Isolation of Arabidopsis extracellular ATP binding proteins by affinity proteomics and identification of PHOSPHOLIPASE C-LIKE 1 as an extracellular protein essential for fumonisin B1 toxicity

8Citations
Citations of this article
25Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

ATP is secreted to the extracellular matrix, where it activates plasma membrane receptors for controlling plant growth and stress-adaptive processes. DOES NOT RESPOND TO NUCLEOTIDES 1 (DORN1), was the first plant ATP receptor to be identified but key downstream proteins remain sought after. Here, we identified 120 proteins secreted by Arabidopsis cell cultures and screened them for putative stress-responsive proteins using ATP-affinity purification. We report three Arabidopsis proteins isolated by ATP-affinity: PEROXIDASE 52, SUBTILASE-LIKE SERINE PROTEASE 1.7 and PHOSPHOLIPASE C-LIKE 1. In wild-type Arabidopsis, the expression of genes encoding all three proteins responded to fumonisin B1, a cell death-activating mycotoxin. The expression of PEROXIDASE 52 and PHOSPHOLIPASE C-LIKE 1 was altered in fumonisin B1-resistant salicylic acid induction-deficient (sid2) mutants. Exposure to fumonisin B1 suppressed PHOSPHOLIPASE C-LIKE 1 expression in sid2 mutants, suggesting that the inactivation of this gene might provide mycotoxin tolerance. Accordingly, gene knockout mutants of PHOSPHOLIPASE C-LIKE 1 were resistant to fumonisin B1-induced death. The activation of PHOSPHOLIPASE C-LIKE 1 gene expression by exogenous ATP was not blocked in dorn1 loss-of-function mutants, indicating that DORN1 is not required. Furthermore, exogenous ATP rescued both the wild type and the dorn1 mutants from fumonisin-B1 toxicity, suggesting that different ATP receptor(s) are operational in this process. Our results point to the existence of additional plant ATP receptor(s) and provide crucial downstream targets for use in designing screens to identify these receptors. Finally, PHOSPHOLIPASE C-LIKE 1 serves as a convergence point for fumonisin B1 and extracellular ATP signalling, and functions in the Arabidopsis stress response to fumonisin B1.

References Powered by Scopus

Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade

6489Citations
N/AReaders
Get full text

Genome-wide insertional mutagenesis of Arabidopsis thaliana

4365Citations
N/AReaders
Get full text

Isochorismate synthase is required to synthesize salicylic acid for plant defence

1811Citations
N/AReaders
Get full text

Cited by Powered by Scopus

Self-incompatibility requires GPI anchor remodeling by the poppy PGAP1 ortholog HLD1

13Citations
N/AReaders
Get full text

Damage Signaling by Extracellular Nucleotides: A Role for Cyclic Nucleotides in Elevating Cytosolic Free Calcium?

10Citations
N/AReaders
Get full text

Extracellular ATP targets Arabidopsis RIBONUCLEASE 1 to suppress mycotoxin stress-induced cell death

6Citations
N/AReaders
Get full text

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Cite

CITATION STYLE

APA

Smith, S. J., Goodman, H., Kroon, J. T. M., Brown, A. P., Simon, W. J., & Chivasa, S. (2021). Isolation of Arabidopsis extracellular ATP binding proteins by affinity proteomics and identification of PHOSPHOLIPASE C-LIKE 1 as an extracellular protein essential for fumonisin B1 toxicity. Plant Journal, 106(5), 1387–1400. https://doi.org/10.1111/tpj.15243

Readers' Seniority

Tooltip

PhD / Post grad / Masters / Doc 7

54%

Researcher 4

31%

Professor / Associate Prof. 2

15%

Readers' Discipline

Tooltip

Biochemistry, Genetics and Molecular Bi... 6

50%

Agricultural and Biological Sciences 5

42%

Engineering 1

8%

Article Metrics

Tooltip
Social Media
Shares, Likes & Comments: 31

Save time finding and organizing research with Mendeley

Sign up for free