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Basal body dysfunction is a likely cause of pleiotropic Bardet–Biedl syndrome
It is shown that BBS is probably caused by a defect at the basal body of ciliated cells, and a new BBS gene is cloned, BBS8, which encodes a protein with a prokaryotic domain, pilF, involved in pilus formation and twitching mobility.
Functional coordination of intraflagellar transport motors
Findings implicate BBS ciliary disease proteins and an OSM-3 kinesin activator in the formation of two IFT pathways that build functional cilia.
MKS and NPHP modules cooperate to establish basal body/transition zone membrane associations and ciliary gate function during ciliogenesis
Eight proteins, defects in which are associated with Meckel-Gruber syndrome and nephronophthisis ciliopathies, work together as two functional modules at the transition zone to establish basal
The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression
It is shown that BBS4 localizes to the centriolar satellites of centrosomes and basal bodies of primary cilia, where it functions as an adaptor of the p150glued subunit of the dynein transport machinery to recruit PCM1 (pericentriolar material 1 protein) and its associated cargo to the satellites.
Disruption of Bardet-Biedl syndrome ciliary proteins perturbs planar cell polarity in vertebrates
It is shown that mice with mutations in genes involved in Bardet-Biedl syndrome share phenotypes with PCP mutants including open eyelids, neural tube defects and disrupted cochlear stereociliary bundles, and that Vangl2 localizes to the basal body and axoneme of ciliated cells, suggesting that cilia are intrinsically involved in PCP processes.
The base of the cilium: roles for transition fibres and the transition zone in ciliary formation, maintenance and compartmentalization
Together with a recently described septin ring diffusion barrier at the ciliary base, the transition fibres and transition zone deserve attention for their varied roles in forming functional ciliary compartments.
Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport.
It is demonstrated that BBS-7 and Bbs-8 are required for the normal localization/motility of the IFT proteins OSM-5/Polaris andCHE-11, and to a notably lesser extent, CHE-2.
Genes and molecular pathways underpinning ciliopathies
Investigating ciliopathies has helped to understand the molecular mechanisms by which the cilium-associated basal body functions in early ciliogenesis, as well as how the transition zone functions in ciliary gating, and how intraflagellar transport enables cargo trafficking and signalling.
The centrosomal protein nephrocystin-6 is mutated in Joubert syndrome and activates transcription factor ATF4
These findings help establish the link between centrosome function, tissue architecture and transcriptional control in the pathogenesis of cystic kidney disease, retinal degeneration, and central nervous system development.