Isolation and characterization of DUSP11, a novel p53 target gene

Greta Caprara; Raffaella Zamponi; Marina Melixetian; Kristian Helin

doi:10.1111/j.1582-4934.2008.00616.x

Isolation and characterization of DUSP11, a novel p53 target gene

Greta Caprara, Raffaella Zamponi, Marina Melixetian, Kristian Helin

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

13 Citationer (Scopus)

Abstract

Udgivelsesdato: 2008-Dec-16

Originalsprog	Engelsk
Tidsskrift	Journal of Cellular and Molecular Medicine
Vol/bind	13
Udgave nummer	8B
Sider (fra-til)	2158-70
Antal sider	12
ISSN	1582-1838
DOI	https://doi.org/10.1111/j.1582-4934.2008.00616.x
Status	Udgivet - aug. 2009

Adgang til dokumentet

10.1111/j.1582-4934.2008.00616.x

Citationsformater

@article{62a27ec0ebb411ddbf70000ea68e967b,

title = "Isolation and characterization of DUSP11, a novel p53 target gene",

abstract = "ABSTRACT p53 regulates the expression of genes involved in cell cycle control, apoptosis and DNA damage repair. Here we demonstrate that DUSP11 (Dual Specificity Phosphatase 11), a member of the Protein Tyrosine Phosphatase family that binds to RNA-RNP complexes and RNA splicing factors, is a p53 target gene. Consistent with this, the expression of DUSP11 is induced in a p53-dependent manner after treatment with DNA damaging agents. Chromatin immunoprecipitation analysis showed that p53 binds to 2 putative p53 DNA binding sites in the promoter region of DUSP11. Colony formation and proliferation assays demonstrated that the ectopic expression of wild type, but not catalytical inactive, DUSP11 leads to growth arrest. Furthermore inhibition of DUSP11 expression by shRNA increases the proliferation of normal and DNA damaged cells in tissue culture. Finally we show that the splicing factor SAM68 (Src-Associated protein in Mitotic cells) binds to DUSP11 in vitro and in vivo. Taken together these results suggest that DUSP11 contributes to p53-dependent inhibition of cell proliferation and that it might be involved in regulating RNA splicing through SAM68.",

author = "Greta Caprara and Raffaella Zamponi and Marina Melixetian and Kristian Helin",

year = "2009",

month = aug,

doi = "10.1111/j.1582-4934.2008.00616.x",

language = "English",

volume = "13",

pages = "2158--70",

journal = "Journal of Cellular and Molecular Medicine",

issn = "1582-1838",

publisher = "Wiley-Blackwell",

number = "8B",

}

TY - JOUR

T1 - Isolation and characterization of DUSP11, a novel p53 target gene

AU - Caprara, Greta

AU - Zamponi, Raffaella

AU - Melixetian, Marina

AU - Helin, Kristian

PY - 2009/8

Y1 - 2009/8

N2 - ABSTRACT p53 regulates the expression of genes involved in cell cycle control, apoptosis and DNA damage repair. Here we demonstrate that DUSP11 (Dual Specificity Phosphatase 11), a member of the Protein Tyrosine Phosphatase family that binds to RNA-RNP complexes and RNA splicing factors, is a p53 target gene. Consistent with this, the expression of DUSP11 is induced in a p53-dependent manner after treatment with DNA damaging agents. Chromatin immunoprecipitation analysis showed that p53 binds to 2 putative p53 DNA binding sites in the promoter region of DUSP11. Colony formation and proliferation assays demonstrated that the ectopic expression of wild type, but not catalytical inactive, DUSP11 leads to growth arrest. Furthermore inhibition of DUSP11 expression by shRNA increases the proliferation of normal and DNA damaged cells in tissue culture. Finally we show that the splicing factor SAM68 (Src-Associated protein in Mitotic cells) binds to DUSP11 in vitro and in vivo. Taken together these results suggest that DUSP11 contributes to p53-dependent inhibition of cell proliferation and that it might be involved in regulating RNA splicing through SAM68.

AB - ABSTRACT p53 regulates the expression of genes involved in cell cycle control, apoptosis and DNA damage repair. Here we demonstrate that DUSP11 (Dual Specificity Phosphatase 11), a member of the Protein Tyrosine Phosphatase family that binds to RNA-RNP complexes and RNA splicing factors, is a p53 target gene. Consistent with this, the expression of DUSP11 is induced in a p53-dependent manner after treatment with DNA damaging agents. Chromatin immunoprecipitation analysis showed that p53 binds to 2 putative p53 DNA binding sites in the promoter region of DUSP11. Colony formation and proliferation assays demonstrated that the ectopic expression of wild type, but not catalytical inactive, DUSP11 leads to growth arrest. Furthermore inhibition of DUSP11 expression by shRNA increases the proliferation of normal and DNA damaged cells in tissue culture. Finally we show that the splicing factor SAM68 (Src-Associated protein in Mitotic cells) binds to DUSP11 in vitro and in vivo. Taken together these results suggest that DUSP11 contributes to p53-dependent inhibition of cell proliferation and that it might be involved in regulating RNA splicing through SAM68.

U2 - 10.1111/j.1582-4934.2008.00616.x

DO - 10.1111/j.1582-4934.2008.00616.x

M3 - Journal article

C2 - 19120688

VL - 13

SP - 2158

EP - 2170

JO - Journal of Cellular and Molecular Medicine

JF - Journal of Cellular and Molecular Medicine

SN - 1582-1838

IS - 8B

ER -