Adducin: structure, function and regulation

  title={Adducin: structure, function and regulation
  author={Yoichiro Matsuoka and X. Li and Vann Bennett},
  journal={Cellular and Molecular Life Sciences CMLS},
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… 
Interaction of the SH2 Domain of Fyn with a Cytoskeletal Protein, β-Adducin*
Findings suggest that tyrosine-phosphorylated β-adducin associates with the SH2 domain of Fyn and colocalizes under plasma membranes.
Identification of adducin-binding residues on the cytoplasmic domain of erythrocyte membrane protein, band 3.
Adducin, a major component of the spectrin-actin junctional complex, binds primarily to residues 246-264 of cdb3, and mutation of two exposed glutamic acid residues within this sequence completely abrogates both α- and β-adducin binding.
The cytoskeletal protein adducin and its role in vascular smooth muscle
Actin dynamics are precisely regulated by a large number of actin binding proteins which collectively alter the rates of actin filament assembly and disassembly. Spectrin, an actin cross-linking
Cross-talk unfolded : MARCKS proteins
There is a consensus emerging that MARCKS proteins are ‘natively unfolded’ and this review focuses on recent, mostly biophysical and biochemical results renewing interest in this protein family.
Erythrocyte adducin: a structural regulator of the red blood cell membrane.
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Modulation of Erythrocyte Membrane Mechanical Function by Protein 4.1 Phosphorylation*
It is shown that the phosphorylation of 4.1R by PKC results in its decreased ability to form a ternary complex with spectrin and actin as well as dissociation of glycophorin C from the membrane skeleton, and a marked decrease in membrane mechanical stability.
Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion.
The required relocation of part of the band 3 population to the spectrin/actin junctional complex and its formation of a new bridge with adducin necessitates a significant revision of accepted models of the erythrocyte membrane.


Adducin Regulation
Findings suggest a complex reciprocal relationship between regulation of adducin function by calmodulin binding and phosphorylation by PKA and PKC.
Mapping the domain structure of human erythrocyte adducin.
Adducin: a Physical Model with Implications for Function in Assembly of Spectrin-Actin Complexes (*)
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.
A New Function for Adducin
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).
Primary structure and domain organization of human alpha and beta adducin
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.
Adducin Is an In Vivo Substrate for Protein Kinase C: Phosphorylation in the MARCKS-related Domain Inhibits Activity in Promoting Spectrin–Actin Complexes and Occurs in Many Cells, Including Dendritic Spines of Neurons
The data demonstrate that ad Ducin is a significant in vivo substrate for PKC or other PMA-activated kinases in a variety of cells, and that phosphorylation of adducin occurs in dendritic spines that are believed to respond to external signals by changes in morphology and reorganization of cytoskeletal structures.
Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding
A putative role for adducin is identified, and a calcium- and calmodulin-dependent mechanism whereby higher states of actin association and its interaction with spectrin in the erythrocyte may be controlled is defined.
Identification of the Spectrin Subunit and Domains Required for Formation of Spectrin/Adducin/Actin Complexes*
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.
Modulation of spectrin–actin assembly by erythrocyte adducin
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+.