期刊
BIOPHYSICAL JOURNAL
卷 121, 期 20, 页码 3826-3836出版社
CELL PRESS
DOI: 10.1016/j.bpj.2022.09.010
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资金
- SciLifeLab summer internship [C-2021-0466]
- Swedish Research Council Starting Grant [2020-02682]
- Karolinska Institutet
- SciLifeLab National COVID-19 Research Program
- Knut and AliceWallenberg Foundation
- National Institutes of Health [R01-GM129325]
- Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases
- Swedish Research Council [2020-02682] Funding Source: Swedish Research Council
The properties of extracellular domains (ECDs) have an impact on the dynamic behavior of plasma membrane proteins, leading to changes in domain partitioning and protein diffusion.
The dynamic behavior of plasma membrane proteins mediates various cellular processes such as cellular motility, communication, and signaling. It is widely accepted that the dynamics of the membrane proteins is determined either by the interactions of the transmembrane domain with the surrounding lipids or by the interactions of the intracellular domain with cytosolic components such as cortical actin. Although initiation of different cellular signaling events at the plasma membrane has been attributed to the extracellular domain (ECD) properties recently, the impact of ECDs on the dynamic behavior of membrane proteins is rather unexplored. Here, we investigate how ECD properties influence protein dynamics in the lipid bilayer by reconstituting ECDs of different sizes or glycosylation in model membrane systems and analyzing ECD-driven protein sorting in lipid domains as well as protein mobility. Our data show that increasing the ECD mass or glycosylation leads to a decrease in ordered domain partitioning and diffusivity. Our data reconcile different mechanisms proposed for the initiation of cellular signaling by linking the ECD size of membrane proteins with their localization and diffusion dynamics in the plasma membrane.
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