The role of SPP/SPPL intramembrane proteases in membrane protein homeostasis

Author:

Mentrup Torben1,Leinung Nadja1,Patel Mehul1,Fluhrer Regina23ORCID,Schröder Bernd1ORCID

Affiliation:

1. Institute for Physiological Chemistry Technische Universität Dresden Germany

2. Biochemistry and Molecular Biology, Institute of Theoretical Medicine, Faculty of Medicine University of Augsburg Germany

3. Center for Interdisciplinary Health Research University of Augsburg Germany

Abstract

Signal peptide peptidase (SPP) and the four SPP‐like proteases SPPL2a, SPPL2b, SPPL2c and SPPL3 constitute a family of aspartyl intramembrane proteases with homology to presenilins. The different members reside in distinct cellular localisations within the secretory pathway and the endo‐lysosomal system. Despite individual cleavage characteristics, they all cleave single‐span transmembrane proteins with a type II orientation exhibiting a cytosolic N‐terminus. Though the identification of substrates is not complete, SPP/SPPL‐mediated proteolysis appears to be rather selective. Therefore, according to our current understanding cleavage by SPP/SPPL proteases rather seems to serve a regulatory function than being a bulk proteolytic pathway. In the present review, we will summarise our state of knowledge on SPP/SPPL proteases and in particular highlight recently identified substrates and the functional and/or (patho)‐physiological implications of these cleavage events. Based on this, we aim to provide an overview of the current open questions in the field. These are connected to the regulation of these proteases at the cellular level but also in context of disease and patho‐physiological processes. Furthermore, the interplay with other proteostatic systems capable of degrading membrane proteins is beginning to emerge.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

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