Academic Bibliography

 Search 200 years of publications by Ghent University researchers.
Advanced search
2 files | 118.02 MB
Add to list
  1. Search results
  2. UBP12 and UBP13 negatively regulate t...

UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2

Hannes Vanhaeren (UGent) , Ying Chen (UGent) , Mattias Vermeersch (UGent) , Liesbeth De Milde (UGent) , Valerie De Vleeschhauwer, Annelore Natran (UGent) , Geert Persiau (UGent) , Dominique Eeckhout (UGent) , Geert De Jaeger (UGent) , Kris Gevaert (UGent) , et al.
(2020) eLife. 9.
Author
Organization
Abstract
Protein ubiquitination is a very diverse post-translational modification leading to protein degradation or delocalization, or altering protein activity. In Arabidopsis thaliana, two E3 ligases, BIG BROTHER (BB) and DA2, activate the latent peptidases DA1, DAR1 and DAR2 by mono-ubiquitination at multiple sites. Subsequently, these activated peptidases destabilize various positive regulators of growth. Here, we show that two ubiquitin-specific proteases, UBP12 and UBP13, deubiquitinate DA1, DAR1 and DAR2, hence reducing their peptidase activity. Overexpression of UBP12 or UBP13 strongly decreased leaf size and cell area, and resulted in lower ploidy levels. Mutants in which UBP12 and UBP13 were downregulated produced smaller leaves that contained fewer and smaller cells. Remarkably, neither UBP12 nor UBP13 were found to be cleavage substrates of the activated DA1. Our results therefore suggest that UBP12 and UBP13 work upstream of DA1, DAR1 and DAR2 to restrict their protease activity and hence fine-tune plant growth and development.
Keywords
General Biochemistry, Genetics and Molecular Biology, General Immunology and Microbiology, General Neuroscience, General Medicine

Downloads

  • Download
    Vanhaeren et al. 2020 eLife 9 e52276.pdf
    • full text (Published version)
    • |
    • open access
    • |
    • PDF
    • |
    • 3.01 MB
  • Download
    (...).pdf
    • full text (Author's original)
    • |
    • UGent only
    • |
    • PDF
    • |
    • 115.01 MB

Citation

Please use this url to cite or link to this publication:

MLA
Vanhaeren, Hannes, et al. “UBP12 and UBP13 Negatively Regulate the Activity of the Ubiquitin-Dependent Peptidases DA1, DAR1 and DAR2.” ELife, vol. 9, ELIFE SCIENCES PUBLICATIONS LTD, 2020, doi:10.7554/elife.52276.
APA
Vanhaeren, H., Chen, Y., Vermeersch, M., De Milde, L., De Vleeschhauwer, V., Natran, A., … Inzé, D. (2020). UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2. ELife, 9. https://doi.org/10.7554/elife.52276
Chicago author-date
Vanhaeren, Hannes, Ying Chen, Mattias Vermeersch, Liesbeth De Milde, Valerie De Vleeschhauwer, Annelore Natran, Geert Persiau, et al. 2020. “UBP12 and UBP13 Negatively Regulate the Activity of the Ubiquitin-Dependent Peptidases DA1, DAR1 and DAR2.” ELife 9. https://doi.org/10.7554/elife.52276.
Chicago author-date (all authors)
Vanhaeren, Hannes, Ying Chen, Mattias Vermeersch, Liesbeth De Milde, Valerie De Vleeschhauwer, Annelore Natran, Geert Persiau, Dominique Eeckhout, Geert De Jaeger, Kris Gevaert, and Dirk Inzé. 2020. “UBP12 and UBP13 Negatively Regulate the Activity of the Ubiquitin-Dependent Peptidases DA1, DAR1 and DAR2.” ELife 9. doi:10.7554/elife.52276.
Vancouver
1.
Vanhaeren H, Chen Y, Vermeersch M, De Milde L, De Vleeschhauwer V, Natran A, et al. UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2. eLife. 2020;9.
IEEE
[1]
H. Vanhaeren et al., “UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2,” eLife, vol. 9, 2020.
@article{8656763,
  abstract     = {{Protein ubiquitination is a very diverse post-translational modification leading to protein degradation or delocalization, or altering protein activity. In Arabidopsis thaliana, two E3 ligases, BIG BROTHER (BB) and DA2, activate the latent peptidases DA1, DAR1 and DAR2 by mono-ubiquitination at multiple sites. Subsequently, these activated peptidases destabilize various positive regulators of growth. Here, we show that two ubiquitin-specific proteases, UBP12 and UBP13, deubiquitinate DA1, DAR1 and DAR2, hence reducing their peptidase activity. Overexpression of UBP12 or UBP13 strongly decreased leaf size and cell area, and resulted in lower ploidy levels. Mutants in which UBP12 and UBP13 were downregulated produced smaller leaves that contained fewer and smaller cells. Remarkably, neither UBP12 nor UBP13 were found to be cleavage substrates of the activated DA1. Our results therefore suggest that UBP12 and UBP13 work upstream of DA1, DAR1 and DAR2 to restrict their protease activity and hence fine-tune plant growth and development.}},
  articleno    = {{e52276}},
  author       = {{Vanhaeren, Hannes and Chen, Ying and Vermeersch, Mattias and De Milde, Liesbeth and De Vleeschhauwer, Valerie and Natran, Annelore and Persiau, Geert and Eeckhout, Dominique and De Jaeger, Geert and Gevaert, Kris and Inzé, Dirk}},
  issn         = {{2050-084X}},
  journal      = {{eLife}},
  keywords     = {{General Biochemistry,Genetics and Molecular Biology,General Immunology and Microbiology,General Neuroscience,General Medicine}},
  language     = {{eng}},
  publisher    = {{ELIFE SCIENCES PUBLICATIONS LTD}},
  title        = {{UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2}},
  url          = {{http://doi.org/10.7554/elife.52276}},
  volume       = {{9}},
  year         = {{2020}},
}
Altmetric
View in Altmetric
Web of Science
Times cited: