ArticleNature communications2024
Chloride intracellular channel (CLIC) proteins function as fusogens.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Use of biomolecular emulator for characterizing flexible proteins by small-angle x-ray scattering.Protein science : a publication of the Protein Society · 2026Article
- A somatic multiple myeloma mutation unravels a mechanism of oligomerization-mediated product inhibition in GGPPS.The FEBS journal · 2025Article
- AAV gene therapy rescues hearing and balance in a model of CLIC5 deafness.EMBO molecular medicine · 2025Article
- CLIC2 regulates immunosuppression and macrophage differentiation in genomically stable gastric cancer.Biology direct · 2025Article
- Intracellular Chloride Channels: A Rising Target in Lung Disease Research.Journal of respiratory biology and translational medicine · 2025Article
- Organ preservation: current limitations and optimization approaches.Frontiers in medicine · 2025Review
- CLIC5 promotes myoblast differentiation and skeletal muscle regeneration via the BGN-mediated canonical Wnt/β-catenin signaling pathway.Science advances · 2024Article
- Placental Origins of Preeclampsia: Insights from Multi-Omic Studies.International journal of molecular sciences · 2024Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Chloride Intracellular Channel (CLIC) family members uniquely transition between soluble and membrane-associated conformations. Despite decades of extensive functional and structural studies, CLICs' function as ion channels remains debated, rendering our understanding of their physiological role incomplete. Here, we expose the function of CLIC5 as a fusogen. We demonstrate that purified CLIC5 directly interacts with the membrane and induces fusion, as reflected by increased liposomal diameter and lipid and content mixing between liposomes. Moreover, we show that this activity is facilitated by acidic pH, a known trigger for CLICs' transition to a membrane-associated conformation, and that increased exposure of the hydrophobic inter-domain interface is crucial for this process. Finally, mutation of a conserved hydrophobic interfacial residue diminishes the fusogenic activity of CLIC5 in vitro and impairs excretory canal extension in C. elegans in vivo. Together, our results unravel the long-sought physiological role of these enigmatic proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.