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Alpha‐ and beta‐ cleavages of the amino‐terminus of the cellular prion protein
Author(s) -
Mangé Alain,
Béranger Florence,
Peoc’h Katell,
Onodera Takashi,
Frobert Yveline,
Lehmann Sylvain
Publication year - 2004
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/j.biolcel.2003.11.007
Subject(s) - cleavage (geology) , gene isoform , biology , n terminus , c terminus , microbiology and biotechnology , peptide sequence , biochemistry , amino acid , gene , paleontology , fracture (geology)
It is commonly assumed that the physiological isoform of prion protein, PrP C , is cleaved during its normal processing between residues 111/112, whereas the pathogenic isoform, PrP Sc , is cleaved at an alternate site in the octapeptide repeat region around position 90. Here we demonstrated both in cultured cells and in vivo , that PrP C is subject to a complex set of post‐translational processing with the molecule being cleaved upstream of position 111/112, in the octapeptide repeat region or at position 96. PrP has therefore two main cleavage sites that we decided to name α and β. Cleavage of PrP C at these sites leads us to re‐evaluate the function of both N‐ and C‐terminus fragments thus generated.