Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

PMID:14520415

Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome.

All C. elegans BBS homologs are expressed exclusively in ciliated sensory neurons

"all available Caenorhabditis elegans BBS homologues are expressed exclusively in ciliated neurons"
BBS genes contain RFX regulatory elements associated with ciliogenesis

"contain regulatory elements for RFX, a transcription factor that modulates the expression of genes associated with ciliogenesis and intraflagellar transport"
Basal body dysfunction is the likely cause of BBS phenotypes

"BBS is probably caused by a defect at the basal body of ciliated cells"

PMID:15231740

Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport.

BBS proteins localize predominantly at the base of cilia

"C. elegans BBS proteins localize predominantly at the base of cilia"
BBS proteins move bidirectionally along the ciliary axoneme like IFT proteins

"like proteins involved in intraflagellar transport (IFT), a process necessary for cilia biogenesis and maintenance, move bidirectionally along the ciliary axoneme"
BBS-7 and BBS-8 are required for normal IFT protein localization and motility

"BBS-7 and BBS-8 are required for the normal localization/motility of the IFT proteins OSM-5/Polaris and CHE-11"
Loss of BBS function causes structural and functional cilia defects

"mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia"

PMID:22922713

The BBSome controls IFT assembly and turnaround in cilia.

The BBSome assembles IFT complexes at the ciliary base

"the BBSome (refs 3, 4), a group of conserved proteins affected in human Bardet-Biedl syndrome(5) (BBS), assembles IFT complexes at the ciliary base"
The BBSome binds to IFT particles as cargo, not as a structural component

"After IFT particles are assembled at the ciliary base, the BBSome binds to the IFT particle like a cargo but not a structural component"
BBSome is required for IFT particle reassembly and turnaround at ciliary tip

"the BBSome is required for assembling IFT particles at both ciliary base and tip"
BBS-2 shows ciliary localization and IFT movement

"the others (BBS-2, -5, -7, -8, -9) only showed very dim ciliary staining when compared to wild-type animals"
BiFC assays confirm BBS proteins form a complex in C. elegans

"In wild-type animals, fluorescence complementation can be observed in BBS-1–BBS-7 and BBS-1–BBS-9 pair, indicative of the coexistence of these three BBS proteins in the same complex"
Loss of BBSome-IFT coupling leads to IFT-B accumulation at ciliary tips

"The absence of the BBSome at the cilia tip leads to the defective recycling of IFT complex"

file:worm/bbs-2/bbs-2-deep-research-falcon.md

Deep research report on bbs-2