Intramembrane protease

From Wikipedia, the free encyclopedia
Jump to: navigation, search

Intramembrane proteases (IMPs), also known as intramembrane-cleaving proteases (I-CLiPs), are enzymes that have the property of cleaving transmembrane domains of integral membrane proteins.[1][2][3] All known intramembrane proteases are themselves integral membrane proteins with multiple transmembrane domains, and they have their active sites buried within the lipid bilayer of cellular membranes.[4]

Intramembrane proteases are not evolutionarily related to classical soluble proteases, having evolved their catalytic sites by convergent evolution.[5][6]

Although only recently discovered, intramembrane proteases are the focus of intense interest because of their major biological functions and their implication in many human diseases.

Classification[edit]

Four major classes of intramembrane proteases have been discovered:[7]

References[edit]

  1. ^ Brown, MS; Ye, J; Rawson, RB; Goldstein, JL (18 February 2000). "Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans.". Cell. 100 (4): 391–8. doi:10.1016/S0092-8674(00)80675-3. PMID 10693756. 
  2. ^ Urban, S; Freeman, M (October 2002). "Intramembrane proteolysis controls diverse signalling pathways throughout evolution.". Current opinion in genetics & development. 12 (5): 512–8. doi:10.1016/s0959-437x(02)00334-9. PMID 12200155. 
  3. ^ Wolfe, MS; Kopan, R (20 August 2004). "Intramembrane proteolysis: theme and variations.". Science. 305 (5687): 1119–23. doi:10.1126/science.1096187. PMID 15326347. 
  4. ^ Erez, E; Fass, D; Bibi, E (21 May 2009). "How intramembrane proteases bury hydrolytic reactions in the membrane.". Nature. 459 (7245): 371–8. doi:10.1038/nature08146. PMID 19458713. 
  5. ^ Koonin, EV; Makarova, KS; Rogozin, IB; Davidovic, L; Letellier, MC; Pellegrini, L (2003). "The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers.". Genome Biology. 4 (3): R19. PMID 12620104. 
  6. ^ Lemberg, M. K.; Freeman, M. (1 November 2007). "Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases". Genome Research. 17 (11): 1634–1646. doi:10.1101/gr.6425307. PMC 2045146Freely accessible. PMID 17938163. 
  7. ^ Wolfe, M. S. (3 February 2009). "Intramembrane-cleaving Proteases". Journal of Biological Chemistry. 284 (21): 13969–13973. doi:10.1074/jbc.R800039200. 
  8. ^ Rawson, RB; Zelenski, NG; Nijhawan, D; Ye, J; Sakai, J; Hasan, MT; Chang, TY; Brown, MS; Goldstein, JL (December 1997). "Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs.". Molecular Cell. 1 (1): 47–57. doi:10.1016/s1097-2765(00)80006-4. PMID 9659902. 
  9. ^ Wolfe, MS; Xia, W; Ostaszewski, BL; Diehl, TS; Kimberly, WT; Selkoe, DJ (8 April 1999). "Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity.". Nature. 398 (6727): 513–7. doi:10.1038/19077. PMID 10206644. 
  10. ^ De Strooper, B; Annaert, W; Cupers, P; Saftig, P; Craessaerts, K; Mumm, JS; Schroeter, EH; Schrijvers, V; Wolfe, MS; Ray, WJ; Goate, A; Kopan, R (8 April 1999). "A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain.". Nature. 398 (6727): 518–22. doi:10.1038/19083. PMID 10206645. 
  11. ^ Weihofen, A; Binns, K; Lemberg, MK; Ashman, K; Martoglio, B (21 June 2002). "Identification of signal peptide peptidase, a presenilin-type aspartic protease.". Science. 296 (5576): 2215–8. doi:10.1126/science.1070925. PMID 12077416. 
  12. ^ Friedmann, E; Hauben, E; Maylandt, K; Schleeger, S; Vreugde, S; Lichtenthaler, SF; Kuhn, PH; Stauffer, D; Rovelli, G; Martoglio, B (August 2006). "SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production.". Nature Cell Biology. 8 (8): 843–8. doi:10.1038/ncb1440. PMID 16829952. 
  13. ^ Urban, S; Lee, JR; Freeman, M (19 October 2001). "Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases.". Cell. 107 (2): 173–82. doi:10.1016/s0092-8674(01)00525-6. PMID 11672525.