Noxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis

Eri Oda; Rieko Ohki; Hideki Murasawa; Jiro Nemoto; Tsukasa Shibue; Toshiharu Yamashita; Takashi Tokino; Tadatsugu Taniguchi; Nobuyuki Tanaka

doi:10.1126/science.288.5468.1053

Abstract

A critical function of tumor suppressor p53 is the induction of apoptosis in cells exposed to noxious stresses. We report a previously unidentified pro-apoptotic gene, Noxa . Expression of Noxa induction in primary mouse cells exposed to x-ray irradiation was dependent on p53. Noxa encodes a Bcl-2 homology 3 (BH3)–only member of the Bcl-2 family of proteins; this member contains the BH3 region but not other BH domains. When ectopically expressed, Noxa underwent BH3 motif–dependent localization to mitochondria and interacted with anti-apoptotic Bcl-2 family members, resulting in the activation of caspase-9. We also demonstrate that blocking the endogenous Noxa induction results in the suppression of apoptosis. Noxa may thus represent a mediator of p53-dependent apoptosis.

Keywords

MediatorApoptosisBcl-2 familyCell biologySuppressorMitochondrionCaspaseBiologyGeneChemistryProgrammed cell deathGenetics

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Publication Info

Year: 2000
Type: article
Volume: 288
Issue: 5468
Pages: 1053-1058
Citations: 2071
Access: Closed

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APA Style

                            
                                
                                    Eri Oda, 
                                
                                    Rieko Ohki, 
                                
                                    Hideki Murasawa
                                
                                et al.
                            
                            (2000). 
                            Noxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis. 
                            Science
                            , 288
                            (5468)
                            , 1053-1058.
                            https://doi.org/10.1126/science.288.5468.1053
                        

Identifiers

DOI: 10.1126/science.288.5468.1053