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Substrate specificity of gamma-secretase and other intramembrane proteases Beel AJ; Sanders CRCell Mol Life Sci 2008[May]; 65 (9): 1311-34Gamma-Secretase is a promiscuous protease that cleaves bitopic membrane proteins within the lipid bilayer. Elucidating both the mechanistic basis of gamma-secretase proteolysis and the precise factors regulating substrate identification is important because modulation of this biochemical degradative process can have important consequences in a physiological and pathophysiological context. Here, we briefly review such information for all major classes of intramembranously cleaving proteases (I-CLiPs), with an emphasis on gamma-secretase, an I-CLiP closely linked to the etiology of Alzheimer's disease. A large body of emerging data allows us to survey the substrates of gamma-secretase to ascertain the conformational features that predispose a peptide to cleavage by this enigmatic protease. Because substrate specificity in vivo is closely linked to the relative subcellular compartmentalization of gamma-secretase and its substrates, we also survey the voluminous body of literature concerning the traffic of gamma-secretase and its most prominent substrate, the amyloid precursor protein.|Amino Acid Sequence[MESH]|Amyloid Precursor Protein Secretases/analysis/chemistry/*metabolism[MESH]|Amyloid beta-Protein Precursor/metabolism[MESH]|Animals[MESH]|Aspartic Acid Endopeptidases/chemistry/metabolism[MESH]|Cell Membrane/*enzymology[MESH]|Membrane Microdomains/enzymology[MESH]|Metalloproteases/chemistry/metabolism[MESH]|Molecular Sequence Data[MESH]|Peptide Hydrolases/*metabolism[MESH]|Serine Endopeptidases/chemistry/metabolism[MESH]|Substrate Specificity[MESH] |
