aids for Cancer Research from the Ministry of Health, Labour and Welfare, and from Japan Society for the Promotion of Science, Japan.",

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doi = "10.1016/S0006-291X(03)01272-5",

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T1 - Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells

AU - Ohashi, Sayaka

AU - Kanai, Masayuki

AU - Hanai, Shuji

AU - Uchiumi, Fumiaki

AU - Maruta, Hideharu

AU - Tanuma, Sei Ichi

AU - Miwa, Masanao

N1 - Funding Information: We are grateful to Dr. T. Urano, Nagoya University, for human breast carcinoma cell line, MDA-435 cells. We thank E. Sugihara, Y. Nogi, and A. Kabayama for precious comments and technical assistance. This work was supported in part by Grant-in-Aids for Cancer Research from the Ministry of Health, Labour and Welfare, and from Japan Society for the Promotion of Science, Japan.

PY - 2003/8/8

Y1 - 2003/8/8

N2 - 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.

AB - 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.

KW - Cell cycle

KW - Centrosomes

KW - PARG

KW - PARP

KW - Poly(ADP-ribose)

KW - Poly(ADP-ribosyl)ation

UR - https://www.scopus.com/pages/publications/0038105404

U2 - 10.1016/S0006-291X(03)01272-5

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SN - 0006-291X

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

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

Abstract

Keywords

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