ArticleeLife2020
Structure of the human BBSome core complex.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 82 citations in OpenAlex.
- Primary cilia: master conductors of cellular communication in development and disease.Nature reviews. Nephrology · 2026Review
- BBS5 as a robust prognostic biomarker in esophageal squamous cell carcinoma: validation in two independent cohorts.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026Article
- Structural insights into predicted protein-protein interactions and protein complexes in the human proteome.Scientific reports · 2026Article
- BBSome: An essential component of hypothalamic regulation of energy homeostasis.Reviews in endocrine & metabolic disorders · 2026Review
- Phosphoproteomic profiling highlights CDC42 and CDK2 as key players in the regulation of the TGF-β pathway in ALMS1 and BBS1 knockout models.Scientific reports · 2025Article
- Homology search confirms widespread presence of BBSome proteins in Hexapoda with implications for potential non-ciliary BBS protein functions in honey bees.Scientific reports · 2025Article
- Methods to Assess Neuronal Primary Cilia Electrochemical Signaling.Journal of cellular physiology · 2025Article
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- BBSome deficiency in Lotmaria passim reveals divergent functions in trypanosomatid parasites.Parasites & vectors · 2025Article
- Ccrk-Mak/Ick signaling is a ciliary transport regulator essential for retinal photoreceptor survival.Life science alliance · 2024Article
- Whole Genome Sequencing Solves an Atypical Form of Bardet-Biedl Syndrome: Identification of Novel Pathogenic Variants ofInternational journal of molecular sciences · 2024Article
- Parkinsonism Sac domain mutation in Synaptojanin-1 affects ciliary properties in iPSC-derived dopaminergic neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Transport and barrier mechanisms that regulate ciliary compartmentalization and ciliopathies.Nature reviews. Nephrology · 2024Review
- Deciphering vesicle-assisted transport mechanisms in cytoplasm to cilium trafficking.Frontiers in cellular neuroscience · 2024Review
- Sequence variants in different genes underlying Bardet-Biedl syndrome in four consanguineous families.Molecular biology reports · 2023Article
- Parkinsonism Sac domain mutation in Synaptojanin-1 affects ciliary properties in iPSC-derived dopaminergic neurons.bioRxiv : the preprint server for biology · 2023Article
- Changes in expression of mesothelial BBS genes in 2D and 3D after lithium chloride and ammonium sulphate induction of primary cilium disturbance: a pilot study.Pharmacological reports : PR · 2023Article
- Organization, functions, and mechanisms of the BBSome in development, ciliopathies, and beyond.eLife · 2023Review
- Primary cilia as dynamic and diverse signalling hubs in development and disease.Nature reviews. Genetics · 2023Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The BBSome is a heterooctameric protein complex that plays a central role in primary cilia homeostasis. Its malfunction causes the severe ciliopathy Bardet-Biedl syndrome (BBS). The complex acts as a cargo adapter that recognizes signaling proteins such as GPCRs and links them to the intraflagellar transport machinery. The underlying mechanism is poorly understood. Here we present a high-resolution cryo-EM structure of a human heterohexameric core subcomplex of the BBSome. The structure reveals the architecture of the complex in atomic detail. It explains how the subunits interact with each other and how disease-causing mutations hamper this interaction. The complex adopts a conformation that is open for binding to membrane-associated GTPase Arl6 and a large positively charged patch likely strengthens the interaction with the membrane. A prominent negatively charged cleft at the center of the complex is likely involved in binding of positively charged signaling sequences of cargo proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.