Mechanisms of RCD-1 pore formation and membrane bending

Keli Ren, James Daniel Farrell, Yueyue Li, Xinrui Guo, Ruipei Xie, Xin Liu, Qiaozhen Kang, Qihui Fan, Fangfu Ye, Jingjin Ding and Fang Jiao ()
Additional contact information
Keli Ren: Chinese Academy of Sciences
James Daniel Farrell: Chinese Academy of Sciences
Yueyue Li: Chinese Academy of Sciences
Xinrui Guo: Chinese Academy of Sciences
Ruipei Xie: Chinese Academy of Sciences
Xin Liu: Zhengzhou University
Qiaozhen Kang: Zhengzhou University
Qihui Fan: Chinese Academy of Sciences
Fangfu Ye: Chinese Academy of Sciences
Jingjin Ding: Chinese Academy of Sciences
Fang Jiao: Chinese Academy of Sciences

Nature Communications, 2025, vol. 16, issue 1, 1-12

Abstract: Abstract Regulator of cell death-1 (RCD-1) governs the heteroallelic expression of RCD-1-1 and RCD-1-2, a pair of fungal gasdermin (GSDM)-like proteins, which prevent cytoplasmic mixing during allorecognition and safeguard against mycoparasitism, genome exploitation, and deleterious cytoplasmic elements (e.g., senescence plasmids) by effecting a form of cytolytic cell death. However, the underlying mechanisms by which RCD-1 acts on the cell membrane remain elusive. Here, we demonstrate that RCD-1 binds acidic lipid membranes, forms pores, and induces membrane bending. Using atomic force microscopy (AFM) and AlphaFold, we show that RCD-1-1 and RCD-1-2 form heterodimers that further self-assemble into ~14.5 nm-wide transmembrane pores (~10 heterodimers). Moreover, through AFM force spectroscopy and micropipette aspiration, we reveal that RCD-1 proteins bend membranes with low bending moduli. This combined action of pore formation and membrane deformation may constitute a conserved mechanism within the broader GSDM family.

Date: 2025
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-56398-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-56398-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-56398-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().