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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

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 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.

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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