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Article

Molecular basis of proteolytic cleavage regulation by the extracellular matrix receptor dystroglycan.

Structure (London, England : 1993) - 7 Nov 2024

Anderson Michael J M, Hayward Amanda N, Smiley Adam T, Shi Ke, Pawlak Matthew R, Aird Eric J, Grant Eva, Greenberg Lauren, Aihara Hideki, Evans Robert L, Ulens Christopher, Gordon Wendy R

Abstract excerpt

The dystrophin-glycoprotein-complex (DGC), anchored by the transmembrane protein dystroglycan, functions to mechanically link the extracellular matrix and actin cytoskeleton. Breaking this connection is associated with diseases such as muscular dystrophy, yet cleavage of dystroglycan by matrix-metalloproteinases (MMPs) remains an understudied mechanism to disrupt the DGC. We determined the crystal structure of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 39305901
DOI: 10.1016/j.str.2024.08.019
PMCID: PMC11560575

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