| Autor: |
Millar AH; ARC Centre of Excellence in Plant Energy Biology, School of Molecular Sciences, University of Western Australia, Crawley, Western Australia 6009, Australia; email: harvey.millar@uwa.edu.au., Heazlewood JL; School of BioSciences, University of Melbourne, Melbourne, Victoria 3010, Australia; email: jheazlewood@unimelb.edu.au., Giglione C; Institute for Integrative Biology of the Cell, CNRS UMR9198, F-91198 Gif-sur-Yvette Cedex, France; email: carmela.giglione@i2bc.paris-saclay.fr., Holdsworth MJ; School of Biosciences, University of Nottingham, Loughborough LE12 5RD, United Kingdom; email: Michael.Holdsworth@nottingham.ac.uk., Bachmair A; Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, A-1030 Vienna, Austria; email: andreas.bachmair@univie.ac.at., Schulze WX; Systembiologie der Pflanze, Universität Hohenheim, 70599 Stuttgart, Germany; email: wschulze@uni-hohenheim.de. |
| Abstrakt: |
Assessing posttranslational modification (PTM) patterns within protein molecules and reading their functional implications present grand challenges for plant biology. We combine four perspectives on PTMs and their roles by considering five classes of PTMs as examples of the broader context of PTMs. These include modifications of the N terminus, glycosylation, phosphorylation, oxidation, and N-terminal and protein modifiers linked to protein degradation. We consider the spatial distribution of PTMs, the subcellular distribution of modifying enzymes, and their targets throughout the cell, and we outline the complexity of compartmentation in understanding of PTM function. We also consider PTMs temporally in the context of the lifetime of a protein molecule and the need for different PTMs for assembly, localization, function, and degradation. Finally, we consider the combined action of PTMs on the same proteins, their interactions, and the challenge ahead of integrating PTMs into an understanding of protein function in plants. |
