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dc.contributor.authorFang, Zhiyou
dc.contributor.authorTakizawa, Norio
dc.contributor.authorWilson, Korey A.
dc.contributor.authorSmith, Tara C.
dc.contributor.authorDelprato, Anna M.
dc.contributor.authorDavidson, Michael W.
dc.contributor.authorLambright, David G.
dc.contributor.authorLuna, Elizabeth J.
dc.date2022-08-11T08:09:18.000
dc.date.accessioned2022-08-23T16:25:49Z
dc.date.available2022-08-23T16:25:49Z
dc.date.issued2010-06-25
dc.date.submitted2011-03-14
dc.identifier.citationTraffic. 2010 Jun;11(6):782-99. Epub 2010 Mar 17. <a href="http://dx.doi.org/10.1111/j.1600-0854.2010.01062.x">Link to article on publisher's site</a>
dc.identifier.issn1398-9219 (Linking)
dc.identifier.doi10.1111/j.1600-0854.2010.01062.x
dc.identifier.pmid20331534
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36430
dc.description.abstractIn migrating cells, the cytoskeleton coordinates signal transduction and redistribution of transmembrane proteins, including integrins and growth factor receptors. Supervillin is an F-actin- and myosin II-binding protein that tightly associates with signaling proteins in cholesterol-rich, 'lipid raft' membrane microdomains. We show here that supervillin also can localize with markers for early and sorting endosomes (EE/SE) and with overexpressed components of the Arf6 recycling pathway in the cell periphery. Supervillin tagged with the photoswitchable fluorescent protein, tdEos, moves both into and away from dynamic structures resembling podosomes at the basal cell surface. Rapid integrin recycling from EE/SE is inhibited in supervillin-knockdown cells, but the rates of integrin endocytosis and recycling from the perinuclear recycling center (PNRC) are unchanged. A lack of synergy between supervillin knockdown and the actin filament barbed-end inhibitor, cytochalasin D, suggests that both treatments affect actin-dependent rapid recycling. Supervillin also enhances signaling from the epidermal growth factor receptor (EGFR) to extracellular signal-regulated kinases (ERKs) 1 and 2 and increases the velocity of cell translocation. These results suggest that supervillin, F-actin and associated proteins coordinate a rapid, basolateral membrane recycling pathway that contributes to ERK signaling and actin-based cell motility.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=20331534&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1111/j.1600-0854.2010.01062.x
dc.subjectActins
dc.subjectAnimals
dc.subjectCOS Cells
dc.subject*Cell Movement
dc.subjectCercopithecus aethiops
dc.subjectCytochalasin D
dc.subjectEndocytosis
dc.subjectEndosomes
dc.subjectExtracellular Signal-Regulated MAP Kinases
dc.subjectHela Cells
dc.subjectHumans
dc.subjectIntegrins
dc.subjectMembrane Proteins
dc.subjectMicrofilament Proteins
dc.subjectReceptor, Epidermal Growth Factor
dc.subjectSignal Transduction
dc.subjectCell Biology
dc.titleThe membrane-associated protein, supervillin, accelerates F-actin-dependent rapid integrin recycling and cell motility
dc.typeJournal Article
dc.source.journaltitleTraffic (Copenhagen, Denmark)
dc.source.volume11
dc.source.issue6
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/luna/1
dc.identifier.contextkey1872112
html.description.abstract<p>In migrating cells, the cytoskeleton coordinates signal transduction and redistribution of transmembrane proteins, including integrins and growth factor receptors. Supervillin is an F-actin- and myosin II-binding protein that tightly associates with signaling proteins in cholesterol-rich, 'lipid raft' membrane microdomains. We show here that supervillin also can localize with markers for early and sorting endosomes (EE/SE) and with overexpressed components of the Arf6 recycling pathway in the cell periphery. Supervillin tagged with the photoswitchable fluorescent protein, tdEos, moves both into and away from dynamic structures resembling podosomes at the basal cell surface. Rapid integrin recycling from EE/SE is inhibited in supervillin-knockdown cells, but the rates of integrin endocytosis and recycling from the perinuclear recycling center (PNRC) are unchanged. A lack of synergy between supervillin knockdown and the actin filament barbed-end inhibitor, cytochalasin D, suggests that both treatments affect actin-dependent rapid recycling. Supervillin also enhances signaling from the epidermal growth factor receptor (EGFR) to extracellular signal-regulated kinases (ERKs) 1 and 2 and increases the velocity of cell translocation. These results suggest that supervillin, F-actin and associated proteins coordinate a rapid, basolateral membrane recycling pathway that contributes to ERK signaling and actin-based cell motility.</p>
dc.identifier.submissionpathluna/1
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages782-99


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