Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/84886
Title: Profilin negatively regulates formin-mediated actin assembly to modulate pamp-triggered plant immunity
Authors: Sun, He
Qiao, Zhu
Chua, Khi Pin
Tursic, Alma
Liu, Xu
Gao, Yong-Gui
Mu, Yuguang
Hou, Xingliang
Miao, Yansong
Keywords: Science::Biological sciences
Actin Cytoskeleton
Profilin
Issue Date: 2018
Source: Sun, H., Qiao, Z., Chua, K. P., Tursic, A., Liu, X., Gao, Y.-G., . . . Miao, Y. (2018). Profilin Negatively Regulates Formin-Mediated Actin Assembly to Modulate PAMP-Triggered Plant Immunity. Current Biology, 28(12), 1882-1895. doi:10.1016/j.cub.2018.04.045
Series/Report no.: Current Biology
Abstract: Profilin functions with formin in actin assembly, a process that regulates multiple aspects of plant development and immune responses. High-level eukaryotes contain multiple isoforms of profilin, formin, and actin, whose partner-specific interactions in actin assembly are not completely understood in plant development and defense responses. To examine the functionally distinct interactions between profilin and formin, we studied all five Arabidopsis profilins and their interactions with formin by using both in vitro biochemical and in vivo cell biology approaches. Unexpectedly, we found a previously undescribed negative regulatory function of AtPRF3 in AtFH1-mediated actin polymerization. The N-terminal 37 residues of AtPRF3 were identified to play a predominant role in inhibiting formin-mediated actin nucleation via their high affinity for the formin polyproline region and their triggering of the oligomerization of AtPRF3. Both in vivo and in vitro mechanistic studies of AtPRF3 revealed a universal mechanism in which the weak interaction between profilin and formin positively regulates actin assembly by ensuring rapid recycling of profilin, whereas profilin oligomerization negatively regulates actin polymerization. Upon recognition of the pathogen-associated molecular pattern, the gene transcription and protein degradation of AtPRF3 are modulated for actin assembly during plant innate immunity. The prf3 Arabidopsis plants show higher sensitivity to the bacterial flagellum peptide in both the plant growth and ROS responses. These findings demonstrate a profilin-mediated actin assembly mechanism underlying the plant immune responses.
URI: https://hdl.handle.net/10356/84886
http://hdl.handle.net/10220/49174
ISSN: 0960-9822
DOI: 10.1016/j.cub.2018.04.045
Rights: © 2018 Elsevier Ltd. All rights reserved. This paper was published in Current Biology and is made available with permission of Elsevier Ltd.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:IGS Journal Articles
SBS Journal Articles
SCBE Journal Articles

Google ScholarTM

Check

Altmetric


Plumx

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.