Hiring in life sciences? Share your open positions with our professional community. Read more Close

Advertisement

A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors

External protocol Created on 10 Apr 2014

Authors

Carine Bécamel, Nathalie Galéotti, Joël Poncet, Patrick Jouin, Aline Dumuis, Joël Bockaert, Philippe Marin

Summary

There is accumulating evidence that membrane-bound receptors interact with many intracellular proteins. Multiprotein complexes associated with ionotropic receptors have been extensively characterized, but the identification of proteins interacting with G protein-coupled receptors (GPCRs) has so far only been achieved in a piecemeal fashion, focusing on one or two protein species. We describe a method based on peptide affinity chromatography, two-dimensional electrophoresis, mass spectrometry and immunoblotting to identify the components of multiprotein complexes interacting directly or indirectly with intracellular domains of GPCRs or, more generally, any other membrane-bound receptor. Using this global approach, we have characterized multiprotein complexes that bind to the carboxy-terminal tail of the 5-hydroxytryptamine type 2C receptor and are important for its subcellular localization in CNS cells (Bécamel et al., EMBO J., 21(10): 2332, 2002).

Further details

The protocol was imported from Springer Protocols. To see the entire protocol, click on the source link, or download the pdf here.

Advertisement

Stats

  • Recommendations n/a n/a positive of 0 vote(s)
  • Views 262
  • Comments 0

Recommended by

  • No recommendations yet.

Post a comment

You need to be signed in to post comments. You can sign in here.

Comments

There are no comments yet.

Advertisement