intramembrane protease

Four major classes of intramembrane proteases have been discovered:

The other types of intramembrane protease are aspartyl- and metallo-proteases, respectively.

Rhomboids were the first intramembrane proteases for which a high resolution crystal structure was solved.

Proteases of this type are known as intramembrane proteases.

Although only recently discovered, intramembrane proteases are the focus of intense interest because of their major biological functions and their implication in many human diseases.

The different intramembrane protease families are evolutionarily and mechanistically unrelated, but there are clear common functional themes that link them.

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.

Intramembrane proteases are not evolutionarily related to classical soluble proteases, having evolved their catalytic sites by convergent evolution.

Presenilins are a family of related multi-pass transmembrane proteins which constitute the catalytic subunits of the gamma-secretase intramembrane protease complex.

S2P cleaves the transmembrane domain of SREPB, making it a member of the class of intramembrane proteases.

All known intramembrane proteases are themselves integral membrane proteins with multiple transmembrane domains, and they have their active sites buried within the lipid bilayer of cellular membranes.

The protein encoded by the M13/HM13 gene is the signal peptide peptidase (SPP), an ER-resident intramembrane protease.

The structures also explained how a proteolytic reaction, which requires water molecules, can occur in the hydrophobic environment of a lipid bilayer: one of the central mysteries of intramembrane proteases.

Intramembrane proteases (IMPs), also known as intramembrane-cleaving proteases (I-CLiPs), are enzymes that have the property of cleaving transmembrane domains of integral membrane proteins.

We have also discovered a new mechanism for controlling receptor activity by regulated translocation and proteolysis of the ligand by Star and Rhomboid; this has led us to a new family of intramembrane proteases, conserved throughout evolution.