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Originally published as MBC in Press, 10.1091/mbc.E05-06-0590 on August 17, 2005

Vol. 16, Issue 11, 5094-5102, November 2005

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A Role for Jsn1p in Recruiting the Arp2/3 Complex to Mitochondria in Budding Yeast

Kammy L. Fehrenbacher, Istvan R. Boldogh, and Liza A. Pon

Department of Anatomy and Cell Biology, Columbia University, College of Physicians and Surgeons, New York, NY 10032

Submitted July 6, 2005; Accepted August 9, 2005
Monitoring Editor: Thomas Pollard

Although the Arp2/3 complex localizes to the leading edge of motile cells, endocytic structures, and mitochondria in budding yeast, the mechanism for targeting the Arp2/3 complex to different regions in the cell is not well understood. We find that Jsn1p, a member of the PUF family of proteins, facilitates association of Arp2/3 complex to yeast mitochondria. Jsn1p localizes to punctate structures that align along mitochondria, cofractionates with a mitochondrial marker protein during subcellular fractionation, and is both protease sensitive and carbonate extractable in isolated mitochondria. Thus, Jsn1p is a peripheral membrane protein that is associated with the outer leaflet of the mitochondrial outer membrane. Jsn1p colocalized and coimmunoprecipitated with mitochondria-associated Arc18p-GFP, and purified Arp2/3 complex bound to isolated TAP-tagged Jsn1p. Moreover, deletion of JSN1 reduces the amount of Arc18p-GFP that colocalizes and is recovered with mitochondria twofold, and jsn1{Delta} cells exhibited defects in mitochondrial morphology and motility similar to those observed in Arp2/3 complex mutants. Thus, Jsn1p has physical interactions with mitochondria-associated Arp2/3 complex and contributes to physical and functional association of the Arp2/3 complex with mitochondria.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05–06–0590) on August 17, 2005.

Abbreviations used: DAPI, 4',6-diamidino-2-phenylindole; GFP, green fluorescent protein; mtDNA, mitochondrial DNA.

Address correspondence to: Liza A. Pon (lap5{at}columbia.edu).




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