Related Experiment Video
Updated: Jan 26, 2026

Analysis of Shear Flow-induced Migration of Murine Marginal Zone B Cells In Vitro
Published on: November 26, 2018
Shear-Induced Migration of a Transmembrane Protein within a Vesicle
Koyo Nakamura1, Toshihiro Omori1, Takuji Ishikawa1
1Department of Finemechanics, Tohoku University, Sendai, Miyagi, Japan.
Abstract:
Biomembranes feature phospholipid bilayers and serve as the interface between cells or organelles and the extracellular and/or cellular environment. Lipids can move freely throughout the membrane; the lipid bilayer behaves like a fluid. Such fluidity is important in terms of the actions of membrane transport proteins, which often mediate biological functions; membrane protein motion has attracted a great deal of attention. Because the proteins are small, diffusion phenomena are often in play, but flow-induced transport has rarely been addressed. Here, we used a dissipative particle dynamics approach to investigate flow-induced membrane protein transport. We analyzed the drift of a membrane protein located within a vesicle. Under the influence of shear flow, the protein gradually migrated toward the vorticity axis via a random walk, and the probability of retention around the axis was high. To understand the mechanism of protein migration, we varied both shear strength and protein size. Protein migration was induced by the balance between the drag and thermodynamic diffusion forces and could be represented by the Péclet number. These results improve our understanding of flow-induced membrane protein transport.
More Related Videos
11:42Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
Published on: January 22, 2015
12:27Single Extracellular Vesicle Transmembrane Protein Characterization by Nano-Flow Cytometry
Published on: July 26, 2022
Related Concept Videos
Single-pass Transmembrane Proteins
Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Insertion of Multi-pass Transmembrane Proteins in the RER
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
Shearing Stress
The average shearing stress can be calculated by dividing the shear by the area of the cross-section.
Shearing Strain