Ubiquitin and Ubiquitin-like Modifiers in Plants

• Published in: Journal of plant biology = Singmul Hakhoe chi Vol. 54; no. 5; pp. 275 - 285
• Main Authors: Park, H.J., Graduate School of Gyeongsang National University, Jinju, Republic of Korea, Park, H.C., Graduate School of Gyeongsang National University, Jinju, Republic of Korea, Lee, S.Y., Graduate School of Gyeongsang National University, Jinju, Republic of Korea, Bohnert, Hans J., Graduate School of Gyeongsang National University, Jinju, Republic of Korea, Yun, D.J., Graduate School of Gyeongsang National University, Jinju, Republic of Korea
• Format: Journal Article
• Language: English
• Published: New York Springer-Verlag 01.10.2011; Springer Nature B.V; 한국식물학회
• Subjects: Amino acids; ARABIDOPSIS; Autophagy; Binding sites; Biodegradation; Biomedical and Life Sciences; Conjugation; Degradation; Enzymes; Flowering; Genes; Homology; Kinases; Life Sciences; Plant Breeding/Biotechnology; Plant Ecology; Plant Genetics and Genomics; Plant growth; Plant Sciences; Plant Systematics/Taxonomy/Biogeography; Polypeptides; Posttranslational modification; Proteasomes; Protein interaction; Proteins; Review; SUMO protein; Transcription factors; Ubiquitin-like modifiers; Ubiquitin-protein ligase; Ubiquitination; 생물학; Posttranslational modification; Ubiquitin-like modifiers; Ubiquitination
• ISSN: 1226-9239; 1867-0725
• DOI: 10.1007/s12374-011-9168-5

Posttranslational modifications of proteins by small polypeptides including ubiquitination, neddylation (related to ubiquitin (RUB) conjugation), and sumoylation are implicated in plant growth and development, and they regulate protein degradation, location, and interaction with other proteins. Ubiquitination mediates the selective degradation of proteins by the ubiquitin (Ub)/proteasome pathway. The ubiquitin-like protein RUB is conjugated to cullins, which are part of a ubiquitin E3 ligase complex that is involved in auxin hormonal signaling. Sumoylation, by contrast, is known for its involvement in guiding protein interactions related to abiotic and biotic stresses and in the regulation of flowering time. ATG8/ATG12-mediated autophagy influences degradation and recycling of cellular components. Other ubiquitin-like modifiers (ULPs) such as homology to Ub-1, ubiquitin-fold modifier 1, and membrane-anchored Ub-fold are also found in Arabidopsis. ULPs share similar three-dimensional structures and a conjugation system, including E1 activating enzymes, E2 conjugation enzymes, and E3 ligases, as well as proteases for deconjugation and recycling of the tags. However, each of the ULP posttranslational modifications possesses its own specific enzymes and modifies its specific targets selectively. This review discusses recent findings on ubiquitination and ubiquitin-like modifier processes and their roles in the posttranslational modification of proteins in Arabidopsis.