title: How intramembrane proteases bury hydrolytic reactions in the membrane.
abstract: Intramembrane proteolysis is increasingly seen as a regulatory step in a range of diverse processes, including development, organelle shaping, metabolism, pathogenicity and degenerative disease. Initial scepticism over the existence of intramembrane proteases was soon replaced by intense exploration of their catalytic mechanisms, substrate specificities, regulation and structures. Crystal structures of metal-dependent and serine intramembrane proteases have revealed active sites embedded in the plane of the membrane but accessible by water, a requirement for hydrolytic reactions. Efforts to understand how these membrane-bound proteases carry out their reactions have started to yield results.
authors.affiliation: Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Elinor
authors.initials: E
authors.lastname: Erez
authors.forename: Deborah
authors.initials: D
authors.lastname: Fass
authors.forename: Eitan
authors.initials: E
authors.lastname: Bibi
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D008565:Membrane Proteins / Q000378:metabolism*; D045726:Metalloproteases / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D008565:Membrane Proteins; D045726:Metalloproteases; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D016282:Aspartic Acid Endopeptidases