Insights into membrane association of the SMP domain of extended synaptotagmin

Yunyun Wang, Zhenni Li, Xinyu Wang, Ziyuan Zhao, Li Jiao, Ruming Liu, Keying Wang, Rui Ma, Yang Yang, Guo Chen, Yong Wang () and Xin Bian ()
Additional contact information
Yunyun Wang: Frontiers Science Center for Cell Responses, Nankai University
Zhenni Li: Frontiers Science Center for Cell Responses, Nankai University
Xinyu Wang: Nankai University
Ziyuan Zhao: Nankai University
Li Jiao: Nankai University
Ruming Liu: Nankai University
Keying Wang: Zhejiang University
Rui Ma: Xiamen University
Yang Yang: Renji Hospital, School of Medicine, Shanghai Jiao Tong University
Guo Chen: Frontiers Science Center for Cell Responses, Nankai University
Yong Wang: Zhejiang University
Xin Bian: Frontiers Science Center for Cell Responses, Nankai University

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: Abstract The Synaptotagmin-like Mitochondrial-lipid-binding Protein (SMP) domain is a newly identified lipid transfer module present in proteins that regulate lipid homeostasis at membrane contact sites (MCSs). However, how the SMP domain associates with the membrane to extract and unload lipids is unclear. Here, we performed in vitro DNA brick-assisted lipid transfer assays and in silico molecular dynamics simulations to investigate the molecular basis of the membrane association by the SMP domain of extended synaptotagmin (E-Syt), which tethers the tubular endoplasmic reticulum (ER) to the plasma membrane (PM). We demonstrate that the SMP domain uses its tip region to recognize the extremely curved subdomain of tubular ER and the acidic-lipid-enriched PM for highly efficient lipid transfer. Supporting these findings, disruption of these mechanisms results in a defect in autophagosome biogenesis contributed by E-Syt. Our results suggest a model that provides a coherent picture of the action of the SMP domain at MCSs.

Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-023-37202-8 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:14:y:2023:i:1:d:10.1038_s41467-023-37202-8

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

DOI: 10.1038/s41467-023-37202-8

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 ().