The intramembrane proteases SPPL2a and SPPL2b regulate the homeostasis of selected SNARE proteins
Author:
Affiliation:
1. Biochemical Institute Christian Albrechts University Kiel Kiel Germany
2. Institute of Physiological Chemistry Technische Universität Dresden Dresden Germany
3. Department of Molecular Biology University Medical Center Göttingen Göttingen Germany
Funder
Deutsche Forschungsgemeinschaft
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.16610
Reference63 articles.
1. Signal peptide peptidase-like 2 proteases: Regulatory switches or proteasome of the membrane?
2. Physiological functions of SPP/SPPL intramembrane proteases
3. Shedding of glycan‐modifying enzymes by signal peptide peptidase‐like 3 ( SPPL 3) regulates cellular N‐glycosylation
4. Secretome Analysis Identifies Novel Signal Peptide Peptidase-Like 3 (SPPL3) Substrates and Reveals a Role of SPPL3 in Multiple Golgi Glycosylation Pathways*
5. Foamy Virus Envelope Protein Is a Substrate for Signal Peptide Peptidase-like 3 (SPPL3)
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1. In vitro cleavage of tumor necrosis factor α (TNFα) by Signal-Peptide-Peptidase-like 2b (SPPL2b) resembles mechanistic principles observed in the cellular context;Chemico-Biological Interactions;2024-05
2. Structure and function of SPP/SPPL proteases: insights from biochemical evidence and predictive modeling;The FEBS Journal;2023-10-13
3. Dynamic association of the intramembrane proteases SPPL2a/b and their substrates with tetraspanin-enriched microdomains;iScience;2023-10
4. The role of SPP/SPPL intramembrane proteases in membrane protein homeostasis;The FEBS Journal;2023-09-05
5. The transmembrane domain of Frey1 harbors a transplantable inhibitory motif for intramembrane proteases;Cellular and Molecular Life Sciences;2023-06
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