Phosphatase GhDsPTP3a interacts with annexin protein GhANN8b to reversely regulate salt tolerance in cotton (Gossypium spp.).

08:00 EDT 15th April 2019 | BioPortfolio

Summary of "Phosphatase GhDsPTP3a interacts with annexin protein GhANN8b to reversely regulate salt tolerance in cotton (Gossypium spp.)."

Salinity is among the major factors limiting crop production worldwide. Despite having moderate salt-tolerance, cotton (Gossypium spp.) suffers severe yield losses to salinity stresses, largely due to being grown on saline-alkali and dry lands. To identify genetic determinants conferring salinity tolerance in cotton, we deployed a functional genomic screen using a cotton cDNA library in a virus-induced gene silencing (VIGS) vector. We have revealed that silencing of GhDsPTP3a, which encodes a protein phosphatase, increases cotton tolerance to salt stress. Yeast two-hybrid screens indicated that GhDsPTP3a interacts with GhANN8b, an annexin protein, which plays a positive role in regulating cotton response to salinity stress. Salt stress induces GhANN8b phosphorylation, which is subsequently dephosphorylated by GhDsPTP3a. Ectopic expression of GhDsPTP3a and GhANN8b oppositely regulates plant salt tolerance and calcium influx. In addition, we have revealed that silencing of GhDsPTP3a or GhANN8b exerts opposing roles in regulating GhSOS1 transcript levels, and ectopic expression of GhANN8b elevates Na efflux in Arabidopsis under salinity stress. Our study demonstrates that a cotton phosphatase GhDsPTP3a and an annexin protein GhANN8b interact and reversely modulate Ca and Na fluxes in cotton salinity responses. This article is protected by copyright. All rights reserved.


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Name: The New phytologist
ISSN: 1469-8137


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Medical and Biotech [MESH] Definitions

A member of the annexin family that is a substrate for a tyrosine kinase, ONCOGENE PROTEIN PP60(V-SRC). Annexin A2 occurs as a 36-KDa monomer and in a 90-KDa complex containing two subunits of annexin A2 and two subunits of S100 FAMILY PROTEIN P11. The monomeric form of annexin A2 was formerly referred to as calpactin I heavy chain.

One of four major classes of mammalian serine/threonine specific protein phosphatases. Protein phosphatase 2C is a monomeric enzyme about 42 kDa in size. It shows broad substrate specificity dependent on divalent cations (mainly manganese and magnesium). Three isozymes are known in mammals: PP2C -alpha, -beta and -gamma. In yeast, there are four PP2C homologues: phosphatase PTC1 that have weak tyrosine phosphatase activity, phosphatase PTC2, phosphatase PTC3, and PTC4. Isozymes of PP2C also occur in Arabidopsis thaliana where the kinase-associated protein phosphatase (KAPP) containing a C-terminal PP2C domain, dephosphorylates Ser/Thr receptor-like kinase RLK5.

Protein of the annexin family exhibiting lipid interaction and steroid-inducibility.

Protein of the annexin family with a probable role in exocytotic and endocytotic membrane events.

A subtype of non-receptor protein tyrosine phosphatase that is closely-related to PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1. Alternative splicing of the mRNA for this phosphatase results in the production at two gene products, one of which includes a C-terminal nuclear localization domain that may be involved in the transport of the protein to the CELL NUCLEUS. Although initially referred to as T-cell protein tyrosine phosphatase the expression of this subtype occurs widely.

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