Stabilization of ubiquitous mitochondrial creatine kinase preprotein by APP family proteins.

Xiaofan Li 1 Tanja Bürklen 2 Xianglin Yuan 3, 4 Uwe Schlattner 2 Dominic Desiderio 3, 4, 5 Theo Wallimann 2 Ramin Homayouni 3
1 Department of Anatomy and Neurobiology
2 Department of Biology
3 Department of Neurology
4 Charles B. Stout Neuroscience Mass Spectrometry Laboratory
5 Department of Molecular Sciences
Abstract : Amyloid precursor protein (APP) is involved in the pathogenesis of Alzheimer's disease (AD). However, the physiological role of APP and its family members is still unclear. To gain insights into APP function, we used a proteomic approach to identify APP interacting proteins. We report here for the first time a direct interaction between the C-terminal region of APP family proteins and ubiquitous mitochondrial creatine kinase (uMtCK). This interaction was confirmed in vitro as well as in cultured cells and in brain. Interestingly, expression of full-length and C-terminal domain of APP family proteins stabilized uMtCK preprotein in cultured cells. Our data suggest that APP may regulate cellular energy levels and mitochondrial function via a direct interaction and stabilization of uMtCK.
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Molecular and Cellular Neuroscience, Elsevier, 2006, 31 (2), pp.263-72. 〈10.1016/j.mcn.2005.09.015〉
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http://www.hal.inserm.fr/inserm-00390877
Contributeur : Sarah Hamant <>
Soumis le : mardi 2 juin 2009 - 23:19:43
Dernière modification le : mardi 7 juillet 2009 - 11:26:32

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Xiaofan Li, Tanja Bürklen, Xianglin Yuan, Uwe Schlattner, Dominic Desiderio, et al.. Stabilization of ubiquitous mitochondrial creatine kinase preprotein by APP family proteins.. Molecular and Cellular Neuroscience, Elsevier, 2006, 31 (2), pp.263-72. 〈10.1016/j.mcn.2005.09.015〉. 〈inserm-00390877〉

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