PrPC interacts with tetraspanin-7 through bovine PrP154-182 containing alpha-helix 1.
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.
Guo
Mingxiong
M
The State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.
Huang
Tao
T
Cui
Yejian
Y
Pan
Baiqun
B
Shen
Ao
A
Sun
Yuting
Y
Yi
Yourong
Y
Wang
Yan
Y
Xiao
Gengfu
G
Sun
Guihong
G
D000818:Animals; D002417:Cattle; D002460:Cell Line; D018076:DNA, Complementary / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D018621:PrPC Proteins / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D020798:Two-Hybrid System Techniques
D018076:DNA, Complementary; D008565:Membrane Proteins; D010446:Peptide Fragments; D018621:PrPC Proteins