Journal of Plant Biology

, 54:275

Ubiquitin and Ubiquitin-like Modifiers in Plants

Authors

  • Hee Jin Park
    • Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research CenterGraduate School of Gyeongsang National University
  • Hyeong Cheol Park
    • Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research CenterGraduate School of Gyeongsang National University
  • Sang Yeol Lee
    • Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research CenterGraduate School of Gyeongsang National University
  • Hans J. Bohnert
    • Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research CenterGraduate School of Gyeongsang National University
    • Department of Plant BiologyUniversity of Illinois at Urbana-Champaign
    • Department of Crop SciencesUniversity of Illinois at Urbana-Champaign
    • Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research CenterGraduate School of Gyeongsang National University
Review

DOI: 10.1007/s12374-011-9168-5

Cite this article as:
Park, H.J., Park, H.C., Lee, S.Y. et al. J. Plant Biol. (2011) 54: 275. doi:10.1007/s12374-011-9168-5

Abstract

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.

Keywords

ArabidopsisPosttranslational modificationUbiquitinationUbiquitin-like modifiers

Copyright information

© The Botanical Society of Korea 2011