ArticleNature communications2020
Crystal structures of fukutin-related protein (FKRP), a ribitol-phosphate transferase related to muscular dystrophy.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Biosynthesis and Regulation of Laminin-Binding O-Mannosyl Glycans Related to Muscular Dystrophy.Advances in experimental medicine and biology · 2026Review
- Substrate flexibility of Mycoplasma fermentans mf1 phosphorylcholine transferase.Glycoconjugate journal · 2025Article
- Congenital muscular dystrophies and myopathies: the leading cause of genetic muscular disorders in eleven Chinese families.BMC musculoskeletal disorders · 2025Article
- Transition transferases prime bacterial capsule polymerization.Nature chemical biology · 2025Article
- Structural and Evolutionary Analysis of Proteins Endowed with a Nucleotidyltransferase, or Non-canonical Palm, Catalytic Domain.Journal of molecular evolution · 2024Article
- Article
- Molecular Study of the Fukutin-Related Protein (International journal of molecular sciences · 2024Article
- Deep Mutational Scanning in Disease-related Genes with Saturation Mutagenesis-Reinforced Functional Assays (SMuRF).bioRxiv : the preprint server for biology · 2024Article
- Article
- A multi-enzyme machine polymerizes the Haemophilus influenzae type b capsule.Nature chemical biology · 2023Article
- Misfolding of fukutin-related protein (FKRP) variants in congenital and limb girdle muscular dystrophies.Frontiers in molecular biosciences · 2023Article
- Dystroglycanopathy: From Elucidation of Molecular and Pathological Mechanisms to Development of Treatment Methods.International journal of molecular sciences · 2021Review
- Biosynthetic Mechanisms and Biological Significance of Glycerol Phosphate-Containing Glycan in Mammals.Molecules (Basel, Switzerland) · 2021Review
- Ribitol in Solution Is an Equilibrium of Asymmetric Conformations.Molecules (Basel, Switzerland) · 2021Article
- High degree of conservation of the enzymes synthesizing the laminin-binding glycoepitope of α-dystroglycan.Open biology · 2021Article
- A universal gene correction approach for FKRP-associated dystroglycanopathies to enable autologous cell therapy.Cell reports · 2021Article
- The structure of POMGNT2 provides new insights into the mechanism to determine the functional O-mannosylation site on α-dystroglycan.Genes to cells : devoted to molecular & cellular mechanisms · 2021Article
- FKRP-dependent glycosylation of fibronectin regulates muscle pathology in muscular dystrophy.Nature communications · 2021Article
- Fukutin-Related Protein: From Pathology to Treatments.Trends in cell biology · 2021Review
- Article
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Dystroglycan (α-DG) is a highly-glycosylated surface membrane protein. Defects in the O-mannosyl glycan of α-DG cause dystroglycanopathy, a group of congenital muscular dystrophies. The core M3 O-mannosyl glycan contains tandem ribitol-phosphate (RboP), a characteristic feature first found in mammals. Fukutin and fukutin-related protein (FKRP), whose mutated genes underlie dystroglycanopathy, sequentially transfer RboP from cytidine diphosphate-ribitol (CDP-Rbo) to form a tandem RboP unit in the core M3 glycan. Here, we report a series of crystal structures of FKRP with and without donor (CDP-Rbo) and/or acceptor [RboP-(phospho-)core M3 peptide] substrates. FKRP has N-terminal stem and C-terminal catalytic domains, and forms a tetramer both in crystal and in solution. In the acceptor complex, the phosphate group of RboP is recognized by the catalytic domain of one subunit, and a phosphate group on O-mannose is recognized by the stem domain of another subunit. Structure-based functional studies confirmed that the dimeric structure is essential for FKRP enzymatic activity.
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