Journal
FEBS LETTERS
Volume 590, Issue 23, Pages 4147-4158Publisher
WILEY
DOI: 10.1002/1873-3468.12450
Keywords
carrier translocase; membrane protein; mitochondria; protein translocation; TIM22; TIM29
Funding
- Deutsche Forschungsgemeinschaft
- Cluster of Excellence
- DFG Research Center Nanoscale Microscopy
- Boehringer Ingelheim Foundation
- European Research Council [ERC335080]
- Max Planck Society
- National Science Centre (NCN) [2016/20/S/NZ1/00423]
- Polish Ministerial Ideas Plus Program [000263]
- Copernicus Award of the Foundation for Polish Science
- [SFB1190]
Ask authors/readers for more resources
Hydrophobic inner mitochondrial membrane proteins with internal targeting signals, such as the metabolite carriers, use the carrier translocase (TIM22 complex) for transport into the inner membrane. Defects in this transport pathway have been associated with neurodegenerative disorders. While the TIM22 complex is well studied in baker's yeast, very little is known about the mammalian TIM22 complex. Using immunoprecipitation, we purified the human carrier translocase and identified a mitochondrial inner membrane protein TIM29 as a novel component, specific to metazoa. We show that TIM29 is a constituent of the 440 kDa TIM22 complex and interacts with oxidized TIM22. Our analyses demonstrate that TIM29 is required for the structural integrity of the TIM22 complex and for import of substrate proteins by the carrier translocase.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available