Irp2 regulates insulin production through iron-mediated Cdkal1-catalyzed tRNA modification.

Santos, Maria C Ferreira Dos; Anderson, Cole P; Neschen, Susanne; Zumbrennen-Bullough, Kimberly B; Romney, Steven J; Kahle-Stephan, Melanie; Rathkolb, Birgit; Gailus-Durner, Valerie et al. · Nat Commun · 2020

basic_science · Level V

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Abstract

Regulation of cellular iron homeostasis is crucial as both iron excess and deficiency cause hematological and neurodegenerative diseases. Here we show that mice lacking iron-regulatory protein 2 (Irp2), a regulator of cellular iron homeostasis, develop diabetes. Irp2 post-transcriptionally regulates the iron-uptake protein transferrin receptor 1 (TfR1) and the iron-storage protein ferritin, and dysregulation of these proteins due to Irp2 loss causes functional iron deficiency in β cells. This impairs Fe-S cluster biosynthesis, reducing the function of Cdkal1, an Fe-S cluster enzyme that catalyzes methylthiolation of t<sup>6</sup>A37 in tRNA<sup>Lys</sup><sub>UUU</sub> to ms<sup>2</sup>t<sup>6</sup>A37. As a consequence, lysine codons in proinsulin are misread and proinsulin processing is impaired, reducing insulin content and secretion. Iron normalizes ms<sup>2</sup>t<sup>6</sup>A37 and proinsulin lysine incorporation, restoring insulin content and secretion in Irp2<sup>-/-</sup> β cells. These studies reveal a previously unidentified link between insulin processing and cellular iron deficiency that may have relevance to type 2 diabetes in humans.

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