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UGO1  -  Ugo1p

Saccharomyces cerevisiae S288c

Synonyms: Mitochondrial fusion and transport protein UGO1, YDR470C
 
 
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High impact information on UGO1

  • Mitochondrial fusion requires two integral outer membrane components, Fzo1p and Ugo1p [1].
  • Taken together, these data suggest a model where Mgm1p functions in fusion to remodel the inner membrane and to connect the inner membrane to the outer membrane via its interactions with Ugo1p and Fzo1p, thereby helping to coordinate the behavior of the four mitochondrial membranes during fusion [1].
  • Fragmentation of mitochondria and loss of mtDNA in ugo1 mutants are rescued by disrupting DNM1, a gene required for mitochondrial division [2].
  • In zygotes formed by mating two ugo1 cells, mitochondria do not fuse and mix their matrix contents [2].
  • Ugo1p appears to contain a single transmembrane segment, with its NH(2) terminus facing the cytosol and its COOH terminus in the intermembrane space [2].
 

Anatomical context of UGO1

  • Like fzo1 and ugo1 mutants, cells disrupted for the MGM1 gene contain numerous mitochondrial fragments instead of the few long, tubular organelles seen in wild-type cells [3].
 

Physical interactions of UGO1

  • Here, we show that the cytoplasmic domain of Ugo1p directly interacts with Fzo1p, whereas its intermembrane space domain binds to Mgm1p [4].
 

Other interactions of UGO1

References

  1. The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion. Wong, E.D., Wagner, J.A., Scott, S.V., Okreglak, V., Holewinske, T.J., Cassidy-Stone, A., Nunnari, J. J. Cell Biol. (2003) [Pubmed]
  2. UGO1 encodes an outer membrane protein required for mitochondrial fusion. Sesaki, H., Jensen, R.E. J. Cell Biol. (2001) [Pubmed]
  3. Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane. Sesaki, H., Southard, S.M., Yaffe, M.P., Jensen, R.E. Mol. Biol. Cell (2003) [Pubmed]
  4. Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion. Sesaki, H., Jensen, R.E. J. Biol. Chem. (2004) [Pubmed]
 
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