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Interactions between the Cell Membrane Repair Protein S100A10 and Phospholipid Monolayers and Bilayers. | LitMetric

AI Article Synopsis

  • - S100A10 is a protein that collaborates with annexin A2 and AHNAK to form a complex that aids in repairing cell membranes, but its own binding properties to membranes were not well-understood prior to this study.
  • - The researchers overexpressed and purified S100A10 to investigate its membrane binding properties using methods like surface tensiometry, ellipsometry, and nuclear magnetic resonance spectroscopy.
  • - The findings reveal that S100A10 has a strong interaction with unsaturated phospholipids and prefers negatively charged lipid head groups, enhancing our understanding of how it contributes to membrane repair.

Article Abstract

Protein S100A10 participates in different cellular mechanisms and has different functions, especially at the membrane. Among those, it forms a ternary complex with annexin A2 and the C-terminal of AHNAK and then joins the dysferlin membrane repair complex. Together, they act as a platform enabling membrane repair. Both AHNAK and annexin A2 have been shown to have membrane binding properties. However, the membrane binding abilities of S100A10 are not clear. In this paper, we aimed to study the membrane binding of S100A10 in order to better understand its role in the cell membrane repair process. S100A10 was overexpressed by and purified by affinity chromatography. Using a Langmuir monolayer as a model membrane, the binding parameters and ellipsometric angles of the purified S100A10 were measured using surface tensiometry and ellipsometry, respectively. Phosphorus-31 solid-state nuclear magnetic resonance spectroscopy was also used to study the interaction of S100A10 with lipid bilayers. In the presence of a lipid monolayer, S100A10 preferentially interacts with unsaturated phospholipids. In addition, its behavior in the presence of a bilayer model suggests that S100A10 interacts more with the negatively charged polar head groups than the zwitterionic ones. This work offers new insights on the binding of S100A10 to different phospholipids and advances our understanding of the parameters influencing its membrane behavior.

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Source
http://dx.doi.org/10.1021/acs.langmuir.1c00342DOI Listing

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