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The B″-family subunits of protein phosphatase 2A are necessary for in-vitro dephosphorylation of the Arabidopsis mechanosensory transcription factor VIP1.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2021 Jan 01; Vol. 534, pp. 353-358. Date of Electronic Publication: 2020 Dec 18. - Publication Year :
- 2021
-
Abstract
- Protein phosphatase 2A (PP2A) B″-family subunits have Ca <superscript>2+</superscript> -binding EF-hand motifs and can bind PP2A substrates. Arabidopsis thaliana PP2A B″-family subunits are encoded by six genes, and bind a transcription factor, VIP1. VIP1 is dephosphorylated and nuclear-localized by hypo-osmotic stress. However, whether PP2A B″-family subunits mediate the VIP1 dephosphorylation is unclear. Here, we show by yeast two-hybrid and in vitro pull down assays that Arabidopsis PP2A B″-family subunits bind Arabidopsis PP2A A (scaffold) subunits. We also show that VIP1 dephosphorylation in vitro can be induced by a PP2A B″-family subunit.<br />Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2020 Elsevier Inc. All rights reserved.)
- Subjects :
- Arabidopsis genetics
Arabidopsis metabolism
Arabidopsis Proteins genetics
Gene Expression Regulation, Plant
Genes, Plant
Osmotic Pressure
Phosphorylation
Plants, Genetically Modified
Protein Interaction Domains and Motifs
Protein Phosphatase 2 genetics
Protein Subunits
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Transcription Factors genetics
Two-Hybrid System Techniques
Arabidopsis Proteins chemistry
Arabidopsis Proteins metabolism
Protein Phosphatase 2 chemistry
Protein Phosphatase 2 metabolism
Transcription Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 534
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 33342519
- Full Text :
- https://doi.org/10.1016/j.bbrc.2020.11.078