Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Koch, Christian, Schuldiner, Maya, Herrmann, Johannes M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
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
_version_ 1783751085154893824
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
work_keys_str_mv AT kochchristian ersurfridingtheendoplasmicreticulumsurfacetomitochondria
AT schuldinermaya ersurfridingtheendoplasmicreticulumsurfacetomitochondria
AT herrmannjohannesm ersurfridingtheendoplasmicreticulumsurfacetomitochondria