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How intramembrane proteases bury hydrolytic reactions in the membrane

Author

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  • Elinor Erez

    (Department of Biological Chemistry)

  • Deborah Fass

    (Weizmann Institute of Science)

  • Eitan Bibi

    (Department of Biological Chemistry)

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.

Suggested Citation

  • Elinor Erez & Deborah Fass & Eitan Bibi, 2009. "How intramembrane proteases bury hydrolytic reactions in the membrane," Nature, Nature, vol. 459(7245), pages 371-378, May.
    • Handle: RePEc:nat:nature:v:459:y:2009:i:7245:d:10.1038_nature08146
    DOI: 10.1038/nature08146
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