NDLI: Phospho-dependent binding of the clathrin AP2 adaptor complex to GABAA receptors regulates the efficacy of inhibitory synaptic transmission

Content Provider	PubMed Central
Author	Kittler, Josef T. Chen, Guojun Honing, Stephan Bogdanov, Yury Kristina, Mcainsh Lorena, Arancibia-carcamo I. Jovanovic, Jasmina N. Pangalos, Menelas N. Haucke, Volker Yan, Zhen Moss, Stephen J.
Copyright Year	2005
Abstract	The efficacy of synaptic inhibition depends on the number of γ-aminobutyric acid type A receptors (GABAARs) expressed on the cell surface of neurons. The clathrin adaptor protein 2 (AP2) complex is a critical regulator of GABAAR endocytosis and, hence, surface receptor number. Here, we identify a previously uncharacterized atypical AP2 binding motif conserved within the intracellular domains of all GABAAR β subunit isoforms. This AP2 binding motif (KTHLRRRSSQLK in the β3 subunit) incorporates the major sites of serine phosphorylation within receptor β subunits, and phosphorylation within this site inhibits AP2 binding. Furthermore, by using surface plasmon resonance, we establish that a peptide (pepβ3) corresponding to the AP2 binding motif in the GABAAR β3 subunit binds to AP2 with high affinity only when dephosphorylated. Moreover, the pepβ3 peptide, but not its phosphorylated equivalent (pepβ3-phos), enhanced the amplitude of miniature inhibitory synaptic current and whole cell GABAAR current. These effects of pepβ3 on GABAAR current were occluded by inhibitors of dynamin-dependent endocytosis supporting an action of pepβ3 on GABAAR endocytosis. Therefore phospho-dependent regulation of AP2 binding to GABAARs provides a mechanism to specify receptor cell surface number and the efficacy of inhibitory synaptic transmission.
Related Links	http://dx.doi.org/10.1073/pnas.0506653102
Starting Page	14871
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	41
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-10-11
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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