Signal Peptide Peptidase-Type Proteases: Versatile Regulators with Functions Ranging from Limited Proteolysis to Protein Degradation
| Autor: | Marius K. Lemberg, Sara Suna Yucel |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
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 |
| Zdroj: | Journal of Molecular Biology. 432:5063-5078 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2020.05.014 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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