Journal
NEURON
Volume 86, Issue 2, Pages 475-489Publisher
CELL PRESS
DOI: 10.1016/j.neuron.2015.03.013
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Funding
- French National Research Agency [ANR-10-INSB-04]
- Ministere de l'Enseignement Superieur et de la Recherche (France) [ANR-10-INBS-04]
- Centre National de la Recherche Scientifique
- Conseil Regional d'Aquitaine
- European Research Council (ERC)
- Marie-Curie Intra-European fellowship [273817]
- EMBO [ALTF 129-2009]
- Marie Curie grant Synapsemap
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PSD-95 is a prominent organizer of the postsynaptic density (PSD) that can present a filamentous orientation perpendicular to the plasma membrane. Interactions between PSD-95 and transmembrane proteins might be particularly sensitive to this orientation, as `` long'' cytoplasmic tails might be required to reach deeper PSD-95 domains. Extension/retraction of transmembrane protein C-tails offer a new way of regulating binding to PSD-95. Using stargazin as a model, we found that enhancing the apparent length of stargazin C-tail through phosphorylation or by an artificial linker was sufficient to potentiate binding to PSD-95, AMPAR anchoring, and synaptic transmission. A linear extension of stargazin C-tail facilitates binding to PSD-95 by preferentially engaging interaction with the farthest located PDZ domains regarding to the plasma membrane, which present a greater affinity for the stargazin PDZ-domain-binding motif. Our study reveals that the concerted orientation of the stargazin C-tail and PSD-95 is a major determinant of synaptic strength.
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