AtPFA‐DSP3, an atypical dual‐specificity protein tyrosine phosphatase, affects salt stress response by modulating MPK3 and MPK6 activity. (15th February 2021)
- Record Type:
- Journal Article
- Title:
- AtPFA‐DSP3, an atypical dual‐specificity protein tyrosine phosphatase, affects salt stress response by modulating MPK3 and MPK6 activity. (15th February 2021)
- Main Title:
- AtPFA‐DSP3, an atypical dual‐specificity protein tyrosine phosphatase, affects salt stress response by modulating MPK3 and MPK6 activity
- Authors:
- Xin, Jing
Li, Chuanling
Ning, Kexin
Qin, Yuan
Shang, Jian‐Xiu
Sun, Yu - Abstract:
- Abstract: Protein phosphorylation, especially serine/threonine and tyrosine phosphorylation, plays significant roles in signalling during plant growth and development as well as plant responses to biotic or abiotic stresses. Dual‐specificity protein tyrosine phosphatases dephosphorylate components of these signalling pathways. Here, we report that an atypical dual‐specificity protein tyrosine phosphatase, AtPFA‐DSP3 (DSP3), negatively affects the response of plants to high‐salt conditions. A DSP3 loss‐of‐function mutant showed reduced sensitivity to salt treatment. DSP3 was primarily localized in nuclei and was degraded during salt treatment. Compared to wild type, the level of ROS was lower in the dsp3 mutant and higher in plants ectopically expressing DSP3, indicating that higher DSP3 level was associated with increased ROS production. DSP3 interacted with and dephosphorylated MPK3 and MPK6. Genetic analyses of a dsp3mpk3 double mutant revealed that DSP3's effect on salt stress depends on MPK3. Moreover, the phosphatase activity of DSP3 was required for its role in salt signalling. These results indicate that DSP3 is a negative regulator of salt responses in Arabidopsis by directly modulating the accumulation of phosphorylated MPK3 and MPK6. Abstract : Protein phosphatases play an important role in balancing the phosphorylation status of signalling components during plant growth and development and responses to environmental signals. ATPFA‐DSP3, a dual‐specificity proteinAbstract: Protein phosphorylation, especially serine/threonine and tyrosine phosphorylation, plays significant roles in signalling during plant growth and development as well as plant responses to biotic or abiotic stresses. Dual‐specificity protein tyrosine phosphatases dephosphorylate components of these signalling pathways. Here, we report that an atypical dual‐specificity protein tyrosine phosphatase, AtPFA‐DSP3 (DSP3), negatively affects the response of plants to high‐salt conditions. A DSP3 loss‐of‐function mutant showed reduced sensitivity to salt treatment. DSP3 was primarily localized in nuclei and was degraded during salt treatment. Compared to wild type, the level of ROS was lower in the dsp3 mutant and higher in plants ectopically expressing DSP3, indicating that higher DSP3 level was associated with increased ROS production. DSP3 interacted with and dephosphorylated MPK3 and MPK6. Genetic analyses of a dsp3mpk3 double mutant revealed that DSP3's effect on salt stress depends on MPK3. Moreover, the phosphatase activity of DSP3 was required for its role in salt signalling. These results indicate that DSP3 is a negative regulator of salt responses in Arabidopsis by directly modulating the accumulation of phosphorylated MPK3 and MPK6. Abstract : Protein phosphatases play an important role in balancing the phosphorylation status of signalling components during plant growth and development and responses to environmental signals. ATPFA‐DSP3, a dual‐specificity protein tyrosine phosphatase, functions as a negative regulator in plant response to salt stress by directly dephosphorylating MPK3 and MPK6 and indirectly affecting ROS levels. … (more)
- Is Part Of:
- Plant, cell and environment. Volume 44:Number 5(2021)
- Journal:
- Plant, cell and environment
- Issue:
- Volume 44:Number 5(2021)
- Issue Display:
- Volume 44, Issue 5 (2021)
- Year:
- 2021
- Volume:
- 44
- Issue:
- 5
- Issue Sort Value:
- 2021-0044-0005-0000
- Page Start:
- 1534
- Page End:
- 1548
- Publication Date:
- 2021-02-15
- Subjects:
- Arabidopsis -- protein phosphorylation -- ROS
Plant physiology -- Periodicals
Plant cells and tissues -- Periodicals
Plant communities -- Periodicals
581.105 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-3040 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/pce.14002 ↗
- Languages:
- English
- ISSNs:
- 0140-7791
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6514.200000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16567.xml