Regulated Intramembrane Proteolysis

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Scopus citations


Regulated intramembrane proteolysis (RIP) is a mechanism for signal transduction that involves the generation of regulatory molecules from membrane proteins through proteolytic cleavage. Such cleavage liberates cytoplasmic or lumenal/extracellular fragments from transmembrane precursor proteins, allowing the cleaved fragments to function at a new location. RIP influences processes as diverse as cellular differentiation, lipid metabolism, immune defense, and the response to unfolded proteins. Proteins that are known to undergo RIP span the membrane bilayer at least once. The intramembrane cleavage of RIP is mediated by four different families of membrane-bound proteases: Site-2 protease (S2P), γ-Secretase, Signal peptide peptidase (SPP), and Rhomboid. In addition to its occurrence in animal cells, RIP has been observed in lower organism including bacteria, and, remarkably, the bacterial proteases are related evolutionarily to the ones used in animal cells.

Original languageEnglish (US)
Title of host publicationEncyclopedia of Biological Chemistry
Subtitle of host publicationSecond Edition
PublisherElsevier Inc.
Number of pages6
ISBN (Electronic)9780123786319
ISBN (Print)9780123786302
StatePublished - Feb 15 2013


  • Alzheimer's disease
  • Cholesterol metabolism
  • Presenilin
  • Protease
  • Regulated intramembrane proteolysis (RIP)
  • Rhomboid
  • Signal-peptide peptidase (SPP)
  • Site-2 protease (S2P)
  • γ-Secretase

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


Dive into the research topics of 'Regulated Intramembrane Proteolysis'. Together they form a unique fingerprint.

Cite this