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Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways
Author(s) -
Minina Elena A.,
Moschou Panagiotis N.,
Bozhkov Peter V.
Publication year - 2017
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.14627
Subject(s) - proteolysis , autophagy , proteases , crosstalk , proteasome , microbiology and biotechnology , biology , proteostasis , ubiquitin , protein degradation , biochemistry , deubiquitinating enzyme , chemistry , enzyme , gene , apoptosis , physics , optics
ContentsSummary 958 I. Introduction 958 II. Proteolysis in the early stages of the autophagy pathway 959 III. Sharing tasks: the UPS–autophagy interface 960 IV. Protein degradation as a final step of autophagy: bulk or selective? 962 V. Concluding remarks 962Acknowledgements 962References 963Summary 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.