Biochemical Characterization of Ezrin-Actin Interaction (*)

The highly related actin isoforms are thought to have different functions. We recently demonstrated a polarized distribution of actin isoforms in gastric parietal cells and association of gastric ezrin with the cytoplasmic β-actin isoform (Yao, X., Chaponnier, C., Gabbiani, G., and Forte, J. G.(1995) Mol. Biol. Cell. 6, 541-557). Here we used ultrastructural immunocytochemistry to verify that β-actin is located within canalicular microvilli and the apical cortex of parietal cells, similar to the localization reported for ezrin. Furthermore, we tested whether ezrin binds preferentially to cytoplasmic β-actin compared with the skeletal muscle α-actin isoform. Purified cytoplasmic β-actin (from erythrocytes) and skeletal α-actin were assembled with gastric ezrin. Co-sedimentation experiments showed that gastric ezrin selectively co-pelleted with the β-actin isoform and only very poorly with α-actin. Binding of erythrocytic β-actin to ezrin is saturable with a molar ratio of 1:10 (ezrin:actin) and a dissociation constant 4.6 × 10M. In addition, ezrin promoted pyrene-labeled actin assembly, with predominant effects on filament elongation and a distinct preference for β-actin compared with α-actin. Given these isoform-selective associations, we speculate that actin isoforms might segregate into different functional domains and exert specificity by interacting with isoform-orientated binding proteins.

• Publication year

  1996

• Venue

  Journal of Biological Chemistry

• Publication date

  1996-03-22

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1074/JBC.271.12.7224PMID 8636161
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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