Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1936882 | Biochemical and Biophysical Research Communications | 2008 | 4 Pages |
Abstract
The cellular prion protein (PrPC) is highly conserved in the evolution of mammals, and therefore, thought to have important cellular functions. Despite decades of intensive research, the physiological function of PrPC remains enigmatic. We carried out a yeast two-hybrid screen on a bovine brain cDNA expression library and identified the transmembrane protein tetraspanin-7 (CD231), as a PrPC interacting protein. We confirmed the interaction between PrPC and tetraspanin-7 by yeast two-hybrid assay, immunofluorescent co-localization, and immunocoprecipitation. Our mutational studies further demonstrated that PrPC specifically binds tetraspanin-7 through the region corresponding to bovine PrP154–182 containing alpha-helix 1.
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Authors
Mingxiong Guo, Tao Huang, Yejian Cui, Baiqun Pan, Ao Shen, Yuting Sun, Yourong Yi, Yan Wang, Gengfu Xiao, Guihong Sun,