Literature DB >> 28574164

Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways.

Elena A Minina1, Panagiotis N Moschou2, Peter V Bozhkov1.   

Abstract

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.
© 2017 The Authors. New Phytologist © 2017 New Phytologist Trust.

Entities:  

Keywords:  autophagy; autophagy-related (ATG) proteins; limited proteolysis; pexophagy; proteases; proteophagy; ubiquitin code; ubiquitin-proteasome system (UPS)

Mesh:

Substances:

Year:  2017        PMID: 28574164     DOI: 10.1111/nph.14627

Source DB:  PubMed          Journal:  New Phytol        ISSN: 0028-646X            Impact factor:   10.151


  12 in total

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