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dc.contributor.authorPestonjamasp, K.
dc.contributor.authorAmieva, M. R.
dc.contributor.authorStrassel, C. P.
dc.contributor.authorNauseef, W. M.
dc.contributor.authorFurthmayr, H.
dc.contributor.authorLuna, Elizabeth J.
dc.date2022-08-11T08:11:04.000
dc.date.accessioned2022-08-23T17:31:34Z
dc.date.available2022-08-23T17:31:34Z
dc.date.issued1995-03-01
dc.date.submitted2007-11-13
dc.identifier.citationMol Biol Cell. 1995 Mar;6(3):247-59. <a href="http://www.molbiolcell.org/cgi/content/abstract/6/3/247">Link to article on publisher's website</a>
dc.identifier.issn1059-1524 (Print)
dc.identifier.pmid7612961
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50763
dc.description.abstractActin-binding proteins in bovine neutrophil plasma membranes were identified using blot overlays with 125I-labeled F-actin. Along with surface-biotinylated proteins, membranes were enriched in major actin-binding polypeptides of 78, 81, and 205 kDa. Binding was specific for F-actin because G-actin did not bind. Further, unlabeled F-actin blocked the binding of 125I-labeled F-actin whereas other acidic biopolymers were relatively ineffective. Binding also was specifically inhibited by myosin subfragment 1, but not by CapZ or plasma gelsolin, suggesting that the membrane proteins, like myosin, bind along the sides of the actin filaments. The 78- and 81-kDa polypeptides were identified as moesin and ezrin, respectively, by co-migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoprecipitation with antibodies specific for moesin and ezrin. Although not present in detectable amounts in bovine neutrophils, radixin (a third and closely related member of this gene family) also bound 125I-labeled F-actin on blot overlays. Experiments with full-length and truncated bacterial fusion proteins localized the actin-binding site in moesin to the extreme carboxy terminus, a highly conserved sequence. Immunofluorescence micrographs of permeabilized cells and cell "footprints" showed moesin co-localization with actin at the cytoplasmic surface of the plasma membrane, consistent with a role as a membrane-actin-linking protein.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7612961&dopt=Abstract">Link to article in PubMed</a>
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBase Sequence
dc.subjectBlood Proteins
dc.subjectCattle
dc.subject*Cytoskeletal Proteins
dc.subjectCytoskeleton
dc.subjectMembrane Proteins
dc.subjectMice
dc.subjectMicrofilament Proteins
dc.subjectMolecular Sequence Data
dc.subjectNeutrophils
dc.subjectPhosphoproteins
dc.subjectProteins
dc.subjectSequence Alignment
dc.subjectSequence Deletion
dc.subjectSequence Homology
dc.subjectCell Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMoesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes
dc.typeArticle
dc.source.journaltitleMolecular biology of the cell
dc.source.volume6
dc.source.issue3
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1289&amp;context=wfc_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/wfc_pp/290
dc.identifier.contextkey392374
refterms.dateFOA2022-08-23T17:31:34Z
html.description.abstract<p>Actin-binding proteins in bovine neutrophil plasma membranes were identified using blot overlays with 125I-labeled F-actin. Along with surface-biotinylated proteins, membranes were enriched in major actin-binding polypeptides of 78, 81, and 205 kDa. Binding was specific for F-actin because G-actin did not bind. Further, unlabeled F-actin blocked the binding of 125I-labeled F-actin whereas other acidic biopolymers were relatively ineffective. Binding also was specifically inhibited by myosin subfragment 1, but not by CapZ or plasma gelsolin, suggesting that the membrane proteins, like myosin, bind along the sides of the actin filaments. The 78- and 81-kDa polypeptides were identified as moesin and ezrin, respectively, by co-migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoprecipitation with antibodies specific for moesin and ezrin. Although not present in detectable amounts in bovine neutrophils, radixin (a third and closely related member of this gene family) also bound 125I-labeled F-actin on blot overlays. Experiments with full-length and truncated bacterial fusion proteins localized the actin-binding site in moesin to the extreme carboxy terminus, a highly conserved sequence. Immunofluorescence micrographs of permeabilized cells and cell "footprints" showed moesin co-localization with actin at the cytoplasmic surface of the plasma membrane, consistent with a role as a membrane-actin-linking protein.</p>
dc.identifier.submissionpathwfc_pp/290
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages247-59


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