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Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes.

Publication ,  Journal Article
Mohler, PJ; Yoon, W; Bennett, V
Published in: J Biol Chem
September 17, 2004

Ankyrin-B is a spectrin-binding protein that is required for localization of inositol 1,4,5-trisphosphate receptor and ryanodine receptor in neonatal cardiomyocytes. This work addresses the interaction between ankyrin-B and beta(2)-spectrin in these cells. Ankyrin-B and beta(2)-spectrin are colocalized in an intracellular striated compartment overlying the M-line and distinct from T-tubules, sarcoplasmic reticulum, Golgi, endoplasmic reticulum, lysosomes, and endosomes. Beta(2)-Spectrin is absent in ankyrin-B-null cardiomyocytes and is restored to a normal striated pattern by rescue with green fluorescent protein-220-kDa ankyrin-B. We identified two mutants (A1000P and DAR976AAA) located in the ZU5 domain which eliminate spectrin binding activity of ankyrin-B. Ankyrin-B mutants lacking spectrin binding activity are normally targeted but do not reestablish beta(2)-spectrin in ankyrin-B(+/-) cardiomyocytes. However, both mutant forms of ankyrin-B are still capable of restoring inositol 1,4,5-trisphosphate receptor localization and normal contraction frequency of cardiomyocytes. Therefore, direct binding of beta(2)-spectrin to ankyrin-B is required for the normal targeting of beta(2)-spectrin in neonatal cardiomyocytes. In contrast, ankyrin-B localization and function are independent of beta(2)-spectrin. In summary, this work demonstrates that interaction between members of the ankyrin and beta-spectrin families previously established in erythrocytes and axon initial segments also occurs in neonatal cardiomyocytes with ankyrin-B and beta(2)-spectrin. This work also establishes a functional hierarchy in which ankyrin-B determines the localization of beta(2)-spectrin and operates independently of beta(2)-spectrin in its role in organizing membrane-spanning proteins.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

September 17, 2004

Volume

279

Issue

38

Start / End Page

40185 / 40193

Location

United States

Related Subject Headings

  • Spectrin
  • Receptors, Cytoplasmic and Nuclear
  • Protein Structure, Tertiary
  • Myocytes, Cardiac
  • Myocardial Contraction
  • Mutagenesis
  • Molecular Sequence Data
  • Mice
  • Membrane Proteins
  • Inositol 1,4,5-Trisphosphate Receptors
 

Citation

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Mohler, P. J., Yoon, W., & Bennett, V. (2004). Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes. J Biol Chem, 279(38), 40185–40193. https://doi.org/10.1074/jbc.M406018200
Mohler, Peter J., Woohyun Yoon, and Vann Bennett. “Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes.J Biol Chem 279, no. 38 (September 17, 2004): 40185–93. https://doi.org/10.1074/jbc.M406018200.
Mohler PJ, Yoon W, Bennett V. Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes. J Biol Chem. 2004 Sep 17;279(38):40185–93.
Mohler, Peter J., et al. “Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes.J Biol Chem, vol. 279, no. 38, Sept. 2004, pp. 40185–93. Pubmed, doi:10.1074/jbc.M406018200.
Mohler PJ, Yoon W, Bennett V. Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes. J Biol Chem. 2004 Sep 17;279(38):40185–40193.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

September 17, 2004

Volume

279

Issue

38

Start / End Page

40185 / 40193

Location

United States

Related Subject Headings

  • Spectrin
  • Receptors, Cytoplasmic and Nuclear
  • Protein Structure, Tertiary
  • Myocytes, Cardiac
  • Myocardial Contraction
  • Mutagenesis
  • Molecular Sequence Data
  • Mice
  • Membrane Proteins
  • Inositol 1,4,5-Trisphosphate Receptors