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Roles of the intramolecular regions of FE65 in its trans‐accumulation and in p53 stabilization in the nuclear matrix of osmotically stressed cells
Author(s) -
Kawai Tomoko,
Nakaya Tadashi,
Suzuki Toshiharu
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.12.040
Subject(s) - cytoplasm , signal transducing adaptor protein , nuclear export signal , nuclear matrix , chemistry , matrix (chemical analysis) , microbiology and biotechnology , nuclear protein , biophysics , nuclear localization sequence , nuclear pore , cell nucleus , biochemistry , biology , phosphorylation , dna , gene , transcription factor , chromatography , chromatin
The neural adaptor protein FE65 interacts with the amyloid β‐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.