Lisa Rehm
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Lisa Rehm has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
- Aayush Srivastava
Department of Physics, Institute of Biophysics, Goethe University, Max-von-Laue-Straße 1, 60438 Frankfurt, Germany
1 shared publication - Abhishek Bhattacharya
National Centre for Biological Sciences - TIFR, Bangalore, India
1 shared publication - Achilleas S. Frangakis
Buchmann Institute for Molecular Life Sciences and Institute for Biophysics, Goethe University, Frankfurt am Main, Germany
1 shared publication - Alexander Gottschalk
Department of Molecular Sciences, Institute of Biophysical Chemistry, Goethe University, Max-von-Laue-Straße 9, 60438 Frankfurt, Germany
1 shared publication - Alexandra N. Birtasu
Buchmann Institute for Molecular Life Sciences, Goethe University, Max-von-Laue-Strasse 15, 60438 Frankfurt, Germany
1 shared publication - Atal Vats
National Centre for Biological Sciences, Tata Institute of Fundamental Research
1 shared publication
Latest Publications
- Open Access
- 7 November 2025
- Published by American Association for the Advancement of Science (AAAS) in Science Advances
- Vol. 11 (45) , eaea8596
In situ structure of a gap junction–stomatin complex
Gap junctions (GJs) are intercellular channels that mediate electrical signals and transfer of small molecules. They are crucial for brain, heart, and other organ functions. While molecular structures of purified homomeric GJs are available, information of in situ structures is lacking. In vivo, GJs can form heteromers with different functionalities and may associate with other proteins. Here, we analyzed Caenorhabditis elegans GJs by cryo–electron tomography and subtomogram averaging. We observed hexagonal arrays of GJs at cellular junctions in primary embryonal cells that displayed distinct wide and narrow conformations. Moreover, we found a cap-like, cytosolic protein assembly enclosing the channel pore. We propose that the cap is formed by the stomatin UNC-1, known to interact with UNC-9 innexins. This is corroborated by matching AlphaFold3 models of UNC-1 multimers with our subtomogram average structure; by expressing GFP-tagged UNC-1, leading to cap structures with additional density; and by coarse-grained MD simulations. UNC-1/stomatin rings may affect GJ formation or functions, possibly beyond nematodes.
- 7 November 2025
- Published by American Association for the Advancement of Science (AAAS) in Science Advances
- Vol. 11 (45) , eaea8596
Open AccessIn situ structure of a gap junction–stomatin complex
Gap junctions (GJs) are intercellular channels that mediate electrical signals and transfer of small molecules. They are crucial for brain, heart, and other organ functions. While molecular structures of purified homomeric GJs are available, information of in situ structures is lacking. In vivo, GJs can form heteromers with different functionalities and may associate with other proteins. Here, we analyzed Caenorhabditis elegans GJs by cryo–electron tomography and subtomogram averaging. We observed hexagonal arrays of GJs at cellular junctions in primary embryonal cells that displayed distinct wide and narrow conformations. Moreover, we found a cap-like, cytosolic protein assembly enclosing the channel pore. We propose that the cap is formed by the stomatin UNC-1, known to interact with UNC-9 innexins. This is corroborated by matching AlphaFold3 models of UNC-1 multimers with our subtomogram average structure; by expressing GFP-tagged UNC-1, leading to cap structures with additional density; and by coarse-grained MD simulations. UNC-1/stomatin rings may affect GJ formation or functions, possibly beyond nematodes.