Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Insulin-Degrading Enzyme Targeted to Mitochondria: A Proteomic Study

Version 1 : Received: 25 April 2023 / Approved: 26 April 2023 / Online: 26 April 2023 (07:40:36 CEST)

A peer-reviewed article of this Preprint also exists.

Yilmaz, A.; Guerrera, C.; Waeckel-Énée, E.; Lipecka, J.; Bertocci, B.; van Endert, P. Insulin-Degrading Enzyme Interacts with Mitochondrial Ribosomes and Respiratory Chain Proteins. Biomolecules 2023, 13, 890. Yilmaz, A.; Guerrera, C.; Waeckel-Énée, E.; Lipecka, J.; Bertocci, B.; van Endert, P. Insulin-Degrading Enzyme Interacts with Mitochondrial Ribosomes and Respiratory Chain Proteins. Biomolecules 2023, 13, 890.

Abstract

Insulin-degrading enzyme (IDE) is a highly conserved metalloprotease mainly localized in the cytosol. Although IDE can degrade insulin and some other low molecular weight substrates efficiently, its ubiquitous expression suggests additional functions supported by experimental findings, such as a role in stress responses, cellular protein homeostasis. Translation of full-length (Met1) IDE transcripts has reported to result in targeting to mitochondria but the role of IDE in this compartment is unknown. To obtain initial leads on the function of IDE in mitochondria, here we used a proximity biotinylation approach to identify proteins interacting with wild-type and protease-dead IDE targeted to the mitochondrial matrix. We find that mitochondrial IDE interacts strongly with mitochondrial ribosomes as well as with proteins of the respiratory chain. The mitochondrial interactomes of wild type and mutant IDE are highly similar and do not reveal any proteolytic IDE substrates. We speculate that IDE could adopt similar functions in mitochondria as in the cytosol, acting as a chaperone and contributing to protein homeostasis and stress responses.

Keywords

Mitochondrion; respiratory chain; mitochondrial translation; chaperone

Subject

Biology and Life Sciences, Cell and Developmental Biology

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