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O2–03–02: Role of the transmembrane GxxxG motifs in the processing of human APP
Author(s) -
Kienlen-Campard Pascal,
Constantinescu Stefan N.,
Tasiaux Bernadette,
Smith Steven O.,
Octave Jean-Noël
Publication year - 2006
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2006.05.121
Subject(s) - transmembrane domain , amyloid precursor protein , presenilin , transmembrane protein , immunoprecipitation , nicastrin , mutant , amyloid precursor protein secretase , microbiology and biotechnology , biochemistry , chemistry , multiprotein complex , intracellular , alanine , membrane protein , biology , amino acid , gene , medicine , receptor , disease , pathology , membrane , alzheimer's disease
specific for APP. They had little or no effect on the shedding of other membrane proteins undergoing an -secretase like cleavage, such as TNFreceptor 2 and L-selectin. Interestingly, the novel protein SNX31 is a phospho-protein, suggesting that phosphorylation of SNX31 may act as a molecular switch controlling APP trafficking and shedding. Conclusion: The mechanistic study of the novel proteins highlights the particular importance of APP trafficking as a prime modulator of APP shedding and access of APP to its secretases. These proteins may open new ways for therapeutically interfering with APP shedding and A -peptide generation.