scholarly journals Why cells need intramembrane proteases - a mechanistic perspective

FEBS Journal ◽  
2016 ◽  
Vol 283 (10) ◽  
pp. 1837-1845 ◽  
Author(s):  
Kvido Strisovsky
Science ◽  
2002 ◽  
Vol 296 (5576) ◽  
pp. 2156-2157 ◽  
Author(s):  
M. S. Wolfe

2014 ◽  
Vol 34 (8) ◽  
pp. 1398-1411 ◽  
Author(s):  
J. Schneppenheim ◽  
S. Huttl ◽  
T. Mentrup ◽  
R. Lullmann-Rauch ◽  
M. Rothaug ◽  
...  

2017 ◽  
Vol 96 (5) ◽  
pp. 372-382 ◽  
Author(s):  
Torben Mentrup ◽  
Regina Fluhrer ◽  
Bernd Schröder

2015 ◽  
Vol 10 (11) ◽  
pp. 2423-2434 ◽  
Author(s):  
Minh T. N. Nguyen ◽  
Tim Van Kersavond ◽  
Steven H. L. Verhelst

2017 ◽  
Vol 398 (4) ◽  
pp. 441-453 ◽  
Author(s):  
Dieter Langosch ◽  
Harald Steiner

Abstract Intramembrane proteases comprise a number of different membrane proteins with different types of catalytic sites. Their common denominator is cleavage within the plane of the membrane, which usually results in peptide bond scission within the transmembrane helices of their substrates. Despite recent progress in the determination of high-resolution structures, as illustrated here for the γ-secretase complex and its substrate C99, it is still unknown how these enzymes function and how they distinguish between substrates and non-substrates. In principle, substrate/non-substrate discrimination could occur at the level of substrate binding and/or cleavage. Focusing on the γ-secretase/C99 pair, we will discuss recent observations suggesting that global motions within a substrate transmembrane helix may be much more important for defining a substrate than local unraveling at cleavage sites.


Nature ◽  
2009 ◽  
Vol 459 (7245) ◽  
pp. 371-378 ◽  
Author(s):  
Elinor Erez ◽  
Deborah Fass ◽  
Eitan Bibi

2021 ◽  
Author(s):  
Claudia Bohg ◽  
Carl Öster ◽  
Tillmann Utesch ◽  
Susanne Bischoff ◽  
Sascha Lange ◽  
...  

Intramembrane proteolysis plays a fundamental role in many biological and pathological processes. Intramembrane proteases thus represent promising pharmacological targets, but few selective inhibitors have been identified. This is in contrast...


2017 ◽  
Author(s):  
Małgorzata Adamiec ◽  
Lucyna Misztal ◽  
Robert Luciński

ABSTRACTThe process of proteolysis is a factor involved in control of the proper development of the plant and its responses to a changeable environment. Recent research has shown that proteases are not only engaged in quality control and protein turnover processes but also participate in the process which is known as regulated membrane proteolysis (RIP). Four families of integral membrane proteases, belonging to three different classes, have been identified: serine intramembrane proteases known as rhomboid proteases, site-2 proteases belonging to zinc metalloproteases, and two families of aspartic proteases: presenilins and signal peptide peptidases. The studies concerning intramembrane proteases in higher plants are, however, focused on Arabidopsis thaliana. The aim of the study was to identify and retrieve protein sequences of intramembrane protease homologs from other higher plant species and perform a detailed analysis of their primary sequences as well as their phylogenetic relations. This approach allows us to indicate several previously undescribed issues which may provide important directions for further research.


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