Journal
JOURNAL OF CELL BIOLOGY
Volume 167, Issue 1, Pages 87-98Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200405100
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Funding
- NCI NIH HHS [P30 CA042014, 5P30 CA 42014] Funding Source: Medline
- NCRR NIH HHS [S10 RR019409-01] Funding Source: Medline
- NIGMS NIH HHS [GM 53466, R01 GM053466] Funding Source: Medline
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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 Gem 1 p (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 Gem 1 p 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 Gem 1 p function. Although overexpression of a mutant human Miro protein caused increased apoptotic activity in cultured cells (Fransson et al., 2003. J. Biol. Chem. 278:6,495-6502), Gem1p is not required for pheromone-induced yeast cell death. Thus, Gem I p defines a novel mitochondrial morphology pathway which may integrate cell signaling events with mitochondrial dynamics.
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