Journal article
The EHD protein Past1 controls postsynaptic membrane elaboration and synaptic function
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
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.
Details
- Title: Subtitle
- The EHD protein Past1 controls postsynaptic membrane elaboration and synaptic function
- Creators
- Kate Koles - Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453Emily M Messelaar - Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453Zachary Feiger - Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453Crystal J Yu - Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453C Andrew Frank - Department of Anatomy and Cell Biology, University of Iowa, Iowa City, IA 52242Avital A Rodal - Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02453 arodal@brandeis.edu
- Resource Type
- Journal article
- Publication Details
- Molecular biology of the cell, Vol.26(18), pp.3275-3288
- DOI
- 10.1091/mbc.E15-02-0093
- PMID
- 26202464
- PMCID
- PMC4569317
- NLM abbreviation
- Mol Biol Cell
- ISSN
- 1059-1524
- eISSN
- 1939-4586
- Publisher
- American Society for Cell Biology; United States
- Grant note
- R00 NS062738 / NINDS NIH HHS K99 NS062738 / NINDS NIH HHS P40 OD018537 / NIH HHS DP2 NS082127 / NCCDPHP CDC HHS NS062738 / NINDS NIH HHS P40OD018537 / NIH HHS DP2 NS082127 / NINDS NIH HHS
- Language
- English
- Date published
- 09/15/2015
- Academic Unit
- Anatomy and Cell Biology; Iowa Neuroscience Institute
- Record Identifier
- 9984025420402771
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