Format

Send to

Choose Destination
See comment in PubMed Commons below
Methods Mol Biol. 2011;741:255-70. doi: 10.1007/978-1-61779-117-8_17.

Analysis of CFTR interactome in the macromolecular complexes.

Author information

1
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201, USA. cl@med.wayne.edu

Abstract

Cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel localized primarily at the apical surface of epithelial cells lining the airway, gut, exocrine glands, etc., where it is responsible for transepithelial salt and water transport. A growing number of proteins have been reported to interact directly or indirectly with CFTR chloride channel, suggesting that CFTR might regulate the activities of other ion channels, receptors, and transporters, in addition to its role as a chloride conductor. Most interactions occur primarily between the opposing terminal tails (N or C) of CFTR and its binding partners, either directly or mediated through various PDZ domain-containing proteins. This chapter describes methods we developed to cross-link CFTR into a macromolecular complex to identify and analyze the assembly and regulation of CFTR-containing complexes in the plasma membrane.

PMID:
21594790
PMCID:
PMC3178881
DOI:
10.1007/978-1-61779-117-8_17
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer Icon for PubMed Central
    Loading ...
    Support Center