Intramembrane proteases protect from atherosclerosis

Intriguing parasites and intramembrane proteases.

Rhomboid intramembrane proteases occur throughout the kingdoms of life. In this issue of Genes & Development, Baxt and colleagues (pp. 1636-1646) report that the single proteolytic rhomboid (EhROM1) from Entamoeba histolytica cleaves cell surface galactose-binding or N-acetylgalactosamine-binding (Gal/Gal-NAc) lectins. EhROM1 and lectins colocalize during phagocytosis and receptor capping. EhRO...

Sheddases and intramembrane-cleaving proteases: RIPpers of the membrane. Symposium on regulated intramembrane proteolysis.

Intramembrane cleaving proteases (I-CLiPs) as guardians of shuttling proteins

The concept of proteases cleaving their substrates within the hydrophobic core of their transmembrane domains is very well established. in the past 15 years, various intramembrane cleaving proteases (i-CliPs) and their respective substrates have been identified.1 Besides the involvement in specific signaling pathways, for instance regulation of cholesterol metabolism or Notch signaling,1 a prot...

Intramembrane proteolysis by presenilin and presenilin-like proteases.

Regulated intramembrane proteolysis is a novel mechanism involving proteases that hydrolyze their substrates in a hydrophobic environment. Presenilin (PS) 1 and PS 2 are required for intramembrane cleavage of an increasing number of type I membrane proteins, including the amyloid precursor protein of Alzheimer's disease and the Notch receptor, which signals during differentiation and developmen...

The roles of intramembrane proteases in protozoan parasites.

Intramembrane proteolysis is widely conserved throughout different forms of life, with three major types of proteases being known for their ability to cleave peptide bonds directly within the transmembrane domains of their substrates. Although intramembrane proteases have been extensively studied in humans and model organisms, they have only more recently been investigated in protozoan parasite...