Roles of the intramolecular regions of FE65 in its trans-accumulation and in p53 stabilization in the nuclear matrix of osmotically stressed cells.
The neural adaptor protein FE65 interacts with the amyloid beta-protein precursor (APP). In osmotically stressed cells, the membrane APP-tethered FE65 is released into the cytoplasm and translocates to the nuclear matrix, where it stabilizes p53 via a non-canonical pathway. In this study, we found that the second phosphotyrosine interaction domain (PI2) of FE65 mediated its trans-accumulation in the nuclear matrix of osmotically stressed cells. The carboxyl-terminal half of FE65, which contains the PI2 domain, failed to stabilize p53, suggesting that the amino-terminal half of the protein plays an important role in the stabilization of p53 in osmotically stressed cells.
Kawai
Tomoko
T
Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Sapporo, Japan.
Nakaya
Tadashi
T
Suzuki
Toshiharu
T
D000818:Animals; D001665:Binding Sites / Q000235:genetics; D045744:Cell Line, Tumor; D002470:Cell Survival / Q000187:drug effects / Q000502:physiology; D015151:Immunoblotting; D051379:Mice; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D015530:Nuclear Matrix / Q000187:drug effects / Q000378:metabolism*; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D009997:Osmotic Pressure; D013012:Sorbitol / Q000494:pharmacology; D014162:Transfection; D016159:Tumor Suppressor Protein p53 / Q000235:genetics / Q000378:metabolism*
C486243:Apbb1 protein, mouse; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D016159:Tumor Suppressor Protein p53; D013012:Sorbitol