Format

Send to

Choose Destination
Mol Cell. 2018 Aug 16;71(4):567-580.e4. doi: 10.1016/j.molcel.2018.06.039.

ACP Acylation Is an Acetyl-CoA-Dependent Modification Required for Electron Transport Chain Assembly.

Author information

1
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132, USA.
2
Department of Cell Biology, Harvard University School of Medicine, Boston, MA 02115, USA.
3
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132, USA; Department of Medicine, University of Utah School of Medicine, Salt Lake City, UT 84132, USA.
4
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132, USA; Howard Hughes Medical Institute, University of Utah School of Medicine, Salt Lake City, UT 84132, USA. Electronic address: rutter@biochem.utah.edu.

Abstract

The electron transport chain (ETC) is an important participant in cellular energy conversion, but its biogenesis presents the cell with numerous challenges. To address these complexities, the cell utilizes ETC assembly factors, which include the LYR protein family. Each member of this family interacts with the mitochondrial acyl carrier protein (ACP), the scaffold protein upon which the mitochondrial fatty acid synthesis (mtFAS) pathway builds fatty acyl chains from acetyl-CoA. We demonstrate that the acylated form of ACP is an acetyl-CoA-dependent allosteric activator of the LYR protein family used to stimulate ETC biogenesis. By tuning ETC assembly to the abundance of acetyl-CoA, which is the major fuel of the TCA cycle and ETC, this system could provide an elegant mechanism for coordinating the assembly of ETC complexes with one another and with substrate availability.

KEYWORDS:

acetyl-CoA; assembly factors; electron transport chain; mitochondria; mitochondrial fatty acid synthesis; respiration

PMID:
30118679
PMCID:
PMC6104058
DOI:
10.1016/j.molcel.2018.06.039
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center