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dc.contributor.authorMathew, Dennis
dc.contributor.authorPopescue, Andrei
dc.contributor.authorBudnik, Vivian
dc.date2022-08-11T08:09:30.000
dc.date.accessioned2022-08-23T16:33:11Z
dc.date.available2022-08-23T16:33:11Z
dc.date.issued2003-11-19
dc.date.submitted2012-05-24
dc.identifier.citationJ Neurosci. 2003 Nov 19;23(33):10710-6. <a href="http://www.jneurosci.org/content/23/33/10710.full.pdf+html" target="_blank">Link to article on publisher's website</a>
dc.identifier.issn0270-6474 (Linking)
dc.identifier.pmid14627656
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38046
dc.description.abstractRecent studies have revealed that endocytosis and exocytosis of postsynaptic receptors play a major role in the regulation of synaptic function, particularly during long-term potentiation and long-term depression. Interestingly, many of the proteins implicated in exocytosis and endocytosis of synaptic vesicles are also involved in postsynaptic protein cycling. In vertebrates, Amphiphysin is postulated to function during endocytosis in nerve terminals; however, several recent reports using a Drosophila amphiphysin (damph) null mutant have failed to substantiate such a role at fly synapses. In addition, Damph is surprisingly enriched at the postsynapse. Here we used the glutamatergic larval neuromuscular junction to study the synaptic role of Damph. By selectively labeling internal and external pools of the cell adhesion molecule Fasciclin II (FasII), and by using a novel in vivo surface FasII immunocapture protocol, we show that the level of external FasII is decreased in damph mutants although the total level of FasII remains constant. In vivo FasII internalization assays indicate that the reincorporation of FasII molecules into the cell surface is severely inhibited in damph mutants. Moreover, we show that blocking soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) function in postsynaptic muscle cells interferes with FasII exocytosis. These experiments suggest that in Drosophila, Damph functions during SNARE-dependent postsynaptic FasII membrane cycling. This study challenges the notion that synaptic Amphiphysin is involved exclusively in endocytosis and suggests a novel role for this protein in postsynaptic exocytosis.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=14627656&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jneurosci.org/content/23/33/10710.full.pdf+html
dc.rightsPublisher PDF posted as allowed by the publisher's author rights policy at http://www.jneurosci.org/site/misc/ifa_policies.xhtml#copyright.
dc.subjectAnimals
dc.subjectCell Adhesion Molecules, Neuronal
dc.subject*Drosophila
dc.subjectExocytosis
dc.subjectLarva
dc.subjectMembrane Proteins
dc.subjectMuscles
dc.subjectMutation
dc.subjectNerve Tissue Proteins
dc.subjectNeuromuscular Junction
dc.subjectNeuronal Plasticity
dc.subjectSNARE Proteins
dc.subjectSynaptic Membranes
dc.subject*Vesicular Transport Proteins
dc.subjectNeuroscience and Neurobiology
dc.titleDrosophila amphiphysin functions during synaptic Fasciclin II membrane cycling
dc.typeJournal Article
dc.source.journaltitleThe Journal of neuroscience : the official journal of the Society for Neuroscience
dc.source.volume23
dc.source.issue33
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1078&amp;context=neurobiology_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/neurobiology_pp/79
dc.identifier.contextkey2911194
refterms.dateFOA2022-08-23T16:33:11Z
html.description.abstract<p>Recent studies have revealed that endocytosis and exocytosis of postsynaptic receptors play a major role in the regulation of synaptic function, particularly during long-term potentiation and long-term depression. Interestingly, many of the proteins implicated in exocytosis and endocytosis of synaptic vesicles are also involved in postsynaptic protein cycling. In vertebrates, Amphiphysin is postulated to function during endocytosis in nerve terminals; however, several recent reports using a Drosophila amphiphysin (damph) null mutant have failed to substantiate such a role at fly synapses. In addition, Damph is surprisingly enriched at the postsynapse. Here we used the glutamatergic larval neuromuscular junction to study the synaptic role of Damph. By selectively labeling internal and external pools of the cell adhesion molecule Fasciclin II (FasII), and by using a novel in vivo surface FasII immunocapture protocol, we show that the level of external FasII is decreased in damph mutants although the total level of FasII remains constant. In vivo FasII internalization assays indicate that the reincorporation of FasII molecules into the cell surface is severely inhibited in damph mutants. Moreover, we show that blocking soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) function in postsynaptic muscle cells interferes with FasII exocytosis. These experiments suggest that in Drosophila, Damph functions during SNARE-dependent postsynaptic FasII membrane cycling. This study challenges the notion that synaptic Amphiphysin is involved exclusively in endocytosis and suggests a novel role for this protein in postsynaptic exocytosis.</p>
dc.identifier.submissionpathneurobiology_pp/79
dc.contributor.departmentBudnik Lab
dc.contributor.departmentNeurobiology
dc.source.pages10710-6


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