henhaobio
Sign in

Nature CommunicationsMolecular BiologyPeer-reviewed journal article

The Bardet-Biedl protein Bbs1 controls photoreceptor outer segment protein and lipid composition

Markus MasekiD, Christelle Etard, Claudia Hofmann, Andreas J. HülsmeieriD, Jingjing ZangiD, Masanari TakamiyaiD, Matthias GesemanniD, Stephan C. F. NeuhaussiD, Thorsten HornemanniD, Uwe SträhleiD, Ruxandra Bachmann‐GagescuiD

PDFDOIPreprint

Abstract

Primary cilia are key sensory organelles whose dysfunction leads to ciliopathy disorders such as Bardet-Biedl syndrome (BBS). Retinal degeneration is common in ciliopathies, since the outer segments (OSs) of photoreceptors are highly specialized primary cilia. BBS1, encoded by the most commonly mutated BBS-associated gene, is part of the BBSome protein complex. Using a new bbs1 zebrafish mutant, we show that retinal development and photoreceptor differentiation are unaffected by Bbs1-loss, supported by an initially unaffected transcriptome. Quantitative proteomics and lipidomics on isolated OSs show that Bbs1 is required for BBSome-entry into OSs and that Bbs1-loss leads to accumulation of membrane-associated proteins in OSs, with enrichment in proteins involved in lipid homeostasis. Disruption of the tightly regulated OS lipid composition with increased OS cholesterol content are paralleled by early functional visual deficits, which precede progressive OS morphological anomalies. Our findings identify a new role for Bbs1/BBSome in OS lipid homeostasis and suggest a new pathomechanism underlying retinal degeneration in BBS.

Citations
40
FWCI
5.43
Field percentile
top 3%

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.