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Updated: Apr 5, 2026

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy
Published on: December 12, 2025
Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF
Noreen Klein1, Nadja Hellmann2, Dirk Schneider1
1Institut für Pharmazie und Biochemie, Johannes Gutenberg Universität Mainz, Mainz, Germany.
Abstract:
The structure and composition of a biological membrane can severely influence the activity of membrane-embedded proteins. Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid bilayers formed from native E. coli lipids. Thus, at first glance, GlpF appears to not be optimized for its natural membrane environment. In fact, we found that GlpF activity was severely affected by negatively charged lipids regardless of the exact chemical nature of the lipid headgroup, whereas GlpF was not sensitive to changes in the lateral membrane pressure. These observations illustrate a potential mechanism by which the activity of an α-helical membrane protein is modulated by the negative charge density around the protein.
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