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dc.contributor.authorPestonjamasp, Kersi N.
dc.contributor.authorPope, Robert K.
dc.contributor.authorWulfkuhle, J. D.
dc.contributor.authorLuna, Elizabeth J.
dc.date2022-08-11T08:11:04.000
dc.date.accessioned2022-08-23T17:31:35Z
dc.date.available2022-08-23T17:31:35Z
dc.date.issued1998-01-07
dc.date.submitted2007-11-28
dc.identifier.citation<p>J Cell Biol. 1997 Dec 1;139(5):1255-69. <a href="http://dx.doi.org/10.1083/jcb.139.5.1255 ">Link to article on publisher's website</a></p>
dc.identifier.issn0021-9525 (Print)
dc.identifier.doi10.1083/jcb.139.5.1255
dc.identifier.pmid9382871
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50769
dc.description.abstractActin-binding membrane proteins are involved in both adhesive interactions and motile processes. We report here the purification and initial characterization of p205, a 205-kD protein from bovine neutrophil plasma membranes that binds to the sides of actin filaments in blot overlays. p205 is a tightly bound peripheral membrane protein that cosediments with endogenous actin in sucrose gradients and immunoprecipitates. Amino acid sequences were obtained from SDS-PAGE-purified p205 and used to generate antipeptide antibodies, immunolocalization data, and cDNA sequence information. The intracellular localization of p205 in MDBK cells is a function of cell density and adherence state. In subconfluent cells, p205 is found in punctate spots along the plasma membrane and in the cytoplasm and nucleus; in adherent cells, p205 concentrates with E-cadherin at sites of lateral cell-cell contact. Upon EGTA-mediated cell dissociation, p205 is internalized with E-cadherin and F-actin as a component of adherens junctions "rings." At later times, p205 is observed in cytoplasmic punctae. The high abundance of p205 in neutrophils and suspension-grown HeLa cells, which lack adherens junctions, further suggests that this protein may play multiple roles during cell growth, adhesion, and motility. Molecular cloning of p205 cDNA reveals a bipartite structure. The COOH terminus exhibits a striking similarity to villin and gelsolin, particularly in regions known to bind F-actin. The NH2 terminus is novel, but contains four potential nuclear targeting signals. Because p205 is now the largest known member of the villin/gelsolin superfamily, we propose the name, "supervillin." We suggest that supervillin may be involved in actin filament assembly at adherens junctions and that it may play additional roles in other cellular compartments.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9382871&dopt=Abstract">Link to article in PubMed</a></p>
dc.rightsPublisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.subjectActins
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCarrier Proteins
dc.subjectCattle
dc.subjectCell Fractionation
dc.subjectCloning, Molecular
dc.subjectDogs
dc.subjectEpithelial Cells
dc.subjectGelsolin
dc.subjectIntercellular Junctions
dc.subjectKidney
dc.subjectMembrane Proteins
dc.subjectMicrofilament Proteins
dc.subjectMicrofilaments
dc.subjectMolecular Sequence Data
dc.subject*Multigene Family
dc.subjectNeutrophils
dc.subjectNuclear Localization Signals
dc.subjectProtein Binding
dc.subjectSequence Analysis, DNA
dc.subjectSequence Homology, Amino Acid
dc.subjectTissue Distribution
dc.subjectCell Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleSupervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily
dc.typeJournal Article
dc.source.journaltitleThe Journal of cell biology
dc.source.volume139
dc.source.issue5
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1295&amp;context=wfc_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/wfc_pp/296
dc.identifier.contextkey397386
refterms.dateFOA2022-08-23T17:31:36Z
html.description.abstract<p>Actin-binding membrane proteins are involved in both adhesive interactions and motile processes. We report here the purification and initial characterization of p205, a 205-kD protein from bovine neutrophil plasma membranes that binds to the sides of actin filaments in blot overlays. p205 is a tightly bound peripheral membrane protein that cosediments with endogenous actin in sucrose gradients and immunoprecipitates. Amino acid sequences were obtained from SDS-PAGE-purified p205 and used to generate antipeptide antibodies, immunolocalization data, and cDNA sequence information. The intracellular localization of p205 in MDBK cells is a function of cell density and adherence state. In subconfluent cells, p205 is found in punctate spots along the plasma membrane and in the cytoplasm and nucleus; in adherent cells, p205 concentrates with E-cadherin at sites of lateral cell-cell contact. Upon EGTA-mediated cell dissociation, p205 is internalized with E-cadherin and F-actin as a component of adherens junctions "rings." At later times, p205 is observed in cytoplasmic punctae. The high abundance of p205 in neutrophils and suspension-grown HeLa cells, which lack adherens junctions, further suggests that this protein may play multiple roles during cell growth, adhesion, and motility. Molecular cloning of p205 cDNA reveals a bipartite structure. The COOH terminus exhibits a striking similarity to villin and gelsolin, particularly in regions known to bind F-actin. The NH2 terminus is novel, but contains four potential nuclear targeting signals. Because p205 is now the largest known member of the villin/gelsolin superfamily, we propose the name, "supervillin." We suggest that supervillin may be involved in actin filament assembly at adherens junctions and that it may play additional roles in other cellular compartments.</p>
dc.identifier.submissionpathwfc_pp/296
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages1255-69


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Publisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.
Except where otherwise noted, this item's license is described as Publisher PDF posted as allowed by the publisher's terms of use policy at: http://www.rupress.org/terms After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Article under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode, or updates thereof.