Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways.

New Phytol 2017 Aug 2;215(3):958-964. Epub 2017 Jun 2.

Department of Molecular Sciences, Uppsala BioCenter, Swedish University of Agricultural Sciences and Linnean Center for Plant Biology, PO Box 7015, SE-75007, Uppsala, Sweden.

Contents 958 I. 958 II. 959 III. 960 IV. 962 V. 962 962 References 963 SUMMARY: Proteases can either digest target proteins or perform the so-called 'limited proteolysis' by cleaving polypeptide chains at specific site(s). Autophagy and the ubiquitin-proteasome system (UPS) are two main mechanisms carrying out digestive proteolysis. While the net outcome of digestive proteolysis is the loss of function of protein substrates, limited proteolysis can additionally lead to gain or switch of function. Recent evidence of crosstalk between autophagy, UPS and limited proteolysis indicates that these pathways are parts of the same proteolytic nexus. Here, we focus on three emerging themes within this area: limited proteolysis as a mechanism modulating autophagy; interplay between autophagy and UPS, including autophagic degradation of proteasomes (proteophagy); and specificity of protein degradation during bulk autophagy.

Download full-text PDF

Source
http://dx.doi.org/10.1111/nph.14627DOI Listing
August 2017
52 Reads

Publication Analysis

Top Keywords

limited proteolysis
12
digestive proteolysis
12
962 962
8
proteolysis
6
autophagy
5
themes area
4
area limited
4
main mechanisms
4
limited
4
net outcome
4
proteolysis net
4
system main
4
carrying digestive
4
mechanisms carrying
4
autophagy ubiquitin-proteasome
4
modulating autophagy
4
parts proteolytic
4
cleaving polypeptide
4
autophagy interplay
4
chains specific
4

Similar Publications