Luiza K. Sanjuán Szklarz

TL;DR: The binding of small Tim proteins to Mia40 is crucial for their transport across the outer membrane and represents an initial step in their assembly into IMS complexes.

TL;DR: It is concluded that Mdm10 plays a specific role in the biogenesis of the TOM complex, indicating a connection between the mitochondrial protein assembly apparatus and the machinery for maintenance of mitochondrial morphology.

TL;DR: The findings suggest that the heat shock protein Zim17 plays a specific role in preventing protein aggregation in the mitochondrial matrix, and that aggregation of Hsp70s causes pleiotropic effects on protein biogenesis and mitochondrial morphology.

TL;DR: It is demonstrated that Su e and Su g sequentially assemble with monomeric ATP synthase to form a dimerization-competent primed monomer, representing an initial step of oligomer formation.

TL;DR: It is reported that Bax promoted an efficient release of soluble IMS proteins while preproteins were still imported, excluding an unspecific damage of mitochondria, and activation of the known protein import and sorting machineries of the outer membrane does not impair the function of Bax at the mitochondria.