CPG2 Recruits Endophilin B2 to the Cytoskeleton for Activity-Dependent Endocytosis of Synaptic Glutamate Receptors

Current Biology : CB
Sven LoebrichElly Nedivi

Abstract

Internalization of glutamate receptors at the postsynaptic membrane via clathrin-mediated endocytosis (CME) is a key mechanism for regulating synaptic strength. A role for the F-actin cytoskeleton in CME is well established, and recently, PKA-dependent association of candidate plasticity gene 2 (CPG2) with the spine-cytoskeleton has been shown to mediate synaptic glutamate receptor internalization. Yet, how the endocytic machinery is physically coupled to the actin cytoskeleton to facilitate glutamate receptor internalization has not been demonstrated. Moreover, there has been no distinction of endocytic-machinery components that are specific to activity-dependent versus constitutive glutamate receptor internalization. Here, we show that CPG2, through a direct physical interaction, recruits endophilin B2 (EndoB2) to F-actin, thus anchoring the endocytic machinery to the spine cytoskeleton and facilitating glutamate receptor internalization. Regulation of CPG2 binding to the actin cytoskeleton by protein kinase A directly impacts recruitment of EndoB2 and clathrin. Specific disruption of EndoB2 or the CPG2-EndoB2 interaction impairs activity-dependent, but not constitutive, internalization of both NMDA- and AMPA-type glutamate r...Continue Reading

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Nov 6, 2013·Proceedings of the National Academy of Sciences of the United States of America·Sven LoebrichElly Nedivi

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Citations

Oct 27, 2018·Frontiers in Cellular Neuroscience·Jonathan G Hanley
Feb 6, 2020·International Journal of Molecular Sciences·Silvia PelucchiElena Marcello
Mar 14, 2021·Seminars in Cell & Developmental Biology·Chiara Cirelli, Giulio Tononi

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