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Identity and function of γ‐secretase
Author(s) -
Kimberly W. Taylor,
Wolfe Michael S.
Publication year - 2003
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.10736
Subject(s) - presenilin , nicastrin , proteolysis , amyloid precursor protein secretase , microbiology and biotechnology , membrane protein , amyloid precursor protein , biology , receptor , alpha secretase , protease , gamma secretase , biochemistry , chemistry , alzheimer's disease , disease , enzyme , membrane , medicine , pathology
γ‐Secretase catalyzes intramembrane proteolysis of various type I membrane proteins, including the amyloid‐β precursor protein and the Notch receptor. Despite its importance in the pathogenesis of Alzheimer's disease and to normal development, this protease has eluded identification until only very recently. Four membrane proteins are now known to be members of the protease complex: presenilin, nicastrin, aph‐1, and pen‐2. Recent findings suggest that these four proteins are sufficient to reconstitute the active γ‐secretase complex and that together they mediate the cell surface signaling of a variety of receptors via intramembrane proteolysis. © 2003 Wiley‐Liss, Inc.