Cell Communication and SignalingCell BiologyPeer-reviewed journal article
Bardet-Biedl Syndrome 1 Mutations Differentially Impact BBSome Integrity and its Function in Ciliary Trafficking
Kristyna MaskovaiD, Hana HajsmanovaiD, Sofiia BykovaiD, Sindija SmiteiD, Avishek PrasaiiD, Daniel RozbeskýiD, Martina HuranováiD
Abstract
Bardet-Biedl Syndrome (BBS) is a pleiotropic ciliopathy marked by retinal degeneration, obesity, polydactyly, renal and reproductive anomalies, and cognitive impairment. BBS1, the most frequently mutated gene in BBS, encodes a key component of the BBSome complex, which is essential for ciliary membrane trafficking. Although BBS1 is known to be essential for proper BBSome function, the effects of disease-associated BBS1 variants on its activity remain incompletely understood. In this study, we examined how patient-derived BBS1 mutations affect BBSome integrity and its role in cargo transport within primary cilia. Our results show that particular BBS1 mutations interfere with distinct stages of BBSome assembly and trafficking. While M390R disrupts initial pre-BBSome assembly at pericentriolar satellites, E224K impairs both the maturation of the pre-BBSome into the BBSome and its movement from pericentriolar satellites to the cilium. In contrast, the R160Q variant preserves BBSome assembly and permits its localization to cilia. It specifically weakens the BBSome-GPCR interaction mediated by TOM1L2, resulting in defective GPR161 export and increased ciliary IFT turnover. Overall, our study establishes a mechanistic framework linking specific BBS1 mutations to distinct defects in BBSome assembly and function. This framework defines functional classes of BBS1 variants and provides deeper insight into the molecular mechanism and severity of Bardet-Biedl Syndrome.
- organism: human
- assay: proteomics
- research focus: cell signaling & trafficking
- approach: experimental assay
- Citations
- 0
- FWCI
- 0.00
- Field percentile
- 41th percentile
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- The BBSome assembly is spatially controlled by BBS1 and BBS4 in human cells
A. Prasai, M. Schmidt Cernohorska, … M. Huranova·bioRxiv·Mar 20, 2020
- De-suppression of mesenchymal cell identities and variable phenotypic outcomes associated with knockout of Bbs1.
Grace Freke, Tiago Martins, … Dagan Jenkins·CellsPeer-reviewed·Nov 20, 2023
- The Bardet-Biedl protein Bbs1 controls photoreceptor outer segment protein and lipid composition
Markus Masek, Christelle Etard, … Ruxandra Bachmann‐Gagescu·Nature CommunicationsPeer-reviewed·Mar 11, 2022
- Structure and activation mechanism of the BBSome membrane-protein trafficking complex
A. Brown, S. K. Singh, … M. C. Yip·eLifePeer-reviewed·Jan 15, 2020
- Depletion of BBSome Subunits Alters Receptor Endocytosis and Promotes EMT via TGF-β Signaling
Carlos Solarat, J. Barra-Carneiro, … Diana Valverde·bioRxiv·Oct 23, 2024
- Molecular Architecture of the Bardet-Biedl Syndrome 2-7-9 Subcomplex
W. G. Ludlam, T. Aoba, … B. M. Willardson·bioRxiv·Jul 11, 2019