A novel 4.1 ezrin radixin moesin (FERM)-containing protein, 'Willin'

Frank J Gunn-Moore, Gavin I Welsh, Lissa R Herron, Frances Brannigan, Kanamarlapudi Venkateswarlu, Stewart Gillespie, Margaret Brandwein-Gensler, Rashna Madan, Jeremy M Tavaré, Peter J Brophy, Michael B Prystowsky, Simon Guild

Research output: Contribution to journalArticlepeer-review

Abstract

The 4.1 superfamily of proteins contain a 4.1 Ezrin Radixin Moesin (FERM) domain and are described as linking the cytoskeleton with the plasma membrane. Here, we describe a new FERM domain-containing protein called Willin. Willin has a recognizable FERM domain within its N-terminus and is capable of binding phospholipids. Its intra-cellular distribution can be cytoplasmic or at the plasma membrane where it can co-localize with actin. However, the plasma membrane location of Willin is not influenced by cytochalasin D induced actin disruption but it is induced by the addition of epidermal growth factor.
Original languageEnglish
Pages (from-to)5089-94
Number of pages6
JournalFEBS Letters
Volume579
Issue number22
DOIs
Publication statusPublished - 2005

Keywords

  • Adaptor Proteins, Signal Transducing/genetics
  • Adaptor Proteins, Signal Transducing/metabolism
  • Amino Acid Sequence
  • Animals
  • Blood Proteins/genetics
  • Blood Proteins/metabolism
  • Cell Line
  • Cell Membrane/chemistry
  • Cell Membrane/metabolism
  • Cytoskeletal Proteins/genetics
  • Cytoskeletal Proteins/metabolism
  • Humans
  • Membrane Proteins/genetics
  • Membrane Proteins/metabolism
  • Microfilament Proteins/genetics
  • Microfilament Proteins/metabolism
  • Molecular Sequence Data
  • Multigene Family
  • Phospholipids/metabolism
  • Phosphoproteins/genetics
  • Phosphoproteins/metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Rats
  • Recombinant Fusion Proteins/genetics
  • Recombinant Fusion Proteins/metabolism
  • Sequence Alignment

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