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TitleStructure and assembly of the dystrophin glycoprotein complex.
Journal, issue, pagesNature, Vol. 637, Issue 8048, Page 1252-1260, Year 2025
Publish dateDec 11, 2024
AuthorsLi Wan / Xiaofei Ge / Qikui Xu / Gaoxingyu Huang / Tiandi Yang / Kevin P Campbell / Zhen Yan / Jianping Wu /
PubMed AbstractThe dystrophin glycoprotein complex (DGC) has a crucial role in maintaining cell membrane stability and integrity by connecting the intracellular cytoskeleton with the surrounding extracellular ...The dystrophin glycoprotein complex (DGC) has a crucial role in maintaining cell membrane stability and integrity by connecting the intracellular cytoskeleton with the surrounding extracellular matrix. Dysfunction of dystrophin and its associated proteins results in muscular dystrophy, a disorder characterized by progressive muscle weakness and degeneration. Despite the important roles of the DGC in physiology and pathology, its structural details remain largely unknown, hindering a comprehensive understanding of its assembly and function. Here we isolated the native DGC from mouse skeletal muscle and obtained its high-resolution structure. Our findings unveil a markedly divergent structure from the previous model of DGC assembly. Specifically, on the extracellular side, β-, γ- and δ-sarcoglycans co-fold to form a specialized, extracellular tower-like structure, which has a central role in complex assembly by providing binding sites for α-sarcoglycan and dystroglycan. In the transmembrane region, sarcoglycans and sarcospan flank and stabilize the single transmembrane helix of dystroglycan, rather than forming a subcomplex as previously proposed. On the intracellular side, sarcoglycans and dystroglycan engage in assembly with the dystrophin-dystrobrevin subcomplex through extensive interaction with the ZZ domain of dystrophin. Collectively, these findings enhance our understanding of the structural linkage across the cell membrane and provide a foundation for the molecular interpretation of many muscular dystrophy-related mutations.
External linksNature / PubMed:39663450
MethodsEM (single particle)
Resolution3.2 - 3.5 Å
Structure data

39568

8yt8

EMDB-39568, PDB-8yt8:
Cryo-EM structure of the dystrophin glycoprotein complex
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-39569: Cryo-EM structure of the dystrophin glycoprotein complex
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CLR:
CHOLESTEROL

ChemComp-ZN:
Unknown entry

ChemComp-P5S:
O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine

ChemComp-CA:
Unknown entry

Source
  • mus musculus (house mouse)
KeywordsSTRUCTURAL PROTEIN / complex membrane stability signaling

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