Allosteric Modulation of Drp1 Mechanoenzyme Assembly and Mitochondrial Fission by the Variable Domain

[摘要]：Background: Mechanisms of Drp1-mediated mitochondrial fission are poorly understood. Results: Substitution of the Drp1 variable domain causes a spectrum of assembly and activity phenotypes but does not compromise the stalk domain-mediated recruitment of Drp1 to the mitochondrial anchoring protein Mff. Conclusion: The variable domain modulates Drp1 activity through oligomeric assembly. Significance: Insight into Drp1 regulatory mechanisms is essential for understanding mitochondrial biology.

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