Open AccessProtein kinase C regulates AMPA receptor auxiliary protein Shisa9/ CKAMP 44 through interactions with neuronal scaffold PICK 1
Author(s) -
Kunde StellaAmrei,
Rademacher Nils,
Zieger Hanna,
Shoichet Sarah A.
Publication year - 2017
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12261
Subject(s) - ampa receptor , scaffold protein , neurotransmission , microbiology and biotechnology , chemistry , synaptic plasticity , transmembrane protein , protein kinase a , protein kinase c , glutamate receptor , phosphorylation , biochemistry , receptor , signal transduction , biology
Synaptic α‐amino‐3‐hydroxyl‐5‐methyl‐4‐isoxazole‐propionate ( AMPA ) receptors are essential mediators of neurotransmission in the central nervous system. Shisa9/cysteine‐knot AMPAR modulating protein 44 ( CKAMP 44) is a transmembrane protein recently found to be present in AMPA receptor‐associated protein complexes. Here, we show that the cytosolic tail of Shisa9/ CKAMP 44 interacts with multiple scaffold proteins that are important for regulating synaptic plasticity in central neurons. We focussed on the interaction with the scaffold protein PICK 1, which facilitates the formation of a tripartite complex with the protein kinase C ( PKC ) and thereby regulates phosphorylation of Shisa9/ CKAMP 44 C‐terminal residues. This work has implications for our understanding of how PICK 1 modulates AMPAR ‐mediated transmission and plasticity and also highlights a novel function of PKC .