Review

Journal of Plant Biology

, Volume 54, Issue 5, pp 275-285

Ubiquitin and Ubiquitin-like Modifiers in Plants

  • Hee Jin ParkAffiliated withDivision of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Graduate School of Gyeongsang National University
  • , Hyeong Cheol ParkAffiliated withDivision of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Graduate School of Gyeongsang National University
  • , Sang Yeol LeeAffiliated withDivision of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Graduate School of Gyeongsang National University
  • , Hans J. BohnertAffiliated withDivision of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Graduate School of Gyeongsang National UniversityDepartment of Plant Biology, University of Illinois at Urbana-ChampaignDepartment of Crop Sciences, University of Illinois at Urbana-Champaign
  • , Dae-Jin YunAffiliated withDivision of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Graduate School of Gyeongsang National University Email author 

Rent the article at a discount

Rent now

* Final gross prices may vary according to local VAT.

Get Access

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

Arabidopsis Posttranslational modification Ubiquitination Ubiquitin-like modifiers