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ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria
Most mitochondrial proteins are synthesized in the cytosol and targeted to the mitochondrial surface in a post-translational manner. The surface of the endoplasmic reticulum (ER) plays an active role in this targeting reaction. ER-associated chaperones interact with certain mitochondrial membrane pr...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8432098/ https://www.ncbi.nlm.nih.gov/pubmed/34502567 http://dx.doi.org/10.3390/ijms22179655 |
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author | Koch, Christian Schuldiner, Maya Herrmann, Johannes M. |
author_facet | Koch, Christian Schuldiner, Maya Herrmann, Johannes M. |
author_sort | Koch, Christian |
collection | PubMed |
description | Most mitochondrial proteins are synthesized in the cytosol and targeted to the mitochondrial surface in a post-translational manner. The surface of the endoplasmic reticulum (ER) plays an active role in this targeting reaction. ER-associated chaperones interact with certain mitochondrial membrane protein precursors and transfer them onto receptor proteins of the mitochondrial surface in a process termed ER-SURF. ATP-driven proteins in the membranes of mitochondria (Msp1, ATAD1) and the ER (Spf1, P5A-ATPase) serve as extractors for the removal of mislocalized proteins. If the re-routing to mitochondria fails, precursors can be degraded by ER or mitochondria-associated degradation (ERAD or MAD respectively) in a proteasome-mediated reaction. This review summarizes the current knowledge about the cooperation of the ER and mitochondria in the targeting and quality control of mitochondrial precursor proteins. |
format | Online Article Text |
id | pubmed-8432098 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-84320982021-09-11 ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria Koch, Christian Schuldiner, Maya Herrmann, Johannes M. Int J Mol Sci Review Most mitochondrial proteins are synthesized in the cytosol and targeted to the mitochondrial surface in a post-translational manner. The surface of the endoplasmic reticulum (ER) plays an active role in this targeting reaction. ER-associated chaperones interact with certain mitochondrial membrane protein precursors and transfer them onto receptor proteins of the mitochondrial surface in a process termed ER-SURF. ATP-driven proteins in the membranes of mitochondria (Msp1, ATAD1) and the ER (Spf1, P5A-ATPase) serve as extractors for the removal of mislocalized proteins. If the re-routing to mitochondria fails, precursors can be degraded by ER or mitochondria-associated degradation (ERAD or MAD respectively) in a proteasome-mediated reaction. This review summarizes the current knowledge about the cooperation of the ER and mitochondria in the targeting and quality control of mitochondrial precursor proteins. MDPI 2021-09-06 /pmc/articles/PMC8432098/ /pubmed/34502567 http://dx.doi.org/10.3390/ijms22179655 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Koch, Christian Schuldiner, Maya Herrmann, Johannes M. ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria |
title | ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria |
title_full | ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria |
title_fullStr | ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria |
title_full_unstemmed | ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria |
title_short | ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria |
title_sort | er-surf: riding the endoplasmic reticulum surface to mitochondria |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8432098/ https://www.ncbi.nlm.nih.gov/pubmed/34502567 http://dx.doi.org/10.3390/ijms22179655 |
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