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Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2.

CD44 has been identified as a membrane-binding partner for ezrin/radixin/moesin (ERM) proteins, plasma membrane/actin filament cross-linkers. ERM proteins, however, are not necessarily colocalized with CD44 in tissues, but with CD43 and ICAM-2 in some types of cells. We found that glutathione-S-transferase fusion proteins with the cytoplasmic domain of CD43 and ICAM-2, as well as CD44, bound to moesin in vitro. The regions responsible for the in vitro binding of CD43 and CD44 to moesin were narrowed down to their juxta-membrane 20-30-amino acid sequences in the cytoplasmic domain. These sequences and the cytoplasmic domain of ICAM-2 (28 amino acids) were all characterized by the positively charged amino acid clusters. When E-cadherin chimeric molecules bearing these positively charged amino acid clusters of CD44, CD43, or ICAM-2 were expressed in mouse L fibroblasts, they were co-concentrated with ERM proteins at microvilli, whereas those lacking these clusters were diffusely distributed on the cell surface. The specific binding of ERM proteins to the juxta-membrane positively charged amino acid clusters of CD44, CD43, and ICAM-2 was confirmed by immunoprecipitation and site-directed mutagenesis. From these findings, we conclude that ERM proteins bind to integral membrane proteins bearing a positively charged amino acid cluster in their juxta-membrane cytoplasmic domain.

Pubmed ID: 9472040


  • Yonemura S
  • Hirao M
  • Doi Y
  • Takahashi N
  • Kondo T
  • Tsukita S
  • Tsukita S


The Journal of cell biology

Publication Data

February 23, 1998

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Amino Acids
  • Animals
  • Antigens, CD
  • Antigens, CD43
  • Antigens, CD44
  • Binding Sites
  • Blood Proteins
  • Cadherins
  • Cell Adhesion Molecules
  • Cells, Cultured
  • Cytoplasm
  • Cytoskeletal Proteins
  • Glutathione Transferase
  • L Cells (Cell Line)
  • Membrane Proteins
  • Mice
  • Microfilament Proteins
  • Microvilli
  • Molecular Sequence Data
  • Phosphoproteins
  • Precipitin Tests
  • Protein Binding
  • Protein Structure, Tertiary
  • Proteins
  • Recombinant Fusion Proteins
  • Sequence Homology, Amino Acid
  • Sialoglycoproteins
  • Transfection