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. 2008 Jan 4;365(1):154-7.
doi: 10.1016/j.bbrc.2007.10.160. Epub 2007 Nov 5.

PrPC interacts with tetraspanin-7 through bovine PrP154-182 containing alpha-helix 1

Mingxiong Guo  1 , Tao Huang, Yejian Cui, Baiqun Pan, Ao Shen, Yuting Sun, Yourong Yi, Yan Wang, Gengfu Xiao, Guihong Sun
Affiliations

PrPC interacts with tetraspanin-7 through bovine PrP154-182 containing alpha-helix 1

Mingxiong Guo et al. Biochem Biophys Res Commun. .

Abstract

The cellular prion protein (PrP(C)) 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 PrP(C) 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 PrP(C) interacting protein. We confirmed the interaction between PrP(C) and tetraspanin-7 by yeast two-hybrid assay, immunofluorescent co-localization, and immunocoprecipitation. Our mutational studies further demonstrated that PrP(C) specifically binds tetraspanin-7 through the region corresponding to bovine PrP(154-182) containing alpha-helix 1.

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