title: Post-Translational Regulation of miRNA Pathway Components, AGO1 and HYL1, in Plants.
abstract: Post-translational modifications (PTMs) of proteins are essential to increase the functional diversity of the proteome. By adding chemical groups to proteins, or degrading entire proteins by phosphorylation, glycosylation, ubiquitination, neddylation, acetylation, lipidation, and proteolysis, the complexity of the proteome increases, and this then influences most biological processes. Although small RNAs are crucial regulatory elements for gene expression in most eukaryotes, PTMs of small RNA microprocessor and RNA silencing components have not been extensively investigated in plants. To date, several studies have shown that the proteolytic regulation of AGOs is important for host-pathogen interactions. DRB4 is regulated by the ubiquitin-proteasome system, and the degradation of HYL1 is modulated by a de-etiolation repressor, COP1, and an unknown cytoplasmic protease. Here, we discuss current findings on the PTMs of microprocessor and RNA silencing components in plants.
authors.affiliation: Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University 03722, Korea.
authors.forename: Seok Keun
authors.initials: SK
authors.lastname: Cho
authors.affiliation: Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University 03722, Korea.
authors.forename: Moon Young
authors.initials: MY
authors.lastname: Ryu
authors.affiliation: Department of Biomedical Engineering, University of California Irvine, 92697, CA, USA.
authors.forename: Pratik
authors.initials: P
authors.lastname: Shah
authors.affiliation: Carlsberg Research Laboratory, Gl. Carlsberg Vej 4, 1799 Copenhagen V, Denmark.
authors.forename: Christian Peter
authors.initials: CP
authors.lastname: Poulsen
authors.affiliation: Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University 03722, Korea.|Department of Plant and Environmental Sciences, Center for UNIK Synthetic Biology, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg, Denmark.
authors.forename: Seong Wook
authors.initials: SW
authors.lastname: Yang
mesh_terms: D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D060565:Argonaute Proteins / Q000235:genetics / Q000378:metabolism*; D018506:Gene Expression Regulation, Plant; D054884:Host-Pathogen Interactions; D035683:MicroRNAs / Q000235:genetics; D010944:Plants; D011499:Protein Processing, Post-Translational; D059748:Proteolysis; D034622:RNA Interference; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D060565:Argonaute Proteins; C420966:HYL1 protein, Arabidopsis; D035683:MicroRNAs; D016601:RNA-Binding Proteins; D025801:Ubiquitin
keywords: AGO1; HYL1; UPS; autophagy; miRNA; protease; proteolysis