TAILIEUCHUNG - Báo cáo khoa học: Metabolic stabilization of p53 by FE65 in the nuclear matrix of osmotically stressed cells

FE65 is a neural adaptor protein known to interact with a number of pro-teins, including Alzheimer’s amyloid b-protein precursor (APP). Although several different functions have been proposed for FE65, its primary physi-ological role remains unclear. We previously showed that APP can liberate FE65 from the membrane as a result of APP phosphorylation, and that the liberated FE65 translocates into the nuclei of osmotically stressed cells. | Metabolic stabilization of p53 by FE65 in the nuclear matrix of osmotically stressed cells Tadashi Nakaya Tomoko Kawai and Toshiharu Suzuki Laboratory of Neuroscience Graduate Schoolof PharmaceuticalSciences Hokkaido University Sapporo Japan Keywords amyloid b-protein precursor APP FE65 p53 phosphorylation cH2AX Correspondence T. Suzuki Laboratory of Neuroscience Graduate School of Pharmaceutical Sciences Hokkaido University Kita-12 Nishi-6 Kita-ku Sapporo 060-0812 Japan Fax 81 11 706 4991 Tel 81 11 706 3250 E-mail tsuzuki@ Received 4 July 2009 revised 30 August 2009 accepted 3 September 2009 doi FE65 is a neural adaptor protein known to interact with a number of proteins including Alzheimer s amyloid b-protein precursor APP . Although several different functions have been proposed for FE65 its primary physiological role remains unclear. We previously showed that APP can liberate FE65 from the membrane as a result of APP phosphorylation and that the liberated FE65 translocates into the nuclei of osmotically stressed cells. Within the nucleus FE65 formed a patched structure at the nuclear matrix which facilitated the induction of yH2AX Nakaya T Kawai T Suzuki T 2008 J Biol Chem 283 19119-19131 . Here we report that the tumor suppressor p53 is colocalized with FE65 in the nuclear patches and is stabilized by FE65 in sorbitol-treated cells. In FE65 knockdown cells protein levels of p53 targeted to the nuclear matrix were rapidly decreased through the proteasome degradation pathway after sorbitol treatment as compared with control cells. These results suggest that the translocation of FE65 to the nuclear matrix along with the formation of nuclear patches is required for the stabilization of p53 by its suppression of the proteasome degradation pathway thus facilitating the subsequent induction of cH2AX in osmotically stressed cells. Structured digital abstract MINT-7261896 Fe65 uniprotkb Q9QXJ1 and Tp53 uniprotkb .

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