PF3D7_1119600

P. falciparum FtsH (PF3D7_1119600) is a zinc-dependent metalloprotease identified as a likely interaction partner of the stomatin-like protein (STOML) through affinity purification of epitope-tagged STOML, with the complex localizing to specific loci—branching points and endings—of the asexual blood-stage mitochondrial network (PMID:41662436). AlphaFold2 prediction indicates STOML structurally resembles bacterial HflK/C, which forms a vault-like assembly around FtsH hexamers, raising the possibility of an analogous STOML–FtsH complex in the parasite (PMID:41662436). Beyond this single association study, no further mechanistic detail—including protease substrates, ATPase activity, or the functional consequence of the interaction—has been characterized in the available corpus.

1. 2026 Medium

   To place a putative parasite FtsH metalloprotease into a functional context, this work asked what it interacts with and where it acts, establishing FtsH as a candidate partner of STOML at defined mitochondrial network loci.

   Evidence Pulldown/Co-IP of epitope-tagged STOML with mass spectrometry, AlphaFold2 structural prediction, and live imaging of epitope-tagged endogenous proteins in P. falciparum

   PMID:41662436

   Open questions at the time

   • No reciprocal Co-IP or in vitro reconstitution confirming a direct STOML–FtsH complex
   • No demonstration of FtsH protease or ATPase activity, nor identification of substrates
   • Functional requirement of FtsH for blood-stage development not tested (e.g. by knockdown/knockout)

• Whether the STOML–FtsH association is direct and vault-forming as in bacteria, and what FtsH proteolyzes to influence mitochondrial function, remain unresolved.
• Direct binding and stoichiometry of the proposed complex unproven
• No substrate or enzymatic characterization of PF3D7_1119600
• Physiological role in parasite mitochondrial biology undetermined