Skip to Main content Skip to Navigation
Journal articles

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

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.
Document type :
Journal articles
Complete list of metadata

https://www.hal.inserm.fr/inserm-00390877
Contributor : Sarah Hamant Connect in order to contact the contributor
Submitted on : Tuesday, June 2, 2009 - 11:19:43 PM
Last modification on : Thursday, May 27, 2021 - 1:54:05 PM

Links full text

Identifiers

Collections

Citation

Xiaofan Li, Tanja Bürklen, Xianglin yuan, Uwe Schlattner, Dominic M. 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⟩

Share

Metrics

Record views

31