Intramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases.
Intramembrane-cleaving proteases are required for reverse signaling and membrane protein degradation. A major class of these proteases is represented by the GXGD-type aspartyl proteases. GXGD describes a novel signature sequence that distinguishes these proteases from conventional aspartyl proteases. Members of the family of the GXGD-type aspartyl proteases are the Alzheimer disease-related gamma-secretase, the signal peptide peptidases and their homologs, and the bacterial type IV prepilin peptidases. We will describe the major biochemical and functional properties of the signal peptide peptidases and their relatives. We then compare these properties with those of gamma-secretase and discuss common mechanisms but also point out a number of substantial differences.
Fluhrer
Regina
R
Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE) and Adolf Butenandt Institute, Biochemistry, Ludwig-Maximilians University, Munich, 80336 Munich, Germany. regina.fluher@med.uni-muech.de
Steiner
Harald
H
Haass
Christian
C
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology*; D006801:Humans; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational
D016282:Aspartic Acid Endopeptidases; C460085:signal peptide peptidase