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TitleThe assembly of the Mitochondrial Complex I Assembly complex uncovers a redox pathway coordination.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 8248, Year 2023
Publish dateDec 12, 2023
AuthorsLindsay McGregor / Samira Acajjaoui / Ambroise Desfosses / Melissa Saïdi / Maria Bacia-Verloop / Jennifer J Schwarz / Pauline Juyoux / Jill von Velsen / Matthew W Bowler / Andrew A McCarthy / Eaazhisai Kandiah / Irina Gutsche / Montserrat Soler-Lopez /
PubMed AbstractThe Mitochondrial Complex I Assembly (MCIA) complex is essential for the biogenesis of respiratory Complex I (CI), the first enzyme in the respiratory chain, which has been linked to Alzheimer's ...The Mitochondrial Complex I Assembly (MCIA) complex is essential for the biogenesis of respiratory Complex I (CI), the first enzyme in the respiratory chain, which has been linked to Alzheimer's disease (AD) pathogenesis. However, how MCIA facilitates CI assembly, and how it is linked with AD pathogenesis, is poorly understood. Here we report the structural basis of the complex formation between the MCIA subunits ECSIT and ACAD9. ECSIT binding induces a major conformational change in the FAD-binding loop of ACAD9, releasing the FAD cofactor and converting ACAD9 from a fatty acid β-oxidation (FAO) enzyme to a CI assembly factor. We provide evidence that ECSIT phosphorylation downregulates its association with ACAD9 and is reduced in neuronal cells upon exposure to amyloid-β (Aβ) oligomers. These findings advance our understanding of the MCIA complex assembly and suggest a possible role for ECSIT in the reprogramming of bioenergetic pathways linked to Aβ toxicity, a hallmark of AD.
External linksNat Commun / PubMed:38086790 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 6.0 Å
Structure data

17659

8phe

EMDB-17659, PDB-8phe:
ACAD9-WT in complex with ECSIT-CTER
Method: EM (single particle) / Resolution: 3.1 Å

17660

8phf

EMDB-17660, PDB-8phf:
Cryo-EM structure of human ACAD9-S191A
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-17661: ACAD9 homodimer WT
Method: EM (single particle) / Resolution: 6.0 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Oxidative phosphorylation (OXPHOS) / Fatty Acid Oxidation (FAO) / Mitochondrial Complex I Assembly Complex (MCIA) / Amyloid-beta / ECSIT phosphorylation / FLAVOPROTEIN

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