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The EHD protein Past1 controls postsynaptic membrane elaboration and synaptic function
Journal article   Open access   Peer reviewed

The EHD protein Past1 controls postsynaptic membrane elaboration and synaptic function

Kate Koles, Emily M Messelaar, Zachary Feiger, Crystal J Yu, C Andrew Frank and Avital A Rodal
Molecular biology of the cell, Vol.26(18), pp.3275-3288
09/15/2015
DOI: 10.1091/mbc.E15-02-0093
PMCID: PMC4569317
PMID: 26202464
url
https://doi.org/10.1091/mbc.E15-02-0093View
Published (Version of record) Open Access

Abstract

Membranes form elaborate structures that are highly tailored to their specialized cellular functions, yet the mechanisms by which these structures are shaped remain poorly understood. Here, we show that the conserved membrane-remodeling C-terminal Eps15 Homology Domain (EHD) protein Past1 is required for the normal assembly of the subsynaptic muscle membrane reticulum (SSR) at the Drosophila melanogaster larval neuromuscular junction (NMJ). past1 mutants exhibit altered NMJ morphology, decreased synaptic transmission, reduced glutamate receptor levels, and a deficit in synaptic homeostasis. The membrane-remodeling proteins Amphiphysin and Syndapin colocalize with Past1 in distinct SSR subdomains and collapse into Amphiphysin-dependent membrane nodules in the SSR of past1 mutants. Our results suggest a mechanism by which the coordinated actions of multiple lipid-binding proteins lead to the elaboration of increasing layers of the SSR and uncover new roles for an EHD protein at synapses.
Nerve Tissue Proteins - metabolism Receptors, Glutamate - metabolism Animals Carrier Proteins - metabolism Larva Neuromuscular Junction - metabolism Presynaptic Terminals - metabolism Adaptor Proteins, Signal Transducing - metabolism Drosophila Proteins - metabolism Drosophila melanogaster Synaptic Membranes - metabolism

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