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Life and death of proteins after protease cleavage: protein degradation by the N‐end rule pathway
Author(s) -
Dissmeyer Nico,
Rivas Susana,
Graciet Emmanuelle
Publication year - 2018
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.14619
Subject(s) - proteases , proteomics , proteome , biology , protease , computational biology , protein degradation , proteolysis , bottleneck , microbiology and biotechnology , bioinformatics , biochemistry , enzyme , computer science , gene , embedded system
ContentsSummary 929 I. Introduction: conservation and diversity of N‐end rule pathways 929 II. Defensive functions of the N‐end rule pathway in plants 930 III. Proteases and degradation by the N‐end rule pathway 930 IV. New proteomics approaches for the identification of N‐end rule substrates 932 V. Concluding remarks 932Acknowledgements 934References 934Summary The N‐end rule relates the stability of a protein to the identity of its N‐terminal residue and some of its modifications. Since its discovery in the 1980s, the repertoire of N‐terminal degradation signals has expanded, leading to a diversity of N‐end rule pathways. Although some of these newly discovered N‐end rule pathways remain largely unexplored in plants, recent discoveries have highlighted roles of N‐end rule‐mediated protein degradation in plant defense against pathogens and in cell proliferation during organ growth. Despite this progress, a bottleneck remains the proteome‐wide identification of N‐end rule substrates due to the prerequisite for endoproteolytic cleavage and technical limitations. Here, we discuss the recent diversification of N‐end rule pathways and their newly discovered functions in plant defenses, stressing the role of proteases. We expect that novel proteomics techniques (N‐terminomics) will be essential for substrate identification. We review these methods, their limitations and future developments.