Carbon and nitrogen metabolism regulated by the ubiquitin-proteasome system

• Published in: Plant signaling & behavior Vol. 6; no. 10; pp. 1465 - 1468
• Main Authors: Sato, Takeo, Maekawa, Shugo, Yasuda, Shigetaka, Yamaguchi, Junji
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 01-10-2011; Landes Bioscience
• Subjects: 14-3-3 Proteins - metabolism; Arabidopsis - metabolism; Binding; Biology; Bioscience; Calcium; Cancer; Carbon - metabolism; Cell; Cycle; Germination - physiology; Landes; Mini-Review; Models, Biological; Nitrogen - metabolism; Organogenesis; Proteasome Endopeptidase Complex - metabolism; Protein Transport; Proteins; Signal Transduction; Ubiquitin - metabolism; Ubiquitin-Protein Ligases - metabolism
• ISSN: 1559-2316; 1559-2324; 1559-2324
• DOI: 10.4161/psb.6.10.17343

The ubiquitin-proteasome system (UPS) is a unique protein degradation mechanism conserved in the eukaryotic cell. In addition to the control of protein quality, UPS regulates diverse cellular signal transduction via the fine-tuning of target protein degradation. Protein ubiquitylation and subsequent degradation by the 26S proteasome are involved in almost all aspects of plant growth and development and response to biotic and abiotic stresses. Recent studies reveal that the UPS plays an essential role in adaptation to carbon and nitrogen availability in plants. Here we highlight ubiquitin ligase ATL31 and the homologue ATL6 target 14-3-3 proteins for ubiquitylation to be degraded, which control signaling for carbon and nitrogen metabolisms and C/N balance response. We also give an overview of the UPS function involved in carbon and nitrogen metabolisms.