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Published 5 June 2006. doi:10.1083/jcb.200603092
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 5, 651-658
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Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p



Hiromi Sesaki1, Cory D. Dunn1, Miho Iijima1, Kelly A. Shepard2, Michael P. Yaffe2, Carolyn E. Machamer1, and Robert E. Jensen1

1 Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205
2 Division of Biology, Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093

Correspondence to Address correspondence to Hiromi Sesaki: hsesaki{at}jhmi.edu

Mgm1p is a conserved dynamin-related GTPase required for fusion, morphology, inheritance, and the genome maintenance of mitochondria in Saccharomyces cerevisiae. Mgm1p undergoes unconventional processing to produce two functional isoforms by alternative topogenesis. Alternative topogenesis involves bifurcate sorting in the inner membrane and intramembrane proteolysis by the rhomboid protease Pcp1p. Here, we identify Ups1p, a novel mitochondrial protein required for the unique processing of Mgm1p and for normal mitochondrial shape. Our results demonstrate that Ups1p regulates the sorting of Mgm1p in the inner membrane. Consistent with its function, Ups1p is peripherally associated with the inner membrane in the intermembrane space. Moreover, the human homologue of Ups1p, PRELI, can fully replace Ups1p in yeast cells. Together, our findings provide a conserved mechanism for the alternative topogenesis of Mgm1p and control of mitochondrial morphology.

H. Sesaki's present address is Department of Cell Biology, Division of Biomedical Sciences, Johns Hopkins Singapore, 31 Biopolis Way, #02-01 The Nanos, Singapore 138669.

K.A. Shepard's present address is Parallel Synthesis Technologies, Inc., 3054 Lawrence Expressway, Santa Clara, CA 95051.

Abbreviations used in this paper: IM, inner membrane; IMS, intermembrane space; mtDNA, mitochondrial DNA; OM, outer membrane; WT, wild type.


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