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Rhomboid protease : ウィキペディア英語版 | Rhomboid protease
The rhomboid proteases are a family of enzymes that exist in almost all species. They are proteases: they cut the polypeptide chain of other proteins. This proteolytic cleavage is irreversible in cells, and an important type of cellular regulation. Although proteases are one of the earliest and best studied class of enzyme, rhomboids belong to a much more recently discovered type: the intramembrane proteases. What is unique about intramembrane proteases is that their active sites are buried in the lipid bilayer of cell membranes, and they cleave other transmembrane proteins within their transmembrane domains.〔Brown, M. S., Ye, J., Rawson, R. B. & Goldstein, J. L. Cell 100, 391-38. (2000)〕 About 30% of all proteins have transmembrane domains, and their regulated processing often has major biological consequences. Accordingly, rhomboids regulate many important cellular processes, and may be involved in a wide range of human diseases. ==Intramembrane proteases==
Rhomboids are intramembrane serine proteases.〔S. Urban, J. R. Lee, M. Freeman, Cell 107, 173 (2001)〕〔Lemberg, M. K. et al. EMBO J. 24, 464-472 (2005〕〔Urban, S. & Wolfe, M. S. Proc. Natl. Acad. Sci. U S A 102, 1883-1888 (2005)〕 The other types of intramembrane protease are aspartyl- and metallo-proteases, respectively. The presenilins and signal peptide peptidase-like family, which are intramembrane aspartyl proteases, cleave substrates that include the Notch receptor and the amyloid precursor protein, which is implicated in Alzheimer's disease. The site-2 protease family, which are intramembrane metalloproteases, regulate among other things cholesterol biosynthesis and stress responses in bacteria. The different intramembrane protease families are evolutionarily and mechanistically unrelated, but there are clear common functional themes that link them. Rhomboids are perhaps the best characterised class.
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