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Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function.
- Source :
-
Molecular cell [Mol Cell] 2016 Aug 18; Vol. 63 (4), pp. 621-632. Date of Electronic Publication: 2016 Aug 04. - Publication Year :
- 2016
-
Abstract
- Mitochondria are essential for numerous cellular processes, yet hundreds of their proteins lack robust functional annotation. To reveal functions for these proteins (termed MXPs), we assessed condition-specific protein-protein interactions for 50 select MXPs using affinity enrichment mass spectrometry. Our data connect MXPs to diverse mitochondrial processes, including multiple aspects of respiratory chain function. Building upon these observations, we validated C17orf89 as a complex I (CI) assembly factor. Disruption of C17orf89 markedly reduced CI activity, and its depletion is found in an unresolved case of CI deficiency. We likewise discovered that LYRM5 interacts with and deflavinates the electron-transferring flavoprotein that shuttles electrons to coenzyme Q (CoQ). Finally, we identified a dynamic human CoQ biosynthetic complex involving multiple MXPs whose topology we map using purified components. Collectively, our data lend mechanistic insight into respiratory chain-related activities and prioritize hundreds of additional interactions for further exploration of mitochondrial protein function.<br /> (Copyright © 2016 Elsevier Inc. All rights reserved.)
- Subjects :
- Databases, Protein
Electron Transport Chain Complex Proteins genetics
Electron Transport Complex I metabolism
HEK293 Cells
Hep G2 Cells
Humans
Mitochondrial Proteins genetics
RNA Interference
Signal Transduction
Transfection
Ubiquinone metabolism
Electron Transport Chain Complex Proteins metabolism
Mitochondria metabolism
Mitochondrial Proteins metabolism
Protein Interaction Mapping methods
Protein Interaction Maps
Proteomics methods
Subjects
Details
- Language :
- English
- ISSN :
- 1097-4164
- Volume :
- 63
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 27499296
- Full Text :
- https://doi.org/10.1016/j.molcel.2016.06.033