ArticleSkeletal muscle2012
Eps homology domain endosomal transport proteins differentially localize to the neuromuscular junction.
Article in Skeletal muscle, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Article
- The endocytic recycling regulatory protein EHD1 Is required for ocular lens development.Developmental biology · 2015Article
- The EHD protein Past1 controls postsynaptic membrane elaboration and synaptic function.Molecular biology of the cell · 2015Article
- Article
- EHD1 mediates vesicle trafficking required for normal muscle growth and transverse tubule development.Developmental biology · 2014Article
- Scratching the surface: actin' and other roles for the C-terminal Eps15 homology domain protein, EHD2.Histology and histopathology · 2014Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
unlabelled
backgroundRecycling of endosomes is important for trafficking and maintenance of proteins at the neuromuscular junction (NMJ). We have previously shown high expression of the endocytic recycling regulator Eps15 homology domain-containing (EHD)1 proteinin the Torpedo californica electric organ, a model tissue for investigating a cholinergic synapse. In this study, we investigated the localization of EHD1 and its paralogs EHD2, EHD3, and EHD4 in mouse skeletal muscle, and assessed the morphological changes in EHD1-/- NMJs.
methodsLocalization of the candidate NMJ protein EHD1 was assessed by confocal microscopy analysis of whole-mount mouse skeletal muscle fibers after direct gene transfer and immunolabeling. The potential function of EHD1 was assessed by specific force measurement and α-bungarotoxin-based endplate morphology mapping in EHD1-/- mouse skeletal muscle.
resultsEndogenous EHD1 localized to primary synaptic clefts of murine NMJ, and this localization was confirmed by expression of recombinant green fluorescent protein labeled-EHD1 in murine skeletal muscle in vivo. EHD1-/- mouse skeletal muscle had normal histology and NMJ morphology, and normal specific force generation during muscle contraction. The EHD 1-4 proteins showed differential localization in skeletal muscle: EHD2 to muscle vasculature, EHD3 to perisynaptic regions, and EHD4 to perinuclear regions and to primary synaptic clefts, but at lower levels than EHD1. Additionally, specific antibodies raised against mammalian EHD1-4 recognized proteins of the expected mass in the T. californica electric organ. Finally, we found that EHD4 expression was more abundant in EHD1-/- mouse skeletal muscle than in wild-type skeletal muscle.
conclusionEHD1 and EHD4 localize to the primary synaptic clefts of the NMJ. Lack of obvious defects in NMJ structure and muscle function in EHD1-/- muscle may be due to functional compensation by other EHD paralogs.
Identifiers
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Registered trials
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