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First published online 24 February 2009
doi: 10.1242/jcs.041764

Journal of Cell Science 122, 867-874 (2009)
Published by The Company of Biologists 2009
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Research Article

Identification of a palmitoyl acyltransferase required for protein sorting to the flagellar membrane

Brian T. Emmer1, Christina Souther1, Krista M. Toriello1, Cheryl L. Olson1, Conrad L. Epting2 and David M. Engman1,*

1 Departments of Pathology and Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA
2 Department of Pediatrics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA

* Author for correspondence (e-mail: d-engman{at}northwestern.edu)

Accepted 17 November 2008

Protein palmitoylation has diverse effects in regulating protein membrane affinity, localization, binding partner interactions, turnover and function. Here, we show that palmitoylation also contributes to the sorting of proteins to the eukaryotic flagellum. African trypanosomes are protozoan pathogens that express a family of unique Ca2+-binding proteins, the calflagins, which undergo N-terminal myristoylation and palmitoylation. The localization of calflagins depends on their acylation status. Myristoylation alone is sufficient for membrane association, but, in the absence of palmitoylation, the calflagins localize to the pellicular (cell body) membrane. Palmitoylation, which is mediated by a specific palmitoyl acyltransferase, is then required for subsequent trafficking of calflagin to the flagellar membrane. Coincident with the redistribution of calflagin from the pellicular to the flagellar membrane is their association with lipid rafts, which are highly enriched in the flagellar membrane. Screening of candidate palmitoyl acyltranferases identified a single enzyme, TbPAT7, that is necessary for calflagin palmitoylation and flagellar membrane targeting. Our results implicate protein palmitoylation in flagellar trafficking, and demonstrate the conservation and specificity of palmitoyl acyltransferase activity by DHHC-CRD proteins across kingdoms.

Key words: Flagellum, Palmitoylation, Membrane microdomains, Acylation, Trypanosoma


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