The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function
Open accessAbstract
SUMMARY Mitochondria are essential for numerous cellular processes, yet hundreds of their proteins lack robust functional annotation. To reveal new 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 new mechanistic insight into respiratory chain-related activities and prioritize hundreds of additional interactions for further exploration of mitochondrial protein function.
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Cites
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The BioPlex network: a systematic exploration of the human interactome
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“Hosp et al., 2015; Huttlin et al., 2015; Keilhauer et al., 2015) have improved the ability to accurately detect PPIs, enabling researchers to overcome the systematic bias against poorly characterized proteins inherent in many large-scale ‘‘interactome’’ analyses (Sahni et al., 2015).”
A Human Interactome in Three Quantitative Dimensions Organized by Stoichiometries and Abundances
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Widespread macromolecular interaction perturbations in human genetic disorders
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Cited by
Architecture of the human interactome defines protein communities and disease networks
Huttlin, E. L., Bruckner, R. J., Paulo, J. A., Cannon, J. R., Ting, L., Baltier, K., Colby, G., Gebreab, F., Gygi, M. P., Parzen, H., et al. (2017) · Nature · doi:10.1038/nature22366 · Cited by 1,437
Mitochondrial proteins: from biogenesis to functional networks
Pfanner, N., Warscheid, B., & Wiedemann, N. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0092-0 · Cited by 1,028
Wang, T., Yu, H., Hughes, N. W., Liu, B., Kendirli, A., Klein, K., Chen, W. W., Lander, E. S., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.01.013 · Cited by 632
The genetics and pathology of mitochondrial disease
Alston, C. L., Rocha, M. C., Lax, N. Z., Turnbull, D. M., & Taylor, R. W. (2017) · The Journal of Pathology · doi:10.1002/path.4809 · Cited by 451
Self-citationBiochemistry of Mitochondrial Coenzyme Q Biosynthesis
Stefely, J. A., & Pagliarini, D. J. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.06.008 · Cited by 331
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Metadata
- Authors
- Floyd, B. J., Wilkerson, E. M., Veling, M. T., Minogue, C. E., Xia, C., Beebe, E. T., Wrobel, R. L., Cho, H., Kremer, L. S., Alston, C. L., Gromek, K. A., Dolan, B. K., Ulbrich, A., Stefely, J. A., Bohl, S. L., Werner, K. M., Jochem, A., Westphall, M. S., Rensvold, J. W., Taylor, R. W., Prokisch, H., Kim, J.-J. P., Coon, J. J., & Pagliarini, D. J.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2016-08
- Volume
- 63
- Issue
- 4
- Pages
- 621-632
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2492521149
- Cited by
- 264
- References
- 9
- FWCI
- 15.35
- Type
- journal article
- Language
- en
- Open access
- bronze
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