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Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos.

Publication ,  Journal Article
Kizhatil, K; Davis, JQ; Davis, L; Hoffman, J; Hogan, BLM; Bennett, V
Published in: J Biol Chem
September 7, 2007

E-cadherin is a ubiquitous component of lateral membranes in epithelial tissues and is required to form the first lateral membrane domains in development. Here, we identify ankyrin-G as a molecular partner of E-cadherin and demonstrate that ankyrin-G and beta-2-spectrin are required for accumulation of E-cadherin at the lateral membrane in both epithelial cells and early embryos. Ankyrin-G binds to the cytoplasmic domain of E-cadherin at a conserved site distinct from that of beta-catenin. Ankyrin-G also recruits beta-2-spectrin to E-cadherin-beta-catenin complexes, thus providing a direct connection between E-cadherin and the spectrin/actin skeleton. In addition to restricting the membrane mobility of E-cadherin, ankyrin-G and beta-2-spectrin also are required for exit of E-cadherin from the trans-Golgi network in a microtubule-dependent pathway. Ankyrin-G and beta-2-spectrin co-localize with E-cadherin in preimplantation mouse embryos. Moreover, knockdown of either ankyrin-G or beta-2-spectrin in one cell of a two-cell embryo blocks accumulation of E-cadherin at sites of cell-cell contact. E-cadherin thus requires both ankyrin-G and beta-2-spectrin for its cellular localization in early embryos as well as cultured epithelial cells. We have recently reported that ankyrin-G and beta-2-spectrin collaborate in biogenesis of the lateral membrane ( Kizhatil, K., Yoon, W., Mohler, P. J., Davis, L. H., Hoffman, J. A., and Bennett, V. (2007) J. Biol. Chem. 282, 2029-2037 ). Together with the current findings, these data suggest a ankyrin/spectrin-based mechanism for coordinating membrane assembly with extracellular interactions of E-cadherin at sites of cell-cell contact.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

September 7, 2007

Volume

282

Issue

36

Start / End Page

26552 / 26561

Location

United States

Related Subject Headings

  • trans-Golgi Network
  • beta Catenin
  • Protein Transport
  • Protein Structure, Tertiary
  • Protein Binding
  • Microtubules
  • Microfilament Proteins
  • Mice
  • Intercellular Junctions
  • Humans
 

Citation

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Kizhatil, K., Davis, J. Q., Davis, L., Hoffman, J., Hogan, B. L. M., & Bennett, V. (2007). Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos. J Biol Chem, 282(36), 26552–26561. https://doi.org/10.1074/jbc.M703158200
Kizhatil, Krishnakumar, Jonathan Q. Davis, Lydia Davis, Jan Hoffman, Brigid L. M. Hogan, and Vann Bennett. “Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos.J Biol Chem 282, no. 36 (September 7, 2007): 26552–61. https://doi.org/10.1074/jbc.M703158200.
Kizhatil K, Davis JQ, Davis L, Hoffman J, Hogan BLM, Bennett V. Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos. J Biol Chem. 2007 Sep 7;282(36):26552–61.
Kizhatil, Krishnakumar, et al. “Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos.J Biol Chem, vol. 282, no. 36, Sept. 2007, pp. 26552–61. Pubmed, doi:10.1074/jbc.M703158200.
Kizhatil K, Davis JQ, Davis L, Hoffman J, Hogan BLM, Bennett V. Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos. J Biol Chem. 2007 Sep 7;282(36):26552–26561.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

September 7, 2007

Volume

282

Issue

36

Start / End Page

26552 / 26561

Location

United States

Related Subject Headings

  • trans-Golgi Network
  • beta Catenin
  • Protein Transport
  • Protein Structure, Tertiary
  • Protein Binding
  • Microtubules
  • Microfilament Proteins
  • Mice
  • Intercellular Junctions
  • Humans