Adducin: structure, function and regulation

@article{Matsuoka2000AdducinSF,
  title={Adducin: structure, function and regulation
},
  author={Yoichiro Matsuoka and X. Li and Vann Bennett},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2000},
  volume={57},
  pages={884-895}
}
Abstract. Adducin is a ubiquitously expressed membrane-skeletal protein localized at spectrin-actin junctions that binds calmodulin and is an in vivo substrate for protein kinase C (PKC) and Rho-associated kinase. Adducin is a tetramer comprised of either α/β or α/γ heterodimers. Adducin subunits are related in sequence and all contain an N-terminal globular head domain, a neck domain and a C-terminal protease-sensitive tail domain. The tail domains of all adducin subunits end with a highly… 
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TLDR
Findings suggest a complex reciprocal relationship between regulation of adducin function by calmodulin binding and phosphorylation by PKA and PKC.
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TLDR
Evidence is provided that adducin in solution is a mixture of heterodimers and tetramers, and cross-linking, proteolysis, and blot-binding experiments suggest a model for the ad Ducin tetramer in which four head domains contact one another to form a globular core with extended interacting α- and β-adducin tails.
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TLDR
A novel function is demonstrated for adducin; it completely blocks elongation and depolymerization at the barbed ends of actin filaments, thus functioning as a barbed end capping protein (K 100 nM).
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TLDR
The complete sequence of both subunits of human adducin, alpha (737 amino acids), and beta (726 amino acids) has been deduced by analysis of the cDNAs, suggesting evolution by gene duplication.
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TLDR
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TLDR
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TLDR
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TLDR
Results demonstrate an unanticipated role of the first repeat of β-spectrin in actin binding activity and of the second repeat in association with adducin/actin, and imply the possibility of an extended contact between ad Ducin, spectrin, and actin involving several actin subunits.
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TLDR
It is demonstrated that a membrane-skeleton-associated calmodulin-binding protein of erythrocytes, called adducin, binds tightly in vitro to spectrin-actin complexes but with much less affinity either toSpectrin or to actin alone, and is inhibited in its ability to induce the binding of additional spectrin molecules toActin by micromolar concentrations of cal modulin and Ca2+.
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