Figure 2. Model of the Dystrophin-Glycoprotein Complex.

Figure 2

Model of the Dystrophin-Glycoprotein Complex. Dystrophin is thought to physically couple the sarcolemma with the costameric cytoskeleton (see Fig. 3) through lateral association of its N-terminal and rod domains with cytoplasmic γ-actin filaments and through direct binding of its cysteine-rich domain to the β-subunit of the dystroglycan complex. Oligosaccharides present on α-dystroglycan are important for its binding to laminin-2 of the extracellular matrix. The sarcoglycan-sarcospan complex is thought to strengthen the noncovalent binding of dystrophin and α-dystroglycan with β-dystroglycan. α-Dystrobrevin appears to couple dystrophin with the sarcoglycan-sarcospan complex and also link the dystrophin-glycoprotein complex with the intermediate filament cytoskeleton (see Fig. 4). Two syntrophin molecules are anchored through homologous binding sites present in the C-terminal domains of dystrophin and α-dystrobrevin. Syntrophins are thought to serve as adaptor molecules that localize signaling molecules near the sarcolemma (see Fig. 4). Redrawn from.95

From: Structure and Function of the Dystrophin-Glycoprotein Complex

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