OMA1 clears traffic jam in TOM tunnel in mammals-Reference-Cited by-同舟云学术

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OMA1 clears traffic jam in TOM tunnel in mammals

Published:2024-04-15 Issue:5 Volume:223 Page:
ISSN:0021-9525
Container-title:Journal of Cell Biology
language:en
Short-container-title:

Author:

Sekine Shiori¹²^ORCID,Sekine Yusuke¹³^ORCID

Affiliation:

1. University of Pittsburgh 1 Aging Institute, , Pittsburgh, PA, USA

2. University of Pittsburgh 2 Department of Cell Biology, School of Medicine, , Pittsburgh, PA, USA

3. University of Pittsburgh 3 Department of Medicine, Division of Endocrinology and Metabolism, School of Medicine, , Pittsburgh, PA, USA

Abstract

Using an engineered mitochondrial clogger, Krakowczyk et al. (https://doi.org/10.1083/jcb.202306051) identified the OMA1 protease as a critical component that eliminates import failure at the TOM translocase in mammalian cells, providing a novel quality control mechanism that is distinct from those described in yeast.

Funder

University of Pittsburgh

National Institutes of Health

National Institute of Diabetes and Digestive and Kidney Diseases

Publisher

Rockefeller University Press

Link

https://rupress.org/jcb/article-pdf/doi/10.1083/jcb.202403190/1927275/jcb_202403190.pdf

Reference10 articles.

1. The role of the proteasome in mitochondrial protein quality control

2. OMA1 protease eliminates arrested protein import intermediates upon mitochondrial depolarization

3. Mitochondrial protein translocation-associated degradation

4. MitoCPR—A surveillance pathway that protects mitochondria in response to protein import stress

5. Mitochondrial complexome reveals quality-control pathways of protein import

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