UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2
© 2020, Vanhaeren et al..
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 growth regulators. 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.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2020 |
|---|---|
| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:9 |
|---|---|
| Enthalten in: |
eLife - 9(2020) vom: 25. März |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Vanhaeren, Hannes [VerfasserIn] |
|---|
| Links: |
|---|
| Anmerkungen: |
Date Completed 07.04.2021 Date Revised 07.04.2021 published: Electronic Citation Status MEDLINE |
|---|
| doi: |
10.7554/eLife.52276 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM307951901 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM307951901 | ||
| 003 | DE-627 | ||
| 005 | 20231225130706.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231225s2020 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.7554/eLife.52276 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n1026.xml |
| 035 | |a (DE-627)NLM307951901 | ||
| 035 | |a (NLM)32209225 | ||
| 035 | |a (PII)e52276 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Vanhaeren, Hannes |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2 |
| 264 | 1 | |c 2020 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 07.04.2021 | ||
| 500 | |a Date Revised 07.04.2021 | ||
| 500 | |a published: Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2020, Vanhaeren et al. | ||
| 520 | |a 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 growth regulators. 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a A. thaliana | |
| 650 | 4 | |a cell proliferation | |
| 650 | 4 | |a deubiquitination | |
| 650 | 4 | |a endoreduplication | |
| 650 | 4 | |a enzymatic activity | |
| 650 | 4 | |a leaf growth | |
| 650 | 4 | |a plant biology | |
| 650 | 4 | |a proteostasis | |
| 650 | 7 | |a Arabidopsis Proteins |2 NLM | |
| 650 | 7 | |a Ubiquitin |2 NLM | |
| 650 | 7 | |a Endopeptidases |2 NLM | |
| 650 | 7 | |a EC 3.4.- |2 NLM | |
| 650 | 7 | |a Peptide Hydrolases |2 NLM | |
| 650 | 7 | |a EC 3.4.- |2 NLM | |
| 650 | 7 | |a Ubiquitin-Specific Proteases |2 NLM | |
| 650 | 7 | |a EC 3.4.19.12 |2 NLM | |
| 650 | 7 | |a UBP12 protein, Arabidopsis |2 NLM | |
| 650 | 7 | |a EC 3.4.99.- |2 NLM | |
| 650 | 7 | |a UBP13 protein, Arabidopsis |2 NLM | |
| 650 | 7 | |a EC 3.4.99.- |2 NLM | |
| 700 | 1 | |a Chen, Ying |e verfasserin |4 aut | |
| 700 | 1 | |a Vermeersch, Mattias |e verfasserin |4 aut | |
| 700 | 1 | |a De Milde, Liesbeth |e verfasserin |4 aut | |
| 700 | 1 | |a De Vleeschhauwer, Valerie |e verfasserin |4 aut | |
| 700 | 1 | |a Natran, Annelore |e verfasserin |4 aut | |
| 700 | 1 | |a Persiau, Geert |e verfasserin |4 aut | |
| 700 | 1 | |a Eeckhout, Dominique |e verfasserin |4 aut | |
| 700 | 1 | |a De Jaeger, Geert |e verfasserin |4 aut | |
| 700 | 1 | |a Gevaert, Kris |e verfasserin |4 aut | |
| 700 | 1 | |a Inzé, Dirk |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t eLife |d 2012 |g 9(2020) vom: 25. März |w (DE-627)NLM221831460 |x 2050-084X |7 nnns |
| 773 | 1 | 8 | |g volume:9 |g year:2020 |g day:25 |g month:03 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.7554/eLife.52276 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 9 |j 2020 |b 25 |c 03 | ||