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    Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes

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    Authors
    Pestonjamasp, K.
    Amieva, M. R.
    Strassel, C. P.
    Nauseef, W. M.
    Furthmayr, H.
    Luna, Elizabeth J.
    UMass Chan Affiliations
    Department of Cell Biology
    Document Type
    Journal Article
    Publication Date
    1995-03-01
    Keywords
    Amino Acid Sequence
    Animals
    Base Sequence
    Blood Proteins
    Cattle
    *Cytoskeletal Proteins
    Cytoskeleton
    Membrane Proteins
    Mice
    Microfilament Proteins
    Molecular Sequence Data
    Neutrophils
    Phosphoproteins
    Proteins
    Sequence Alignment
    Sequence Deletion
    Sequence Homology
    Cell Biology
    Life Sciences
    Medicine and Health Sciences
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    Abstract
    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.
    Source
    Mol Biol Cell. 1995 Mar;6(3):247-59. Link to article on publisher's website
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/50763
    PubMed ID
    7612961
    Related Resources
    Link to article in PubMed
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    UMass Chan Faculty and Researcher Publications
    Radiology Publications
    Luna Lab

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