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

@inproceedings{Rentschler1999TheWD,
  title={The WW Domain of Dystrophin Requires EF-Hands Region to Interact with $\beta$-Dystroglycan},
  author={Stacey L. Rentschler and Hillary Linn and Katrin Deininger and Mark T. Bedford and Xavier Espanel and Marius Sudol},
  booktitle={Biological chemistry},
  year={1999}
}
Abstract Skeletal muscle dystrophin is a 427 kDa protein thought to act as a link between the actin cytoskeleton and the extracellular matrix. Perturbations of the dystrophin-associated complex, for example, between dystrophin and the transmembrane glycoprotein β-dystroglycan, may lead to muscular dystrophy. Previously, the cysteine-rich region and first half of the carboxy-terminal domain of dystrophin were shown to interact with β-dystroglycan through a stretch of fifteen amino acids at the… 

Figures from this paper

Structure of a WW domain containing fragment of dystrophin in complex with β-dystroglycan

The crystal structure of the C-terminal region of dystrophin in complex with the proline-rich binding site in β-dystroglycan reveals striking similarities in the mechanisms of proline recognition employed by WW domains and SH3 domains.

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

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.

WW and EF hand domains of dystrophin-family proteins mediate dystroglycan binding.

This work has characterized interactions between dystrophin family members and dystroglycan: cytoskeletal and transmembrane components of the complex, respectively and demonstrates the first demonstration of a direct interaction between a dystrobrevin or utrophin and dyStrogly can.

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

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.

The conserved WW-domain binding sites in Dystroglycan C-terminus are essential but partially redundant for Dystroglycan function

It is proposed that the presence of the two WW binding sites in Dystroglycan secures the essential interaction between Dg and Dys and might further provide additional regulation for the cytoskeletal interactions of this complex.

A Putative Src Homology 3 Domain Binding Motif but Not the C-terminal Dystrophin WW Domain Binding Motif Is Required for Dystroglycan Function in Cellular Polarity in Drosophila*

In loss-of-function and overexpression studies more than half (34 residues) of the Dg proline-rich conserved C-terminal regions can be truncated without significantly compromising its function in regulating cellular polarity in Drosophila.
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