Inner mitochondrial membrane protein Prohibitin 1 mediates Nix-induced, Parkin-independent mitophagy

Abstract Autophagy of damaged mitochondria, called mitophagy, is an important organelle quality control process involved in the pathogenesis of inflammation, cancer, aging, and age-associated diseases. Many of these disorders are associated with altered expression of the inner mitochondrial membrane...

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Main Authors: Kibrom M. Alula, Yaritza Delgado-Deida, Rosemary Callahan, Andreas Till, Lucia Underwood, Winston E. Thompson, Rhonda F. Souza, Themistocles Dassopoulos, Joseph Onyiah, K. Venuprasad, Arianne L. Theiss
Format: Article
Language:English
Published: Nature Portfolio 2023-01-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-022-26775-x
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author Kibrom M. Alula
Yaritza Delgado-Deida
Rosemary Callahan
Andreas Till
Lucia Underwood
Winston E. Thompson
Rhonda F. Souza
Themistocles Dassopoulos
Joseph Onyiah
K. Venuprasad
Arianne L. Theiss
author_facet Kibrom M. Alula
Yaritza Delgado-Deida
Rosemary Callahan
Andreas Till
Lucia Underwood
Winston E. Thompson
Rhonda F. Souza
Themistocles Dassopoulos
Joseph Onyiah
K. Venuprasad
Arianne L. Theiss
author_sort Kibrom M. Alula
collection DOAJ
description Abstract Autophagy of damaged mitochondria, called mitophagy, is an important organelle quality control process involved in the pathogenesis of inflammation, cancer, aging, and age-associated diseases. Many of these disorders are associated with altered expression of the inner mitochondrial membrane (IMM) protein Prohibitin 1. The mechanisms whereby dysfunction occurring internally at the IMM and matrix activate events at the outer mitochondrial membrane (OMM) to induce mitophagy are not fully elucidated. Using the gastrointestinal epithelium as a model system highly susceptible to autophagy inhibition, we reveal a specific role of Prohibitin-induced mitophagy in maintaining intestinal homeostasis. We demonstrate that Prohibitin 1 induces mitophagy in response to increased mitochondrial reactive oxygen species (ROS) through binding to mitophagy receptor Nix/Bnip3L and independently of Parkin. Prohibitin 1 is required for ROS-induced Nix localization to mitochondria and maintaining homeostasis of epithelial cells highly susceptible to mitochondrial dysfunction.
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spelling doaj.art-409c2db6f86d4000bd758ce74a53ab922023-01-08T12:11:05ZengNature PortfolioScientific Reports2045-23222023-01-0113111610.1038/s41598-022-26775-xInner mitochondrial membrane protein Prohibitin 1 mediates Nix-induced, Parkin-independent mitophagyKibrom M. Alula0Yaritza Delgado-Deida1Rosemary Callahan2Andreas Till3Lucia Underwood4Winston E. Thompson5Rhonda F. Souza6Themistocles Dassopoulos7Joseph Onyiah8K. Venuprasad9Arianne L. Theiss10Division of Gastroenterology and Hepatology, Department of Medicine, University of Colorado School of MedicineDivision of Gastroenterology and Hepatology, Department of Medicine, University of Colorado School of MedicineDivision of Gastroenterology and Hepatology, Department of Medicine, University of Colorado School of MedicineDepartment of Internal Medicine, University Hospital BonnDivision of Gastroenterology and Hepatology, Department of Medicine, University of Colorado School of MedicineDepartment of Obstetrics and Gynecology, Morehouse School of MedicineCenter for Esophageal Diseases, Baylor University Medical Center and Center for Esophageal Research, Baylor Scott & White Research InstituteCenter for Esophageal Diseases, Baylor University Medical Center and Center for Esophageal Research, Baylor Scott & White Research InstituteDivision of Gastroenterology and Hepatology, Department of Medicine, University of Colorado School of MedicineCollege of Medicine, University of Texas Southwestern Medical CenterDivision of Gastroenterology and Hepatology, Department of Medicine, University of Colorado School of MedicineAbstract Autophagy of damaged mitochondria, called mitophagy, is an important organelle quality control process involved in the pathogenesis of inflammation, cancer, aging, and age-associated diseases. Many of these disorders are associated with altered expression of the inner mitochondrial membrane (IMM) protein Prohibitin 1. The mechanisms whereby dysfunction occurring internally at the IMM and matrix activate events at the outer mitochondrial membrane (OMM) to induce mitophagy are not fully elucidated. Using the gastrointestinal epithelium as a model system highly susceptible to autophagy inhibition, we reveal a specific role of Prohibitin-induced mitophagy in maintaining intestinal homeostasis. We demonstrate that Prohibitin 1 induces mitophagy in response to increased mitochondrial reactive oxygen species (ROS) through binding to mitophagy receptor Nix/Bnip3L and independently of Parkin. Prohibitin 1 is required for ROS-induced Nix localization to mitochondria and maintaining homeostasis of epithelial cells highly susceptible to mitochondrial dysfunction.https://doi.org/10.1038/s41598-022-26775-x
spellingShingle Kibrom M. Alula
Yaritza Delgado-Deida
Rosemary Callahan
Andreas Till
Lucia Underwood
Winston E. Thompson
Rhonda F. Souza
Themistocles Dassopoulos
Joseph Onyiah
K. Venuprasad
Arianne L. Theiss
Inner mitochondrial membrane protein Prohibitin 1 mediates Nix-induced, Parkin-independent mitophagy
Scientific Reports
title Inner mitochondrial membrane protein Prohibitin 1 mediates Nix-induced, Parkin-independent mitophagy
title_full Inner mitochondrial membrane protein Prohibitin 1 mediates Nix-induced, Parkin-independent mitophagy
title_fullStr Inner mitochondrial membrane protein Prohibitin 1 mediates Nix-induced, Parkin-independent mitophagy
title_full_unstemmed Inner mitochondrial membrane protein Prohibitin 1 mediates Nix-induced, Parkin-independent mitophagy
title_short Inner mitochondrial membrane protein Prohibitin 1 mediates Nix-induced, Parkin-independent mitophagy
title_sort inner mitochondrial membrane protein prohibitin 1 mediates nix induced parkin independent mitophagy
url https://doi.org/10.1038/s41598-022-26775-x
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