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Probing γ‐secretase–substrate interactions at the single amino acid residue level
Author(s) -
ChávezGutiérrez Lucía,
De Strooper Bart
Publication year - 2016
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.201694978
Subject(s) - biology , proteolysis , amyloid precursor protein secretase , cleavage (geology) , substrate specificity , biochemistry , microbiology and biotechnology , enzyme , biophysics , amyloid precursor protein , disease , alzheimer's disease , medicine , paleontology , pathology , fracture (geology)
Intramembrane proteolysis by γ‐secretases plays major roles in disease pathology and cellular signalling, yet the dynamics of these enzyme complexes and how they recognize substrates remains poorly understood. New work in The EMBO Journal utilizes photo‐affinity cross‐linking to map APP interactions to different γ‐secretase subunits, suggesting a succession of recruitment and engagement steps that lead up to substrate cleavage.