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The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly
- Source :
- The Journal of Cell Biology
- Publication Year :
- 2005
- Publisher :
- Rockefeller University Press, 2005.
-
Abstract
- Mitochondrial division requires coordinated interactions among Fis1p, Mdv1p, and the Dnm1p GTPase, which assemble into fission complexes on the outer mitochondrial membrane. The integral outer membrane protein Fis1p contains a cytoplasmic domain consisting of a tetratricopeptide repeat (TPR)–like fold and a short NH2-terminal helix. Although it is known that the cytoplasmic domain is necessary for assembly of Mdv1p and Dnm1p into fission complexes, the molecular details of this assembly are not clear. In this study, we provide new evidence that the Fis1p–Mdv1p interaction is direct. Furthermore, we show that conditional mutations in the Fis1p TPR-like domain cause fission complex assembly defects that are suppressed by mutations in the Mdv1p-predicted coiled coil. We also define separable functions for the Fis1p NH2-terminal arm and TPR-like fold. These studies suggest that the concave binding surface of the Fis1p TPR-like fold interacts with Mdv1p during mitochondrial fission and that Mdv1p facilitates Dnm1p recruitment into functional fission complexes.
- Subjects :
- Saccharomyces cerevisiae Proteins
Protein Conformation
Fission
Saccharomyces cerevisiae
Mitochondrion
Biology
Article
GTP Phosphohydrolases
Mitochondrial Proteins
03 medical and health sciences
0302 clinical medicine
Research Articles
Adaptor Proteins, Signal Transducing
030304 developmental biology
Coiled coil
0303 health sciences
Temperature
Cell Biology
Mitochondrial carrier
Molecular biology
Mitochondria
Protein Structure, Tertiary
Tetratricopeptide
Mutation
Translocase of the inner membrane
Biophysics
Mitochondrial fission
Carrier Proteins
Bacterial outer membrane
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 15408140 and 00219525
- Volume :
- 171
- Database :
- OpenAIRE
- Journal :
- Journal of Cell Biology
- Accession number :
- edsair.doi.dedup.....c0794ab467bb6d4dc3bd7060e11aec64
- Full Text :
- https://doi.org/10.1083/jcb.200506158