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MBC in Press, published online ahead of print May 24, 2006
Mol. Biol. Cell 10.1091/mbc.E06-03-0192

A more recent version of this article appeared on August 1, 2006
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Submitted on March 13, 2006
Revised on May 4, 2006
Accepted on May 11, 2006

ABC Transporters Are Required for Efficient RNAi in Caenorhabditis elegans

Prema Sundaram,* Benjamin Echalier,*{dagger} Wang Han, Dawn Hull,{ddagger} and Lisa Timmons

Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66045

Monitoring Editor: Marvin P. Wickens

RNA interference (RNAi) is a conserved gene-silencing phenomenon that can be triggered by delivery of double-stranded RNA (dsRNA) to cells and is a widely exploited technology in analyses of gene function. While a number of proteins that facilitate RNAi have been identified, current descriptions of RNAi and interrelated mechanisms are far from complete. Here we report that the Caenorhabditis elegans gene haf-6 is required for efficient RNAi. HAF-6 is a member of the ATP binding Cassette (ABC) transporter gene superfamily. ABC transporters utilize ATP to translocate small molecule substrates across the membranes in which they reside, often against a steep concentration gradient. Collectively, ABC transporters are involved in a variety of activities, including protective or barrier mechanisms that export drugs or toxins from cells (Broeks et al., 1996; Bauer et al., 1999; Begley, 2004; Fromm, 2004), in organellar biogenesis (Aubourg, 1994), and in mechanisms that protect against viral infection (Trowsdale et al., 1990; Abele and Tampe, 2004). HAF-6 is expressed predominantly in the intestine and germline and is localized to intracellular reticular organelles. We further demonstrate that nine additional ABC genes from diverse subfamilies are each required for efficient RNAi in C. elegans. Thus, the ability to mount a robust RNAi response to dsRNA depends upon the deployment of two ancient systems that respond to environmental assaults: RNAi mechanisms and membrane transport systems that utilize ABC proteins.

*These authors contributed equally to this work.

Present addresses: {dagger}Department of Plant Pathology, Kansas State University, Manhattan, KS 66506; {ddagger}Biomune Company, Lenexa, KS 66215.

Address correspondence to: Lisa Timmons (timmons{at}ku.edu)




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