FTSH10 is localized to the mitochondrial inner membrane, where it functions as part of a high-molecular-weight (2-MDa) complex with prohibitins (PHB) and FTSH3 . Its roles include:
Protein Quality Control: Degradation of misfolded or unassembled subunits of oxidative phosphorylation complexes (e.g., Complex I and V) .
Complex Assembly: Stabilization of mitochondrial Complex I and V during biogenesis .
Redundancy with FTSH3: In ftsh3 mutants, FTSH10 synthesis increases to compensate for the loss of FTSH3, though FTSH10 homo-oligomers cannot fully replace hetero-oligomeric FTSH3/FTSH10 complexes .
The FTSH10 antibody has been validated for detecting FTSH10 in mitochondrial extracts:
Specificity: Recognizes a single band at ~84–90 kDa in A. thaliana mitochondrial lysates .
Interaction Studies: Co-immunoprecipitation with FTSH3 confirms their association in hetero-oligomeric complexes .
Key Insight: FTSH10 and FTSH3 exhibit partial functional redundancy but distinct substrate specificities .
Mitochondrial Quality Control: FTSH10’s role in degrading unassembled subunits highlights its importance in preventing proteotoxic stress .
Complex I Regulation: While FTSH3 interacts with Complex I subunits (e.g., PSST), FTSH10 does not, suggesting distinct regulatory pathways .
Cross-Species Utility: Predicted reactivity in Gossypium and Brassica species may enable comparative studies in diverse plant models .