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Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells
Published on: June 30, 2018
Subcellular localization of mammalian type II membrane proteins
Rajith N Aturaliya1, J Lynn Fink, Melissa J Davis
1Institute for Molecular Bioscience and ARC Centre in Bioinformatics, University of Queensland, St. Lucia, Queensland 4072, Australia.
Traffic (Copenhagen, Denmark)
|April 29, 2006
Summary
This study identifies type II membrane proteins using the MemO pipeline, revealing their subcellular localization across cellular compartments. The findings provide crucial data for understanding protein organization and function within the cell.
Area of Science:
- Cell Biology
- Proteomics
- Bioinformatics
Background:
- Type II membrane proteins possess a single transmembrane domain and lack signal peptides.
- Accurate identification and localization of these proteins are essential for understanding cellular processes.
Purpose of the Study:
- To computationally identify type II membrane proteins in the mouse proteome.
- To develop and apply a systematic protocol for documenting their subcellular localization.
- To curate and present localization data in the LOCATE database.
Main Methods:
- Application of the MemO computational pipeline for predicting type II membrane proteins.
- Integration of literature mining and high-throughput PCR-based experimental approaches for localization.
- Data curation and validation to minimize false positives.
Main Results:
- Identified 1408 transcriptional units encoding type II membrane proteins.
- Generated a dataset of 1831 transcripts for 1408 transcriptional units.
- Determined subcellular localization for 26% of the defined dataset, observing biases towards the early secretory pathway.
Conclusions:
- The study successfully identified and localized a significant portion of type II membrane proteins.
- Localization data reveals specific cellular compartment preferences for these proteins.
- The curated data in the LOCATE database serves as a valuable resource for future research.
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