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Signal peptide peptidase-type proteases: versatile regulators with functions ranging from limited proteolysis to protein degradation

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 f...

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Bibliographic Details
Main Authors: Lipp, Sara Suna (Author) , Lemberg, Marius (Author)
Format: Article (Journal)
Language:English
Published: 26 May 2020
In: Journal of molecular biology
Year: 2020, Volume: 432, Issue: 18, Pages: 5063-5078
ISSN:1089-8638
DOI:10.1016/j.jmb.2020.05.014
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.jmb.2020.05.014
Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0022283620303557
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Author Notes:Sara Suna Yücel and Marius K. Lemberg
Description
Summary: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.
Item Description:Gesehen am 24.09.2020
Physical Description:Online Resource
ISSN:1089-8638
DOI:10.1016/j.jmb.2020.05.014

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