Strategies for membrane interaction proteomics: No mass spectrometry required

Membrane‐bound proteins are one of the most important protein types in the cell, and are involved in many major cell processes and signaling pathways. Most proteins, including those at membranes, must interact with other proteins to form complexes, which are essential for their function(s). In this...

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Bibliographic Details
Published in:Proteomics (Weinheim) 2012-05, Vol.12 (10), p.1519-1526
Main Authors: Lam, Mandy H. Y., Stagljar, Igor
Format: Article
Language:English
Subjects:
Animals
Biochemical methods
Cell signaling pathways
Humans
Mass spectrometry
Membrane proteins
Membrane Proteins - analysis
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Mice
Protein Binding
Protein Interaction Mapping - methods
Protein-protein interactions
Proteins
Proteomics
Proteomics - methods
Scientific imaging
Signal Transduction
Technology
Two-Hybrid System Techniques
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Summary:Membrane‐bound proteins are one of the most important protein types in the cell, and are involved in many major cell processes and signaling pathways. Most proteins, including those at membranes, must interact with other proteins to form complexes, which are essential for their function(s). In this review, we describe some of the major non‐mass spectrometry‐based methods and technologies used for the investigation of intracellular membrane protein complexes including Tango, fluorescence/bioluminescence resonance energy transfer (F/BRET), luminescence‐based mammalian interactome mapping (LUMIER), protein‐fragment complementation assay (PCA), and membrane yeast two‐hybrid assay (MYTH). We highlight the advantages and drawbacks of these methods, describe recent studies utilizing these methods, and discuss some of the major findings in the study of membrane protein‐based cell pathways.
ISSN:1615-9853
1615-9861
DOI:10.1002/pmic.201100471