Molecular Cloning and Characterization of Human Aph2 Gene, Involved in Ap-1 Regulation by Interaction with Jab1.
From: State Key Laboratory of Oncogenes and Related Genes, Shanghai Cancer Institute and Cancer Institute of Shanghai Jiaotong University, Shanghai 200032, PR China.
Biochimica et biophysica acta
- Publish Date:
- ISSN: 0006-3002
- Volume: 1759
- Issue: 11-12
- Pages: 514-25
- Medium: Print
- Language: English
- Citation (JAMA): Zhang Fengrui, Di Yujun, Li Jinjun, et al. Molecular Cloning and Characterization of Human Aph2 Gene, Involved in Ap-1 Regulation by Interaction with Jab1.. Biochim. Biophys. Acta ;1759:514-25
Abstract
A human Aph2 gene (hAph2) was identified and cloned from a human placenta cDNA library. Bioinformatics analysis revealed hAPH2 protein shares 96% identity with mouse APH2 and contains a zf-DHHC domain (148-210aa), which is always involved in protein-protein or protein-DNA interaction. Differential expression patterns of hAph2 mRNA were observed in normal human tissues. Yeast two-hybrid screening found another hAPH2-interacting protein JAB1. The zf-DHHC domain of hAPH2 and the C-terminal of JAB1 were confirmed to be critical for the interaction. Fused with GFP and expressed in COS-7, NIH/3T3 and SMMC-7721 cell lines, hAPH2 showed predominant distribution in the cytoplasm and co-localized with JAB1 around the nucleus. Furthermore, overexpression of hAPH2 could increase apoptosis of COS-7 cells and negatively regulate JAB1-induced activation of AP-1 in a concentration dependent manner. The expression level of c-jun was also down-regulated by overexpression of hAPH2 in COS-7 cells. These data showed some basic characterization and function of hAph2 (hAPH2), dependent or independent with JAB1.
Mesh Headings (Keywords): Amino Acid Sequence, Amyloid Precursor Protein Secretases, Animals, Base Sequence, Binding Sites, Blotting, Western, COS Cells, Cell Line, Tumor, Cercopithecus aethiops, Cloning, Molecular, Female, Gene Expression Profiling, Green Fluorescent Proteins, Humans, Intracellular Signaling Peptides and Proteins, Luciferases, Membrane Glycoproteins, Mice, Microscopy, Fluorescence, Molecular Sequence Data, NIH 3T3 Cells, Peptide Hydrolases, Protein Binding, Sequence Homology, Amino Acid, Transcription Factor AP-1, Transfection, Two-Hybrid System Techniques
Check for Full Text / PubMed Unique Identifier (PMID): 17123647
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