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Parisima Ghaffarian Zavarzadeh1
Kathigna Panchal1
Dylan Bishop1
Elizabeth Gilbert1
Mahi Trivedi1
Tovaria Kee1
Srivastav Ranganathan2*
Anoop Arunagiri1*- 1Department of Biological Sciences, East Tennessee State University, Johnson City, TN, United States
- 2Max Planck Institute for the Physics of Complex Systems, Dresden, Germany
A Corrigendum on
Exploring proinsulin proteostasis: insights into beta cell health and diabetes
by Zavarzadeh PG, Panchal K, Bishop D, Gilbert E, Trivedi M, Kee T, Ranganathan S and Arunagiri A (2025). Front. Mol. Biosci. 12:1554717. doi: 10.3389/fmolb.2025.1554717
In the published article, there was an error in the legend for Figure 7 as published. A sentence was incomplete in the 7th point in the legend. The corrected legend appears below.
“Orchestrating proinsulin proteostasis in β-cells: Molecular Chaperones, oxidoreductases, and the UPR. (1) PERK ablation, leading to Erp72 upregulation, may impair proinsulin degradation or trafficking. Independently, PERK inhibition can induce ER stress in β-cells, (2) PERK inhibition (by PERKi) prevents eIF2α phosphorylation, negatively impacting the UPR primarily through dysregulation of protein synthesis, (3) Treatment of β-cells with PERKi for 10–12 h induces proinsulin misfolding, (4) BiP inactivation (by SubAB or PERK inhibition) impairs proinsulin folding in β-cells, (5) PDIA6 deletion may impair both the UPR and proinsulin trafficking; Defective proinsulin trafficking could hinder proinsulin folding in the ER, (6) Inhibition of the IRE1α-XBP1 pathway deregulates PDI activity in β-cells, potentially impeding proinsulin folding or disrupting ERAD through impaired PDI-mediated retrotranslocation, (7) Grp170 either directly targets mutant high-molecular weight (HMW) proinsulin aggregates or collaborates with reticulon 3 (RTN3), which engages with PGRMC1 on the ER luminal side (not shown), to clear aggregates via ER-phagy in the cytosol, (8) FBKBP2 knockout results in proinsulin misfolding, (9) High-glucose-induced sulfonylation of PRDX4 impairs its protective function against proinsulin misfolding, (10) Erdj3 may promote proinsulin folding by acting as a co-chaperone with BiP.”
The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.
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Keywords: proinsulin folding, trafficking, beta cells, proteostasis, insulin biosynthesis, diabetes
Citation: Zavarzadeh PG, Panchal K, Bishop D, Gilbert E, Trivedi M, Kee T, Ranganathan S and Arunagiri A (2025) Corrigendum: Exploring proinsulin proteostasis: insights into beta cell health and diabetes. Front. Mol. Biosci. 12:1592000. doi: 10.3389/fmolb.2025.1592000
Received: 11 March 2025; Accepted: 13 March 2025;
Published: 19 March 2025.
Edited and reviewed by:
Venkateswarlu Kanamarlapudi, Swansea University Medical School, United KingdomCopyright © 2025 Zavarzadeh, Panchal, Bishop, Gilbert, Trivedi, Kee, Ranganathan and Arunagiri. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Anoop Arunagiri, YXJ1bmFnaXJpQGV0c3UuZWR1; Srivastav Ranganathan, c3JhbmdhODhAcGtzLm1wZy5kZQ==