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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 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.

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Metadaten
Author:Christian KochORCiD, Maya SchuldinerORCiD, Johannes M. Herrmann
URN (permanent link):urn:nbn:de:hbz:386-kluedo-66078
ISSN:1422-0067
Parent Title (English):International Journal of Molecular Sciences
Document Type:Review
Language of publication:English
Publication Date:2021/09/06
Year of Publication:2021
Publishing Institute:Technische Universität Kaiserslautern
Date of the Publication (Server):2021/10/06
Issue:2021, 22(17)
Number of page:13
Source:doi.org/10.3390/ijms22179655
Faculties / Organisational entities:Fachbereich Biologie
DDC-Cassification:5 Naturwissenschaften und Mathematik / 570 Biowissenschaften, Biologie
Collections:Open-Access-Publikationsfonds
Licence (German):Zweitveröffentlichung