University of Massachusetts Medical School Faculty Publications

UMMS Affiliation

Department of Cell and Developmental Biology; Department of Biochemistry and Molecular Pharmacology

Date

4-15-2013

Document Type

Article

Medical Subject Headings

Chlamydomonas reinhardtii; Cilia; Endocytosis; Multiprotein Complexes; Phospholipase D; Signal Transduction

Disciplines

Cell Biology

Abstract

The BBSome is a complex of seven proteins, including BBS4, that is cycled through cilia by intraflagellar transport (IFT). Previous work has shown that the membrane-associated signaling protein phospholipase D (PLD) accumulates abnormally in cilia of Chlamydomonas reinhardtii bbs mutants. Here we show that PLD is a component of wild-type cilia but is enriched approximately 150-fold in bbs4 cilia; this accumulation occurs progressively over time and results in altered ciliary lipid composition. When wild-type BBSomes were introduced into bbs cells, PLD was rapidly removed from the mutant cilia, indicating the presence of an efficient BBSome-dependent mechanism for exporting ciliary PLD. This export requires retrograde IFT. Importantly, entry of PLD into cilia is BBSome and IFT independent. Therefore, the BBSome is required only for the export phase of a process that continuously cycles PLD through cilia. Another protein, carbonic anhydrase 6, is initially imported normally into bbs4 cilia but lost with time, suggesting that its loss is a secondary effect of BBSome deficiency.

Rights and Permissions

Citation: J Cell Biol. 2013 Apr 15;201(2):249-61. doi: 10.1083/jcb.201207139. Link to article on publisher's site

Comments

Publisher PDF posted as allowed by the publisher's author rights policy at http://www.rupress.org/site/subscriptions/terms.xhtml.

This article was selected for the Cover and for highlighting in the Journal of Cell Biology's "In This Issue" section.

Related Resources

Link to Article in PubMed

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