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Cited by 371

The DOI matches its Crossref record; 82 of the 82 references it cites were found in a registry or an index.

Protein Language: Post-Translational Modifications Talking to Each Other

Vu, Lam Dai, Gevaert, Kris, De Smet, Ive·2018·Trends in Plant Science
DOI 10.1016/j.tplants.2018.09.004
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Abstract

Post-translational modifications (PTMs) are at the heart of many cellular signaling events. Apart from a single regulatory PTM, there are also PTMs that function in orchestrated manners. Such PTM crosstalk usually serves as a fine-tuning mechanism to adjust cellular responses to the slightest changes in the environment. While PTM crosstalk has been studied in depth in various species; in plants, this field is just emerging. In this review, we discuss recent studies on crosstalk between three of the most common protein PTMs in plant cells, being phosphorylation, ubiquitination, and sumoylation, and we highlight the diverse underlying mechanisms as well as signaling outputs of such crosstalk.

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Cites

Show all 82 references

Research works printed but not linked: 19

  1. Tomanov, 2018, Sumoylation and phosphorylation: hidden and overt links, J. Exp. Bot., 69, 4583, 10.1093/jxb/ery167 · doi:10.1093/jxb/ery167
  2. Hunter, 2007, The age of crosstalk: phosphorylation, ubiquitination, and beyond, Mol. Cell, 28, 730, 10.1016/j.molcel.2007.11.019 · DOI · Paper page
  3. Lyzenga, 2017, The kinase activity of calcineurin B-like interacting protein kinase 26 (CIPK26) influences its own stability and that of the ABA-regulated ubiquitin ligase, Keep on Going (KEG), Front. Plant Sci., 8, 502, 10.3389/fpls.2017.00502 · doi:10.3389/fpls.2017.00502
  4. Monaghan, 2018, Conserved degradation of orthologous RLCKs regulates immune homeostasis, Trends Plant Sci., 23, 554, 10.1016/j.tplants.2018.05.001 · doi:10.1016/j.tplants.2018.05.001
  5. Cheng, 2017, SCFAtPP2-B11 modulates ABA signaling by facilitating SnRK2.3 degradation in Arabidopsis thaliana, PLoS Genet., 13, 10.1371/journal.pgen.1006947 · doi:10.1371/journal.pgen.1006947
  6. Augustine, 2016, Defining the SUMO system in maize: SUMOylation is up-regulated during endosperm development and rapidly induced by stress, Plant Physiol., 171, 2191, 10.1104/pp.16.00353 · doi:10.1104/pp.16.00353
  7. Khan, 2014, Interplay between phosphorylation and SUMOylation events determines CESTA protein fate in brassinosteroid signalling, Nat. Commun., 5, 4687, 10.1038/ncomms5687 · doi:10.1038/ncomms5687
  8. Lee, 2015, Systemic immunity requires SnRK2.8-mediated nuclear import of NPR1 in Arabidopsis, Plant Cell, 27, 3425, 10.1105/tpc.15.00371 · doi:10.1105/tpc.15.00371
  9. Elrouby, 2010, Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes, Proc. Natl. Acad. Sci., 107, 17415, 10.1073/pnas.1005452107 · doi:10.1073/pnas.1005452107
  10. Miller, 2010, Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis, Proc. Natl. Acad. Sci., 107, 16512, 10.1073/pnas.1004181107 · DOI · Paper page
  11. McManus, 2017, Identification of cross talk between SUMOylation and ubiquitylation using a sequential peptide immunopurification approach, Nat. Protoc., 12, 2342, 10.1038/nprot.2017.105 · doi:10.1038/nprot.2017.105
  12. Budhiraja, 2009, Substrates related to chromatin and to RNA-dependent processes are modified by Arabidopsis SUMO isoforms that differ in a conserved residue with influence on desumoylation, Plant Physiol., 149, 1529, 10.1104/pp.108.135053 · doi:10.1104/pp.108.135053
  13. Crozet, 2016, SUMOylation represses SnRK1 signaling in Arabidopsis, Plant J., 85, 120, 10.1111/tpj.13096 · doi:10.1111/tpj.13096
  14. Lin, 2016, An Arabidopsis SUMO E3 ligase, SIZ1, negatively regulates photomorphogenesis by promoting COP1 activity, PLoS Genet., 12, 1, 10.1371/journal.pgen.1006016 · doi:10.1371/journal.pgen.1006016
  15. Sadanandom, 2015, SUMOylation of phytochrome-B negatively regulates light-induced signaling in Arabidopsis thaliana, Proc. Natl. Acad. Sci., 112, 11108, 10.1073/pnas.1415260112 · doi:10.1073/pnas.1415260112
  16. Kim, 2018, Nitrate reductases are relocalized to the nucleus by atSIZ1 and their levels are negatively regulated by COP1 and ammonium, Int. J. Mol. Sci., 19, 1
  17. Nukarinen, 2017, Protein sumoylation and phosphorylation intersect in Arabidopsis signaling, Plant J., 91, 505, 10.1111/tpj.13575 · doi:10.1111/tpj.13575
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Metadata

Authors
Vu, L. D., Gevaert, K., & De Smet, I.
Venue
Trends in Plant Science
Publisher
Elsevier BV
Published
2018-12
Volume
23
Issue
12
Pages
1068-1080
ISSN
1360-1385 (ISSN-L)
DOI
10.1016/j.tplants.2018.09.004
OpenAlex
W2893791677
Cited by
371
References
82
FWCI
1.55
Type
journal article
Language
en
Open access
closed
Licence
  • www.elsevier.com/tdm/userlicense/1.0/ (tdm)
  • www.elsevier.com/legal/tdmrep-license (tdm)

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CoChat. (2026). Citation check: Protein Language: Post-Translational Modifications Talking to Each Other. https://app.cochat.ai/papers/10.1016/j.tplants.2018.09.004
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Vu, L. D., Gevaert, K., & De Smet, I. (2018). Protein Language: Post-Translational Modifications Talking to Each Other. Trends in Plant Science. https://doi.org/10.1016/j.tplants.2018.09.004

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