Site-2 proteases in prokaryotes: regulated intramembrane proteolysis expands to microbial pathogenesis.
Regulated intramembrane proteolysis (RIP) is a widely distributed mechanism of signal transduction in which membrane-bound proteases cleave transmembrane domains of substrate proteins. The site-2 protease (S2P) class of RIP metalloproteases is present in most bacterial genomes but is generally of unknown function except for the well-characterized proteases RseP and SpoIVFB. In this review we will discuss the biochemical functions and physiologic roles of S2P proteases in bacteria and highlight recent data implicating S2P family members in host-pathogen interactions.
Makinoshima
Hideki
H
Immunology Program, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Glickman
Michael S
MS
D001419:Bacteria / Q000201:enzymology* / Q000472:pathogenicity; D001426:Bacterial Proteins / Q000502:physiology*; D010450:Endopeptidases / Q000502:physiology*; D008565:Membrane Proteins / Q000502:physiology*; D037521:Virulence Factors / Q000502:physiology*
D001426:Bacterial Proteins; D008565:Membrane Proteins; D037521:Virulence Factors; D010450:Endopeptidases