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The Protein Phosphatase PP2A Plays Multiple Roles in Plant Development by Regulation of Vesicle Traffic-Facts and Questions
- Source :
- International Journal of Molecular Sciences, International Journal of Molecular Sciences, Vol 22, Iss 975, p 975 (2021)
- Publication Year :
- 2020
-
Abstract
- The protein phosphatase PP2A is essential for the control of integrated eukaryotic cell functioning. Several cellular and developmental events, e.g., plant growth regulator (PGR) mediated signaling pathways are regulated by reversible phosphorylation of vesicle traffic proteins. Reviewing present knowledge on the relevant role of PP2A is timely. We discuss three aspects: (1) PP2A regulates microtubule-mediated vesicle delivery during cell plate assembly. PP2A dephosphorylates members of the microtubule associated protein family MAP65, promoting their binding to microtubules. Regulation of phosphatase activity leads to changes in microtubule organization, which affects vesicle traffic towards cell plate and vesicle fusion to build the new cell wall between dividing cells. (2) PP2A-mediated inhibition of target of rapamycin complex (TORC) dependent signaling pathways contributes to autophagy and this has possible connections to the brassinosteroid signaling pathway. (3) Transcytosis of vesicles transporting PIN auxin efflux carriers. PP2A regulates vesicle localization and recycling of PINs related to GNOM (a GTP–GDP exchange factor) mediated pathways. The proper intracellular traffic of PINs is essential for auxin distribution in the plant body, thus in whole plant development. Overall, PP2A has essential roles in membrane interactions of plant cell and it is crucial for plant development and stress responses.
- Subjects :
- autophagy
protein phosphatase PP2A
Cytoplasmic Vesicles
Plant Development
transcytosis
Biological Transport
Review
vesicle traffic
lcsh:Chemistry
phragmoplast
lcsh:Biology (General)
lcsh:QD1-999
Plant Cells
cell plate
PIN auxin efflux carriers
Protein Phosphatase 2
Phosphorylation
lcsh:QH301-705.5
Signal Transduction
Subjects
Details
- ISSN :
- 14220067
- Volume :
- 22
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- International journal of molecular sciences
- Accession number :
- edsair.pmid.dedup....8479657c8c5e8b9177bb7fac17dae455