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dc.contributor.authorOkamoto, Patricia M.
dc.contributor.authorGamby, Chantal
dc.contributor.authorWells, David G.
dc.contributor.authorFallon, Justin R.
dc.contributor.authorVallee, Richard B.
dc.date2022-08-11T08:10:03.000
dc.date.accessioned2022-08-23T16:53:54Z
dc.date.available2022-08-23T16:53:54Z
dc.date.issued2001-10-05
dc.date.submitted2008-08-04
dc.identifier.citation<p>J Biol Chem. 2001 Dec 21;276(51):48458-65. Epub 2001 Oct 2. <a href="http://dx.doi.org/10.1074/jbc.M104927200">Link to article on publisher's site</a></p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.M104927200
dc.identifier.pmid11583995
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42381
dc.description.abstractDynamin is a GTPase involved in endocytosis and other aspects of membrane trafficking. A critical function in the presynaptic compartment attributed to the brain-specific dynamin isoform, dynamin-1, is in synaptic vesicle recycling. We report that dynamin-2 specifically interacts with members of the Shank/ProSAP family of postsynaptic density scaffolding proteins and present evidence that dynamin-2 is specifically associated with the postsynaptic density. These data are consistent with a role for this otherwise broadly distributed form of dynamin in glutamate receptor down-regulation and other aspects of postsynaptic membrane turnover.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=11583995&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2715172/
dc.subjectActins
dc.subject*Adaptor Proteins, Signal Transducing
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCOS Cells
dc.subjectCarrier Proteins
dc.subjectCloning, Molecular
dc.subjectDynamin I
dc.subjectDynamins
dc.subjectGTP Phosphohydrolases
dc.subjectNerve Tissue Proteins
dc.subjectPrecipitin Tests
dc.subjectProtein Binding
dc.subjectProtein Isoforms
dc.subjectSynapses
dc.subjectTwo-Hybrid System Techniques
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleDynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume276
dc.source.issue51
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/735
dc.identifier.contextkey564650
html.description.abstract<p>Dynamin is a GTPase involved in endocytosis and other aspects of membrane trafficking. A critical function in the presynaptic compartment attributed to the brain-specific dynamin isoform, dynamin-1, is in synaptic vesicle recycling. We report that dynamin-2 specifically interacts with members of the Shank/ProSAP family of postsynaptic density scaffolding proteins and present evidence that dynamin-2 is specifically associated with the postsynaptic density. These data are consistent with a role for this otherwise broadly distributed form of dynamin in glutamate receptor down-regulation and other aspects of postsynaptic membrane turnover.</p>
dc.identifier.submissionpathoapubs/735
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages48458-65


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