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Study on interaction between microtubule associated protein tau and prion protein
Authors:HAN Jun  ZHANG Jin  YAO Hailan  WANG Xiaofan  LI Feng  CHEN Lan  GAO Chen  GAO Jianmei  NIE Kai  ZHOU Wei  DONG Xiaoping
Institution:1. State Key Laboratory for Infectious Diseases Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China
2. State Key Laboratory for Infectious Diseases Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China;School of Medicine, Xi'an Jiao-Tong University, Xi'an 710061, China
3. State Key Laboratory for Infectious Diseases Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China;Tong-Ji Medical College, Hua-Zhong University of Science and Technology, Wuhan 430030, China
4. State Key Laboratory for Infectious Diseases Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China;National Laboratory of Medical Molecular Biology, Institute of Basic Medical Science, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100005, China
Abstract:Microtubule-associated protein tau is considered to play roles in many neurodegenerative diseases including some transmissible spongiform encephalopathies. To address the possible molecular linkage of prion protein (PrP) and tau, a GST-fusion segment of human tau covering the three-repeat region and various PrP segments was used in the tests of GST pull-down and immunoprecipitation. We found tau protein interacted with various style prion proteins such as native prion protein (PrPC) or protease-resistant isoform (prpSc). Co-localization signals of tau and PrP were found in the CHO cell tranfected with both PrP and tau gene. The domain of interaction with tau was located at N-terminal of PrP (residues 23 to 91). The evidence of molecular interactions between PrP and tau protein highlights a potential role of tau in the biological function of PrP and the pathogenesis of TSEs.
Keywords:tau  PrP  interaction
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