Phosphatidic acid counteracts S-RNase signaling in pollen by stabilizing the actin cytoskeleton

Chen, Jianqing, Wang, Peng, De Graaf, Barend H. J. ORCID: https://orcid.org/0000-0003-0542-5510, Zhang, Hao, Jiao, Huijun, Tang, Chao, Zhang, Shaoling and Wu, Juyou 2018. Phosphatidic acid counteracts S-RNase signaling in pollen by stabilizing the actin cytoskeleton. Plant Cell 30 (5) , pp. 1023-1039. 10.1105/tpc.18.00021

Full text not available from this repository.

Abstract

S-RNase is the female determinant of self-incompatibility (SI) in pear (Pyrus bretschneideri). After translocation to the pollen tube, S-RNase degrades rRNA and induces pollen tube death in an S-haplotype-specific manner. In this study, we found that the actin cytoskeleton is a target of P. bretschneideri S-RNase (PbrS-RNase) and uncovered a mechanism that involves phosphatidic acid (PA) and protects the pollen tube from PbrS-RNase cytotoxicity. PbrS-RNase interacts directly with PbrActin1 in an S-haplotype-independent manner, causing the actin cytoskeleton to depolymerize and promoting programmed cell death in the self-incompatible pollen tube. Pro-156 of PbrS-RNase is essential for the PbrS-RNase-PbrActin1 interaction, and the actin cytoskeleton-depolymerizing function of PbrS-RNase does not require its RNase activity. PbrS-RNase cytotoxicity enhances the expression of phospholipase D (PbrPLDδ1), resulting in increased PA levels in the incompatible pollen tube. PbrPLDδ1-derived PA initially prevents depolymerization of the actin cytoskeleton elicited by PbrS-RNase and delays the SI signaling that leads to pollen tube death. This work provides insights into the orchestration of the S-RNase-based SI response, in which increased PA levels initially play a protective role in incompatible pollen, until sustained PbrS-RNase activity reaches the point of no return and pollen tube growth ceases.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Publisher:	American Society of Plant Biologists
ISSN:	1040-4651
Date of First Compliant Deposit:	24 May 2018
Date of Acceptance:	27 April 2018
Last Modified:	23 Oct 2022 13:47
URI:	https://orca.cardiff.ac.uk/id/eprint/111745

Citation Data

Cited 68 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item