Multimeric Ionotropic Purinoceptor Detection by Protein Cross-Linking

Vincent Compan; François Rassendren

doi:10.1007/978-1-4939-9717-6_10

Multimeric Ionotropic Purinoceptor Detection by Protein Cross-Linking

Methods Mol Biol. 2020:2041:147-153. doi: 10.1007/978-1-4939-9717-6_10.

Authors

Vincent Compan^{1

2}, François Rassendren^{3

4}

Affiliations

¹ IGF, University of Montpellier, CNRS, INSERM, Montpellier, France. vincent.compan@igf.cnrs.fr.
² Labex ICST, Montpellier, France. vincent.compan@igf.cnrs.fr.
³ IGF, University of Montpellier, CNRS, INSERM, Montpellier, France.
⁴ Labex ICST, Montpellier, France.

PMID: 31646486
DOI: 10.1007/978-1-4939-9717-6_10

Abstract

P2X receptor subunits (P2X1 to P2X7) assemble to form trimeric homomers or heteromers. Here, we describe the use of protein cross-linking to study the composition of P2X receptor complexes. This simple protocol is useful for determining the stoichiometry of P2X heteromeric receptors as well as for assessing the effect of point mutation, truncation, or concatenation on the quaternary architecture of these receptors.

Keywords: Cross-linking; Heteromer; Homomer; P2X; Quaternary structure; Trimer.

MeSH terms

Cross-Linking Reagents / chemistry*
HEK293 Cells
Humans
Protein Multimerization*
Protein Subunits
Receptors, Purinergic / chemistry*
Receptors, Purinergic / classification
Receptors, Purinergic / metabolism*

Substances

Cross-Linking Reagents
Protein Subunits
Receptors, Purinergic