The Arabidopsis SUMO E3 Ligase AtMMS21 Dissociates the E2Fa/DPa Complex in Cell Cycle Regulation. Issue 9 (4th August 2016)
- Record Type:
- Journal Article
- Title:
- The Arabidopsis SUMO E3 Ligase AtMMS21 Dissociates the E2Fa/DPa Complex in Cell Cycle Regulation. Issue 9 (4th August 2016)
- Main Title:
- The Arabidopsis SUMO E3 Ligase AtMMS21 Dissociates the E2Fa/DPa Complex in Cell Cycle Regulation
- Authors:
- Liu, Yiyang
Lai, Jianbin
Yu, Mengyuan
Wang, Feige
Zhang, Juanjuan
Jiang, Jieming
Hu, Huan
Wu, Qian
Lu, Guohui
Xu, Panglian
Yang, Chengwei - Abstract:
- Abstract : The Arabidopsis SUMO E3 ligase AtMMS21 dissociates the E2Fa/DPa complex by physical competition and SUMOylation in the G1/S cell cycle transition. Abstract: Development requires the proper execution and regulation of the cell cycle via precise, conserved mechanisms. Critically, the E2F/DP complex controls the expression of essential genes during cell cycle transitions. Here, we discovered the molecular function of the Arabidopsis thaliana SUMO E3 ligase METHYL METHANESULFONATE SENSITIVITY GENE21 (AtMMS21) in regulating the cell cycle via the E2Fa/DPa pathway. DPa was identified as an AtMMS21-interacting protein and AtMMS21 competes with E2Fa for interaction with DPa. Moreover, DPa is a substrate for SUMOylation mediated by AtMMS21, and this SUMOylation enhances the dissociation of the E2Fa/DPa complex. AtMMS21 also affects the subcellular localization of E2Fa/DPa. The E2Fa/DPa target genes are upregulated in the root of mms21-1 and mms21-1 mutants showed increased endoreplication. Overexpression of DPa affected the root development of mms21-1, and overexpression of AtMMS21 completely recovered the abnormal phenotypes of 35S:E2Fa-DPa plants. Our results suggest that AtMMS21 dissociates the E2Fa/DPa complex via competition and SUMOylation in the regulation of plant cell cycle.
- Is Part Of:
- The Plant Cell. Volume 28:Issue 9(2016)
- Journal:
- The Plant Cell
- Issue:
- Volume 28:Issue 9(2016)
- Issue Display:
- Volume 28, Issue 9 (2016)
- Year:
- 2016
- Volume:
- 28
- Issue:
- 9
- Issue Sort Value:
- 2016-0028-0009-0000
- Page Start:
- 2225
- Page End:
- 2237
- Publication Date:
- 2016-08-04
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.16.00439 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16319.xml