Assaying AMPA receptor oligomerization

Catherine L. Salussolia; Quan Gan; Lonnie P. Wollmuth

doi:10.1007/978-1-4939-2812-5_1

Assaying AMPA receptor oligomerization

Catherine L. Salussolia
, Quan Gan
, Lonnie P. Wollmuth

Neurobiology and Behavior

Stony Brook University

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

2 Scopus citations

Abstract

Functional AMPA receptors (AMPARs) are tetrameric complexes formed by four identical (homomeric) or similar (heteromeric) subunits. Variations in the number and composition of AMPARs on the plasma membrane impact synaptic strength, neurodevelopment, and brain disorders. While the mechanisms mediating oligomerization of AMPARs are not well understood, they form the template for defining the number and preferential assembly of AMPARs. In this chapter we describe the application of two methods, blue-native PAGE (BN-PAGE) and fluorescence-detection size-exclusion chromatography (FSEC), to delineate the oligomeric state of AMPAR complexes and factors that determine the oligomerization process.

Original language	English
Title of host publication	Ionotropic Glutamate Receptor Technologies
Publisher	Springer New York
Pages	3-14
Number of pages	12
ISBN (Electronic)	9781493928125
ISBN (Print)	9781493928118
DOIs	https://doi.org/10.1007/978-1-4939-2812-5_1
State	Published - Sep 25 2015

Keywords

Blue-native PAGE
Fluorescence-detection size-exclusion chromatography
Ionotropic glutamate receptors
M4 segment
Transmembrane domain

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10.1007/978-1-4939-2812-5_1

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PY - 2015/9/25

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KW - M4 segment

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Assaying AMPA receptor oligomerization

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