title: High-throughput identification of transient extracellular protein interactions.
abstract: Protein interactions are highly diverse in their biochemical nature, varying in affinity and are often dependent on the surrounding biochemical environment. Given this heterogeneity, it seems unlikely that any one method, and particularly those capable of screening for many protein interactions in parallel, will be able to detect all functionally relevant interactions that occur within a living cell. One major class of interactions that are not detected by current popular high-throughput methods are those that occur in the extracellular environment, especially those made by membrane-embedded receptor proteins. In the present article, we discuss some of our recent research in the development of a scalable assay to identify this class of protein interaction and some of the findings from its application in the construction of extracellular protein interaction networks.
authors.affiliation: Cell Surface Signalling Laboratory, Wellcome Trust Sanger Institute, Hinxton, Cambridge CB10 1HH, UK. gw2@sanger.ac.uk
authors.forename: Gavin J
authors.initials: GJ
authors.lastname: Wright
authors.forename: Stephen
authors.initials: S
authors.lastname: Martin
authors.forename: K Mark
authors.initials: KM
authors.lastname: Bushell
authors.forename: Christian
authors.initials: C
authors.lastname: Söllner
mesh_terms: D000818:Animals; D005110:Extracellular Space / Q000378:metabolism*; D057166:High-Throughput Screening Assays / Q000379:methods*; D006801:Humans; D053858:Metabolic Networks and Pathways / Q000502:physiology; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000378:metabolism*; D013997:Time Factors
chemical_list: D011506:Proteins