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Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70.

Cell | Jan 10, 2003

http://www.ncbi.nlm.nih.gov/pubmed/12526792

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.

Pubmed ID: 12526792 RIS Download

Mesh terms: Adenosine Triphosphatases | Amino Acid Substitution | Animals | Biological Transport, Active | COS Cells | Cytosol | Fungal Proteins | HSP70 Heat-Shock Proteins | HSP90 Heat-Shock Proteins | Humans | Membrane Proteins | Mitochondria | Mitochondrial Membrane Transport Proteins | Models, Biological | Protein Binding | Protein Precursors | Rats | Receptors, Cell Surface | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins

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