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Published 11 October 2004. doi:10.1083/jcb.200405100
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 1, 87-98
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Article

 Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway

Rebecca L. Frederick1,2, J. Michael McCaffery3, Kyle W. Cunningham4, Koji Okamoto1,2, and Janet M. Shaw1,2

1 Department of Biology, University of Utah, Salt Lake City, UT 84112
2 Department of Biochemistry, University of Utah, Salt Lake City, UT 84112
3 Integrated Imaging Center, Department of Biology
4 Department of Biology, Johns Hopkins University, Baltimore, MD 21218

Correspondence to Janet M. Shaw: shaw{at}bioscience.utah.edu; or Koji Okamoto: kokamoto{at}biology.utah.edu

Cell signaling events elicit changes in mitochondrial shape and activity. However, few mitochondrial proteins that interact with signaling pathways have been identified. Candidates include the conserved mitochondrial Rho (Miro) family of proteins, which contain two GTPase domains flanking a pair of calcium-binding EF-hand motifs. We show that Gem1p (yeast Miro; encoded by YAL048C) is a tail-anchored outer mitochondrial membrane protein. Cells lacking Gem1p contain collapsed, globular, or grape-like mitochondria. We demonstrate that Gem1p is not an essential component of characterized pathways that regulate mitochondrial dynamics. Genetic studies indicate both GTPase domains and EF-hand motifs, which are exposed to the cytoplasm, are required for Gem1p function. Although overexpression of a mutant human Miro protein caused increased apoptotic activity in cultured cells (Fransson et al., 2003. J. Biol. Chem. 278:6495–6502), Gem1p is not required for pheromone-induced yeast cell death. Thus, Gem1p defines a novel mitochondrial morphology pathway which may integrate cell signaling events with mitochondrial dynamics.

Abbreviations used in this paper: 3-PGK, protein 3-phosphoglycerate kinase; Miro, mitochondrial Rho; MITO, mitochondrial pellet; mito-GFP, mitochondrial-targeted GFP; PK, proteinase K; PMS, post-mitochondrial supernatant; TEM, transmission electron microscopy; WCE, whole cell extract.


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