1. A BBSome Subunit Links Ciliogenesis, Microtubule Stability, and Acetylation
- Author
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John S. Beck, Diane C. Slusarski, J. Fernando Bazan, Val C. Sheffield, Charles Searby, Todd E. Scheetz, Maxence V. Nachury, Qihong Zhang, Peter K. Jackson, and Alexander V. Loktev
- Subjects
congenital, hereditary, and neonatal diseases and abnormalities ,Cytoplasm ,BBSome ,BBS1 ,Molecular Sequence Data ,Biology ,Histone Deacetylase 6 ,Microtubules ,Models, Biological ,General Biochemistry, Genetics and Molecular Biology ,Histone Deacetylases ,Cell Line ,Microtubule ,Ciliogenesis ,Animals ,Amino Acid Sequence ,Cilia ,Molecular Biology ,Ciliary membrane ,Cytoplasmic microtubule ,Bardet-Biedl Syndrome ,Zebrafish ,Sequence Homology, Amino Acid ,Cilium ,Gene Expression Regulation, Developmental ,Acetylation ,Cell Biology ,Zebrafish Proteins ,Cell biology ,Tubulin ,Gene Expression Regulation ,biology.protein ,CELLBIO ,Carrier Proteins ,Developmental Biology - Abstract
SummaryPrimary cilium dysfunction affects the development and homeostasis of many organs in Bardet-Biedl syndrome (BBS). We recently showed that seven highly conserved BBS proteins form a stable complex, the BBSome, that functions in membrane trafficking to and inside the primary cilium. We have now discovered a BBSome subunit that we named BBIP10. Similar to other BBSome subunits, BBIP10 localizes to the primary cilium, BBIP10 is present exclusively in ciliated organisms, and depletion of BBIP10 yields characteristic BBS phenotypes in zebrafish. Unexpectedly, BBIP10 is required for cytoplasmic microtubule polymerization and acetylation, two functions not shared with any other BBSome subunits. Strikingly, inhibition of the tubulin deacetylase HDAC6 restores microtubule acetylation in BBIP10-depleted cells, and BBIP10 physically interacts with HDAC6. BBSome-bound BBIP10 may therefore function to couple acetylation of axonemal microtubules and ciliary membrane growth.
- Published
- 2008
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