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Tetraspanner-based nanodomains modulate BAR domain-induced membrane curvature
Open accessPreprint — published as 10.15252/embr.202357232 · Paper page
Abstract
Topography is a critical feature driving formation and dynamics of protein and lipid domains within biological membranes. The yeast plasma membrane (PM) has provided a powerful model system to study lateral domain formation, including characteristic BAR domain-induced PM furrows. Currently, it is not clear how the components involved in the establishment of these furrows cooperate to precisely regulate local PM topography. Here we report opposing functions for the Sur7 and Nce102 families of tetraspanner proteins in modulating membrane curvature and domain topography. Using STED nanoscopy and freeze-fracture EM we found that Sur7 tetraspanners form multimeric strands at the upper edges of PM furrows, which counteract the forces exerted by BAR domain proteins and prevent membrane tubulation. In contrast, Nce102 tetraspanners are located basal to the Sur7 proteins and promote BAR domain-induced curvature. The segregation of the two tetraspanner-based nanodomains is further supported by differential distribution of ergosterol to the upper edge of furrows and PIP2 lipids at the furrow base. These findings suggest a general role of tetraspanner proteins in sculpting local membrane domains.
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Metadata
- Authors
- Haase, D., Rasch, C., Keller, U., Elting, A., Wittmar, J., Janning, A., Kahms, M., Schuberth, C., Klingauf, J., & Wedlich-Söldner, R.
- Affiliations
- University of Münster (DE)
- Venue
- EMBO Reports
- Publisher
- openRxiv
- Published
- 2022-11-21
- Volume
- 24
- Issue
- 12
- Pages
- e57232-e57232
- ISSN
- 1469-221X (ISSN-L)
- PMC
- PMC10702824
- OpenAlex
- W4388014044
- Cited by
- 5
- References
- 1
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 2
- FWCI
- 0.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- EMBO Reports (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (SFB 944, SFB1557, SFB1348)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Keywords
- BAR domain proteins, membrane curvature, membrane tubulation, lipid rafts, protein oligomerization, membrane invagination, yeast plasma membrane
- MeSH terms
- Cell Membrane, Proteins
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