MassIVE MSV000091946

Partial Public

Cardiolipin prolongs the lifetimes of respiratory proteins in Drosophila flight muscle

Description

To measure concurrently the lifetimes of proteins and lipids, we incubated fruit flies with stable isotope-labeled precursors (13C615N2-lysine or 13C6-glucose) and determined the relative abundance of heavy isotopomers in protein and lipid species by mass spectrometry. We restricted our analysis to a single, post-mitotic tissue, the indirect flight muscle, in order to measure lifetimes controlled by metabolic turnover but not tissue regeneration. Analysis of 680 protein and 45 lipid species, showed that the subunits of respiratory complexes I-V and the carriers for phosphate and ADP/ATP were among the longest-lived proteins in flight muscle (average half-life of 48+-16 days) while the molecular species of cardiolipin were the longest-lived lipids (average half-life of 27+-6 days). The remarkable longevity of these crista residents was not shared by all mitochondrial proteins, especially not by those residing in the matrix and the inner boundary membrane. Ablation of cardiolipin synthase, which causes replacement of cardiolipin by phosphatidylglycerol, and ablation of tafazzin, which causes partial replacement of cardiolipin by monolyso-cardiolipin, decreased the lifetimes of all subunits of the respiratory complexes. Ablation of tafazzin also decreased the lifetimes of the remaining cardiolipin species. These data suggest that an important function of cardiolipin in mitochondria is to protect respiratory complexes from degradation. [doi:10.25345/C5ZS2KP8R] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Insect, isotopic tracer, lipid-protein interaction, membrane biogenesis, mitochondrial respiratory chain complex

Contact

Principal Investigators:
(in alphabetical order)
Dr. Michael Schlame, New York University School of Medicine, USA
Dr. Thomas A. Neubert, New York University School of Medicine, USA
Submitting User: hbromage
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