Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein.
Hsp70 family member mot-2/mthsp70/GRP75/PBP74 was shown to bind to the tumor suppressor protein p53. In this study, by in vivo coimmunoprecipitation of mot-2 with p53 and its deletion mutants, the mot-2 binding site of p53 was mapped to its C-terminal amino acid residues 312-352, a region of p53 that includes ... its cytoplasmic sequestration domain. These data demonstrate that cytoplasmic sequestration and inactivation of p53 by mot-2 occurs by its binding to the cytoplasmic sequestration domain. Therefore, perturbation of mot-p53 interactions can be employed to abrogate cytoplasmic retention of wild-type p53 in tumors.
Mesh Terms:
3T3 Cells, Animals, Binding Sites, COS Cells, Cell Compartmentation, Cell Nucleus, Cell Transformation, Neoplastic, Cytoplasm, DNA-Binding Proteins, Gene Expression Regulation, Neoplastic, HSP70 Heat-Shock Proteins, Humans, Mice, Mutation, Neoplasms, Protein Structure, Tertiary, Tumor Cells, Cultured, Tumor Suppressor Protein p53
3T3 Cells, Animals, Binding Sites, COS Cells, Cell Compartmentation, Cell Nucleus, Cell Transformation, Neoplastic, Cytoplasm, DNA-Binding Proteins, Gene Expression Regulation, Neoplastic, HSP70 Heat-Shock Proteins, Humans, Mice, Mutation, Neoplasms, Protein Structure, Tertiary, Tumor Cells, Cultured, Tumor Suppressor Protein p53
Exp. Cell Res.
Date: Apr. 01, 2002
PubMed ID: 11900485
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