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        <r:String xml:lang="en">Influence of the extracellular domain size on the dynamic behavior of membrane proteins</r:String>
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          <r:URN>urn:ddi:se.researchdata:doi-10-17044-scilifelab-21102061.Individual-0:2.0</r:URN>
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          <r:String xml:lang="sv">Karolinska Institutet</r:String>
          <r:String xml:lang="en">Karolinska Institutet</r:String>
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        <r:PublisherName>
          <r:String xml:lang="sv">Karolinska Institutet</r:String>
          <r:String xml:lang="en">Karolinska Institutet</r:String>
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        <r:SimpleDate>2022-09-19</r:SimpleDate>
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      <r:Content xml:lang="en">This item contains datasets from Gurdap et al, Biophysical Journal, 2022 (https://doi.org/10.1016/j.bpj.2022.09.010).  This includes confocal images of vesicles for partitioning, Fluorescence Correlation Spectroscopy curves, excel and Prism files for all graphs for diffusion and partitoning and svg files of figures.

Abstract 

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 the 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 shows that increasing the  ECD mass or glycosylation leads to a decrease in ordered domain  partitioning and diffusivity. Our data reconciles 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. 

Data Usage

Researchers  are welcome to use the data contained in the dataset for  any projects.  Please cite this item upon use or when published. We   encourage reuse using the same CC BY 4.0 License. 

Data Content

Excel and Prism files for graphs

Microscopy Images

FCS Curves

Inkscape figure files

Software to open files

.csv - Microsoft Excel

.czi, .lsm - Fiji (https://imagej.net/Fiji.html#Downloads)

.pzfx - GraphPad Prism

.svg - Inkscape (https://inkscape.org/)

.fcs - FoCuS_point (https://academic.oup.com/bioinformatics/article/32/6/958/1744608)

Abbreviations 

GUV - giant unilamellar vesicle

GPMV- giant plasna membrane vesicle

DO- di-oleyl

DP- di-palmitol

CD- cluster of differentiation

PODXL- Podocalyxin-like protein

FCS- fluroescence correlation spectroscopy

A488- Alexa 488

ICAM- Intercellular Adhesion Molecule</r:Content>
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