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Title: Methods for Mapping of Interaction Networks Involving Membrane Proteins

Journal Article · · Biochemical and Biophysical Research Communications, 363(3):457-461

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