Methods for Mapping of Interaction Networks Involving Membrane Proteins
Numerous approaches have been taken to study protein interactions, such as tagged protein complex isolation followed by mass spectrometry, yeast two-hybrid methods, fluorescence resonance energy transfer, surface plasmon resonance, site-directed mutagenesis, and crystallography. Membrane protein interactions pose significant challenges due to the need to solubilize membranes without disrupting protein-protein interactions. Traditionally, analysis of isolated protein complexes by high-resolution 2D gel electrophoresis has been the main method used to obtain an overall picture of proteome constituents and interactions. However, this method is time consuming, labor intensive, detects only abundant proteins and is not suitable for the coverage required to elucidate large interaction networks. In this review, we discuss the application of various methods to elucidate interactions involving membrane proteins. These techniques include methods for the direct isolation of single complexes or interactors as well as methods for characterization of entire subcellular and cellular interactomes.
- Research Organization:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 919285
- Report Number(s):
- PNNL-SA-56804; BBRCA9; 6504; 6504a; KP1501021; TRN: US0806345
- Journal Information:
- Biochemical and Biophysical Research Communications, 363(3):457-461, Vol. 363, Issue 3; ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
72 PHYSICS OF ELEMENTARY PARTICLES AND FIELDS
CRYSTALLOGRAPHY
ELECTROPHORESIS
ENERGY TRANSFER
FLUORESCENCE
MASS SPECTROSCOPY
MEMBRANE PROTEINS
MEMBRANES
MUTAGENESIS
PLASMONS
PROTEINS
RESONANCE
YEASTS
Protein networks
membrane proteins
protein complexes
chromatography
cofractionation
Environmental Molecular Sciences Laboratory