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Published on: July 16, 2020
The identification and characterization of membranome components
Dhimankrishna Ghosh1, Ron C Beavis, John A Wilkins
1Manitoba Centre for Proteomics and Systems Biology, Department of Internal Medicine, University of Manitoba, Winnipeg, Manitoba R3E 3P4, Canada.
Journal of Proteome Research
|February 23, 2008
Summary
Many identified cell membrane proteins lack transmembrane regions, suggesting they associate closely with membranes rather than being contaminants. This study investigated integral and intimately associated proteins in K562 cell membranes.
Area of Science:
- Proteomics
- Cell Biology
- Biochemistry
Background:
- Proteomic studies reveal many cell membrane proteins lack predicted transmembrane regions.
- This suggests potential contamination or genuine, non-integral membrane associations.
Purpose of the Study:
- To identify integral and intimately associated proteins in K562 cell microsomal membranes.
- To differentiate between true membrane proteins and peripherally associated ones.
Main Methods:
- Isolated K562 cell membranes were treated to remove peripheral proteins.
- Residual proteins were analyzed using SDS-PAGE and Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS).
- Tandem lectin affinity chromatography was used to enrich membrane glycoproteins.
Main Results:
- Approximately 41% of isolated proteins were classified as membrane proteins based on transmembrane regions or post-translational modifications.
- A significant portion of non-integral proteins were found to be intimately associated with membranes.
Conclusions:
- Cell membranes contain a substantial number of non-integral proteins that associate closely with the membrane.
- These findings challenge the exclusive definition of membrane proteins based solely on transmembrane domains.
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