Back to Search
Start Over
Signal Peptide Peptidase-Type Proteases: Versatile Regulators with Functions Ranging from Limited Proteolysis to Protein Degradation
- Source :
- Journal of Molecular Biology. 432:5063-5078
- Publication Year :
- 2020
- Publisher :
- Elsevier BV, 2020.
-
Abstract
- Intramembrane proteases catalyze the unusual cleavage of peptide bonds in the plane of biological membranes. They are categorized according to their active site. The GxGD aspartyl proteases comprise presenilin, the signal peptide peptidase (SPP), and SPP-like (SPPL) proteases. Here we focus on the functionally related SPP and SPPL proteases, and review the current understanding of their substrate specificity and summarize known physiological functions in mammalian cells. We discuss how on the one hand regulated intramembrane proteolysis generates signaling molecules, and on the other hand how processes such as endoplasmic reticulum-associated degradation controls the quantity and activity of central regulators. While the enzymatic core of GxGD intramembrane proteases is conserved, association with regulatory factors and substrate adaptors may have tailored enzymes for various specific functions.
- Subjects :
- Proteases
Proteolysis
Protein degradation
Endoplasmic Reticulum
Regulated Intramembrane Proteolysis
Presenilin
03 medical and health sciences
0302 clinical medicine
Structural Biology
Catalytic Domain
medicine
Animals
Aspartic Acid Endopeptidases
Humans
Molecular Biology
Phylogeny
030304 developmental biology
chemistry.chemical_classification
0303 health sciences
medicine.diagnostic_test
Chemistry
Endoplasmic reticulum
Cell Membrane
Protein Transport
Enzyme
Biochemistry
Signal peptide peptidase
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 432
- Database :
- OpenAIRE
- Journal :
- Journal of Molecular Biology
- Accession number :
- edsair.doi.dedup.....78def52d2d9b8d5c1f99092ec8ac4674