Analysis of epidermal growth factor receptor dimerization by BS cross-linking. Academic Article

abstract

• Dimerization of receptor tyrosine kinases is a well-characterized process. It is imperative for the activation of many receptors, including the epidermal growth factor receptor (EGFR). EGFR has been shown to be regulated by a number of factors, including lipid raft localization. For example, alteration of the lipid raft localization of EGFR has been demonstrated to modify receptor dimerization. This protocol describes an assay to quantify EGFR dimers using BS(3) cross-linking. BS(3) cross-linking is well suited for this purpose because of its length, water solubility, and membrane impermeability. Although this protocol is written specifically for EGFR, the assay can be extrapolated in order to characterize dimerization of other receptor tyrosine kinases.

authors

• Chapkin, Robert

published proceedings

• Methods Mol Biol

author list (cited authors)

• Turk, H. F., & Chapkin, R. S.

citation count

• 12

complete list of authors

• Turk, Harmony F||Chapkin, Robert S

publication date

• January 2015

publisher

• Springer Nature  Publisher

keywords

• Animals
• Blotting, Western
• Cell Line, Transformed
• Colon
• Cross-Linking Reagents
• Epidermal Growth Factor
• Epithelial Cells
• ErbB Receptors
• Gene Expression
• Membrane Microdomains
• Mice
• Protein Multimerization
• Succinimides

Digital Object Identifier (DOI)

• 10.1007/978-1-4939-1789-1_3

start page

• 25

end page

• 34

volume

• 1233

URL

• http://dx.doi.org/10.1007/978-1-4939-1789-1_3