The N-terminus of a novel isoform of human iASPP is required for its cytoplasmic localization

• Published in: Oncogene Vol. 23; no. 56; pp. 9007 - 9016
• Main Authors: Slee, Elizabeth A, Gillotin, Sébastien, Bergamaschi, Daniele, Royer, Christophe, Llanos, Susana, Ali, Safia, Jin, Boquan, Trigiante, Giuseppe, Lu, Xin
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 02.12.2004; Nature Publishing; Nature Publishing Group
• Subjects: Adaptor Proteins, Signal Transducing; Ageing, cell death; Amino Acid Sequence; Amino acids; Apoptosis; Apoptosis - physiology; Apoptosis Regulatory Proteins; Base Sequence; Biological and medical sciences; Cancer research; Carrier Proteins - chemistry; Carrier Proteins - metabolism; Cell Biology; Cell cycle; Cell death; Cell division; Cell Line, Tumor; Cell physiology; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes; Cytoplasm; Cytoplasm - metabolism; DNA damage; DNA Primers; Fundamental and applied biological sciences. Psychology; Human Genetics; Humans; Internal Medicine; Localization; Medical research; Medicine; Medicine & Public Health; Molecular and cellular biology; Molecular Sequence Data; N-Terminus; Nematodes; Oncology; original-paper; p53 Protein; Protein Isoforms - chemistry; Protein Isoforms - metabolism; Proteins; Sequence Homology, Amino Acid; Tumor Suppressor Protein p53 - metabolism; Tumor Suppressor Protein p53 - physiology; apoptosis; iASPP; p53; Human; Molecular form; TP53 Gene; Localization; Carcinogenesis; Apoptosis; Tumor suppressor gene

ASPP1 and ASPP2 are both proteins that interact with p53 and enhance its ability to induce apoptosis by selectively elevating the expression of proapoptotic p53-responsive genes. iASPP(RAI) is a third member of the family that is the most conserved inhibitor of p53-mediated apoptosis. Here, we have...