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Adducin: a physical model with implications for function in assembly of spectrin-actin complexes.

Publication ,  Journal Article
Hughes, CA; Bennett, V
Published in: J Biol Chem
August 11, 1995

Adducin binds to spectrin-actin complexes, promotes association of spectrin with actin, and is subject to regulation by calmodulin as well as protein kinases A and C. Adducin is a heteromer comprised of homologous alpha and beta-subunits with an NH2-terminal protease-resistant head domain, connected by a neck region to a COOH-terminal hydrophilic, protease-sensitive region. This study provides evidence that adducin in solution is a mixture of heterodimers and tetramers. CD spectroscopy of COOH-terminal domains of alpha- and beta-adducin bacterial recombinants provides direct evidence for an unstructured random coil configuration. Cross-linking, proteolysis, and blot-binding experiments suggest a model for the adducin tetramer in which four head domains contact one another to form a globular core with extended interacting alpha- and beta-adducin tails. The site for binding to spectrin-actin complexes on adducin was identified as the COOH-terminal tail of both the alpha- and beta-adducin subunits. The capacity of native adducin to recruit spectrin to actin filaments is similar to that of adducin tail domains. Thus, adducin tail domains alone are sufficient to interact with F-actin and a single spectrin and to recruit additional spectrin molecules to the ternary complex.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

August 11, 1995

Volume

270

Issue

32

Start / End Page

18990 / 18996

Location

United States

Related Subject Headings

  • Spectrin
  • Recombinant Proteins
  • Rabbits
  • Models, Structural
  • Humans
  • Calmodulin-Binding Proteins
  • Blood Proteins
  • Biochemistry & Molecular Biology
  • Animals
  • Actins
 

Citation

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Hughes, C. A., & Bennett, V. (1995). Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. J Biol Chem, 270(32), 18990–18996. https://doi.org/10.1074/jbc.270.32.18990
Hughes, C. A., and V. Bennett. “Adducin: a physical model with implications for function in assembly of spectrin-actin complexes.J Biol Chem 270, no. 32 (August 11, 1995): 18990–96. https://doi.org/10.1074/jbc.270.32.18990.
Hughes CA, Bennett V. Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. J Biol Chem. 1995 Aug 11;270(32):18990–6.
Hughes, C. A., and V. Bennett. “Adducin: a physical model with implications for function in assembly of spectrin-actin complexes.J Biol Chem, vol. 270, no. 32, Aug. 1995, pp. 18990–96. Pubmed, doi:10.1074/jbc.270.32.18990.
Hughes CA, Bennett V. Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. J Biol Chem. 1995 Aug 11;270(32):18990–18996.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

August 11, 1995

Volume

270

Issue

32

Start / End Page

18990 / 18996

Location

United States

Related Subject Headings

  • Spectrin
  • Recombinant Proteins
  • Rabbits
  • Models, Structural
  • Humans
  • Calmodulin-Binding Proteins
  • Blood Proteins
  • Biochemistry & Molecular Biology
  • Animals
  • Actins