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Review

Ubiquitination modification precisely modulates the ABA signaling pathway in plants

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  • 1. State Key Laboratory of Plant Genomics, National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China
    2. College of Life Science, University of Chinese Academy of Sciences, Beijing 100049, China

Received date: 2017-02-13

  Revised date: 2017-03-24

  Online published: 2017-12-25

Supported by

the National Basic Research Program of China (973 Program)(2011CB915402)

Abstract

Protein post-translational modification by ubiquitination is essential for the activity and stability of proteins in the eukaryotic life cycle. In the past few years, it has been found that ubiquitination subtly modulates the abscisic acid (ABA) signaling pathway to regulate plant growth, development and stress responses, such as drought, salinity and cold stress responses. In this review, how the ubiquitin-proteasome system and ubiquitination-related membrane trafficking pathway affect ABA synthesis and signal transduction will be addressed and analysed. Also, the challenging questions in this field will be raised. These comprehensive views on the regulatory role of ubiquitination modification in the ABA pathway will shed light on future researches on how the ubiquitination-related process affects other hormone signaling pathways.

Cite this article

Feifei Yu,Qi Xie . Ubiquitination modification precisely modulates the ABA signaling pathway in plants[J]. Hereditas(Beijing), 2017 , 39(8) : 692 -706 . DOI: 10.16288/j.yczz.17-043

References

[1] Vierstra RD. The expanding universe of ubiquitin and ubiquitin-like modifiers. Plant Physiol, 2012, 160( 6): 2-14.
[2] Vierstra RD. The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins. Trends Plant Sci, 2003, 8( 3): 135-142.
[3] Smalle J, Vierstra RD. The ubiquitin 26S proteasome proteolytic pathway. Annu Rev Plant Biol, 2004, 55: 555-590.
[4] Lopez-Molina L, Mongrand S, Chua NH. A postgermination developmental arrest checkpoint is mediated by abscisic acid and requires the ABI5 transcription factor in Arabidopsis. Proc Natl Acad Sci USA, 2001, 98( 8): 4782-4787.
[5] Isono E, Nagel MK. Deubiquitylating enzymes and their emerging role in plant biology. Front Plant Sci, 2014, 5: 56.
[6] Qiu JZ, Sheedlo MJ, Yu KW, Tan YH, Nakayasu ES, Das C, Liu XY, Luo ZQ. Ubiquitination independent of E1 and E2 enzymes by bacterial effectors. Nature, 2016, 533( 7601): 120-124.
[7] Vierstra RD. The ubiquitin-26S proteasome system at the nexus of plant biology. Nat Rev Mol Cell Biol, 2009, 10( 6): 385-397.
[8] Yan N, Doelling JH, Falbel TG, Durski AM, Vierstra RD. The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine. Plant Physiol, 2000, 124( 4): 1828-1843.
[9] Hua ZH, Vierstra RD. The cullin-RING ubiquitin-protein ligases. Annu Rev Plant Biol, 2011, 62: 299-334.
[10] Michelle C, Vourc'h P, Mignon L, Andres CR. What was the set of ubiquitin and ubiquitin-like conjugating enzymes in the eukaryote common ancestor? J Mol Evol, 2009, 68( 6): 616-628.
[11] Callis J. The ubiquitination machinery of the ubiquitin system. Arabidopsis Book, 2014, 12: e0174.
[12] Bachmair A, Novatchkova M, Potuschak T, Eisenhaber F. Ubiquitylation in plants: a post-genomic look at a post-translational modification. Trends Plant Sci, 2001, 6( 10): 463-470.
[13] Komander D, Rape M. The ubiquitin code. Annu Rev Biochem, 2012, 81( 1): 203-229.
[14] Hatfield PM, Gosink MM, Carpenter TB, Vierstra RD. The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana. Plant J, 1997, 11( 2): 213-226.
[15] Jin JP, Li X, Gygi SP, Harper JW. Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging. Nature, 2007, 447( 7148): 1135-1138.
[16] Kraft E, Stone SL, Ma L, Su N, Gao Y, Lau OS, Deng XW, Callis J. Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination e
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