Regulated Intramembrane Proteolysis

Regulated intramembrane proteolysis: from the endoplasmic reticulum to the nucleus.

Regulated intramembrane proteolysis (Rip) is an ancient and widespread process by which cells transmit information from one compartment (the endoplasmic reticulum) to another (the nucleus). Two separate cleavages that are carried out by two separate proteases are required for Rip. The first protease cleaves its protein substrate within an extracytoplasmic domain; the second cleaves it within a ...

Regulated intramembrane proteolysis: signaling pathways and biological functions.

Intramembrane cleavage of transmembrane proteins is a fundamental cellular process. Several enzymes capable of releasing domains of integral membrane proteins have been described. Transmembrane protein proteolytic cleavage is regulated and involved not only in degrading membrane spanning segments but also in generating messengers that elicit biological responses. This review examines the role o...

Long-term Proposal Report Structural Study of Regulated Intramembrane Proteolysis

Regulated Intramembrane Proteolysis (RIP) is a highly conserved signaling mechanism, where a signaling molecule is cleaved within the lipid bilayer by an intramembrane protease. Traditional wisdom argued that proteolysis requires water; however, in RIP, both the protease and the substrate are integral membrane proteins and the cleavage occurs within the hydrophobic lipid bilayer. It has been mo...

Intramembrane Proteolysis of Signal

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