ArticleNature communications2020
Structural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex.
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 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- DHDDS-related juvenile parkinsonism is caused by impaired lipid metabolism, glycosylation, and mitochondrial dysfunction, which can be rescued by NADmedRxiv : the preprint server for health sciences · 2026Article
- Evolutionary divergence and functional insights into the heteromeric cis-prenyltransferase of Paramecium tetraurelia.The FEBS journal · 2026Article
- Case Report: Recurrent pathogenic mutation c.110G>A inFrontiers in neuroscience · 2026Article
- Structural mechanisms of allosteric regulation in the human cis-prenyltransferase complex.Nature communications · 2025Article
- Dhdds T206A and Dhdds K42E knock-in mouse models of retinitis pigmentosa 59 are phenotypically similar.Disease models & mechanisms · 2025Article
- Identifying and quantifying membrane interactions of the protein human cis-prenyltransferase.Protein science : a publication of the Protein Society · 2025Article
- Niemann-Pick C-like Endolysosomal Dysfunction in DHDDS Patient Cells, a Congenital Disorder of Glycosylation, Can Be Treated with Miglustat.International journal of molecular sciences · 2025Article
- Case Report:Frontiers in pediatrics · 2025Article
- Enhanced Immune Response Against Echinococcus Granulosus Through a CTLA-4/B7 Affinity-Based Vaccine.Vaccines · 2024Article
- Complexation and evolution of cis-prenyltransferase homologues in Cinnamomum kanehirae deduced from kinetic and functional characterizations.Protein science : a publication of the Protein Society · 2023Article
- A Dhdds K42E knock-in RP59 mouse model shows inner retina pathology and defective synaptic transmission.Cell death & disease · 2023Article
- Case report: Identification of a recurrent pathogenicFrontiers in genetics · 2023Article
- Perspectives on Retinal Dolichol Metabolism, and Visual Deficits in Dolichol Metabolism-Associated Inherited Disorders.Advances in experimental medicine and biology · 2023Review
- Vertebrate Animal Models of RP59: Current Status and Future Prospects.International journal of molecular sciences · 2022Review
- Structural basis for long-chain isoprenoid synthesis byScience advances · 2022Article
- De novo DHDDS variants cause a neurodevelopmental and neurodegenerative disorder with myoclonus.Brain : a journal of neurology · 2022Article
- Evidence that nuclear receptors are related to terpene synthases.Journal of molecular endocrinology · 2022Article
- Reconstitution of prenyltransferase activity on nanodiscs by components of the rubber synthesis machinery of the Para rubber tree and guayule.Scientific reports · 2022Article
- Adult-onset rapidly worsening progressive myoclonic epilepsy caused by a novel variant in DHDDS.Annals of clinical and translational neurology · 2021Article
- Lysosomal cholesterol accumulation contributes to the movement phenotypes associated with NUS1 haploinsufficiency.Genetics in medicine : official journal of the American College of Medical Genetics · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human cis-prenyltransferase (hcis-PT) is an enzymatic complex essential for protein N-glycosylation. Synthesizing the precursor of the glycosyl carrier dolichol-phosphate, mutations in hcis-PT cause severe human diseases. Here, we reveal that hcis-PT exhibits a heterotetrameric assembly in solution, consisting of two catalytic dehydrodolichyl diphosphate synthase (DHDDS) and inactive Nogo-B receptor (NgBR) heterodimers. Importantly, the 2.3 Å crystal structure reveals that the tetramer assembles via the DHDDS C-termini as a dimer-of-heterodimers. Moreover, the distal C-terminus of NgBR transverses across the interface with DHDDS, directly participating in active-site formation and the functional coupling between the subunits. Finally, we explored the functional consequences of disease mutations clustered around the active-site, and in combination with molecular dynamics simulations, we propose a mechanism for hcis-PT dysfunction in retinitis pigmentosa. Together, our structure of the hcis-PT complex unveils the dolichol synthesis mechanism and its perturbation in disease.
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