Molecular Chaperones Hsp90 and Hsp70 Deliver Preproteins to the Mitochondrial Import Receptor Tom70

2003/01/01 by Jason C. Young, Nicholas J. Hoogenraad, F.Ulrich Hartl +1 · 6 citations
Biochemistry, Genetics and Molecular Biology · #Heat shock proteins research #ATP Synthase and ATPases Research #Mitochondrial Function and Pathology

paper · pdf · doi:10.1016/s0092-8674(02)01250-3

Abstract

The role of cytosolic factors in protein targeting to mitochondria is poorly understood. Here, we show that in mammals, the cytosolic chaperones Hsp90 and Hsp70 dock onto a specialized TPR domain in the import receptor Tom70 at the outer mitochondrial membrane. This interaction serves to deliver a set of preproteins to the receptor for subsequent membrane translocation dependent on the Hsp90 ATPase. Disruption of the chaperone/Tom70 recognition inhibits the import of these preproteins into mitochondria. In yeast, Hsp70 rather than Hsp90 is used in import, and Hsp70 docking is required for the formation of a productive preprotein/Tom70 complex. We outline a novel mechanism in which chaperones are recruited for a specific targeting event by a membrane-bound receptor.

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