Contribution of the different modules in the utrophin carboxy‐terminal region to the formation and regulation of the DAP complex

@article{TommasidiVignano2000ContributionOT,
  title={Contribution of the different modules in the utrophin carboxy‐terminal region to the formation and regulation of the DAP complex},
  author={Alice Tommasi di Vignano and Giovanni di Zenzo and Marius Sudol and Gianni Cesareni and Luciana Dente},
  journal={FEBS Letters},
  year={2000},
  volume={471}
}

ZZ domain is essentially required for the physiological binding of dystrophin and utrophin to beta-dystroglycan.

TLDR
Determination of this binding range is important not only for understanding of the mechanism of dystrophy, but also useful for the design of truncated dystrophin constructs for gene therapy.

ZZ domain of dystrophin and utrophin: topology and mapping of a beta-dystroglycan interaction site.

TLDR
The results suggest that residues 3326-3332 of dystrophin form a crucial part of the contact region between dyStrophin and beta-dystroglycan and provide new insight into ZZ domain organization and function.

Structural comparison of actin binding in utrophin and dystrophin

  • N. Keep
  • Medicine, Biology
    Neurological Sciences
  • 2000
TLDR
Studies that elucidate and compare the actin-binding function of utrophin and dystrophin, particularly those initiated in the laboratory of Dr. John Kendrick-Jones at the MRC in Cambridge are reviewed.

A study of short utrophin isoforms in mice deficient for full-length utrophin

TLDR
The study of testis expression shows, for the first time, that full-length utrophin is expressed at high levels in Leydig cells, raising the possibility that this protein is involved in testosterone secretion.

Characterization of the β-Dystroglycan–Growth Factor Receptor 2 (Grb2) Interaction☆

TLDR
The data suggest a highly regulated and dynamic dystrophin/dystroglycan complex formation and that this complex is involved in cell signaling.

Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members.

TLDR
It is shown that interaction of caveolin-3 with beta-dystroglycan may competitively regulate the recruitment of dystrophin to the sarcolemma and the possible implications of the findings in the context of Duchenne muscular dystrophy.

Spectrin, alpha-actinin, and dystrophin.

Dp 71 , utrophin and β-dystroglycan expression and distribution in PC 12 / L 6 cell co-cultures

TLDR
This is the first work on the role of dystrophins as well as members of the DAP complex in a cell-line based co-culturing system, which may prove useful in determining protein associations in a more controlled environment than ex-vivo systems.

Dp 71 , utrophin and beta-dystroglycan expression and distribution in PC 12 / L 6 cell cocultures

TLDR
This is the first work on the role of dystrophins as well as members of the DAP complex in a cell-line based co-culturing system, which may prove useful in determining protein associations in a more controlled environment than ex-vivo systems.

References

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The WW Domain of Dystrophin Requires EF-Hands Region to Interact with β-Dystroglycan

TLDR
It is shown that the WW domain of dystrophin along with the EF-hand motifs binds to the carboxy-terminus of β-dystroglycan.

Characterization of the WW Domain of Human Yes-associated Protein and Its Polyproline-containing Ligands*

We had previously identified the WW domain as a novel globular domain that is composed of 38–40 semiconserved amino acids and is involved in mediating protein-protein interaction. The WW domain is

Isolation and characterization of different C-terminal fragments of dystrophin expressed in Escherichia coli.

TLDR
The results indicate that the two C-terminal fragments of dystrophin have differing biophysical properties, indicating that they may play distinct roles in the function of the protein.

Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide

TLDR
The structure of the WW domain differs from that of the SH3 domain and reveals a new design for a protein module that uses stacked aromatic surface residues to arrange a binding site for proline-rich peptides.

Identification and Characterization of the Dystrophin Anchoring Site on β-Dystroglycan (*)

TLDR
The identification of the interaction sites in dystrophin and β-dystroglycan provides further insight into the structure and the molecular organization of the dyStrophin-glycoprotein complex at the sarcolemma membrane and will be helpful for studying the pathogenesis of Duchenne muscular dystrophy.

Mammalian alpha 1- and beta 1-syntrophin bind to the alternative splice- prone region of the dystrophin COOH terminus

TLDR
A revised model of the domain organization of dystrophin from the view point of protein-protein interactions is proposed, which suggests that the function of syntrophin is tightly linked to the functional diversity among dyStrophin isoforms.

Ca-Calmodulin Binds to the Carboxyl-terminal Domain of Dystrophin (*)

TLDR
The unique COOH-terminal domain of dystrophin was expressed as a chimeric fusion protein (with the maltose-binding protein) and its binding to calmodulin was assessed, and it was found thatCalmodulin binding may modulate these interactions.

Dystrobrevin and dystrophin: an interaction through coiled-coil motifs.

Dystrobrevin, a dystrophin-related and -associated protein, has been proposed to be important in the formation and maintenance of the neuromuscular junction. Dystrobrevin coprecipitates with both the

Characterization of the Transmembrane Molecular Architecture of the Dystroglycan Complex in Schwann Cells*

TLDR
The results indicate 1) that Dp116 is a component of the submembranous cytoskeletal system that anchors the dystroglycan complex in Schwann cells, and 2) that this fragility may be attributable to the absence of the sarcoglycan complex.