Escobar-Henriques, Mafalda ORCID: 0000-0002-0879-3119 and Anton, Vincent ORCID: 0000-0003-3008-6346 (2020). Mitochondrial Surveillance by Cdc48/p97: MAD vs. Membrane Fusion. Int. J. Mol. Sci., 21 (18). BASEL: MDPI. ISSN 1422-0067

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Abstract

Cdc48/p97 is a ring-shaped, ATP-driven hexameric motor, essential for cellular viability. It specifically unfolds and extracts ubiquitylated proteins from membranes or protein complexes, mostly targeting them for proteolytic degradation by the proteasome. Cdc48/p97 is involved in a multitude of cellular processes, reaching from cell cycle regulation to signal transduction, also participating in growth or death decisions. The role of Cdc48/p97 in endoplasmic reticulum-associated degradation (ERAD), where it extracts proteins targeted for degradation from the ER membrane, has been extensively described. Here, we present the roles of Cdc48/p97 in mitochondrial regulation. We discuss mitochondrial quality control surveillance by Cdc48/p97 in mitochondrial-associated degradation (MAD), highlighting the potential pathologic significance thereof. Furthermore, we present the current knowledge of how Cdc48/p97 regulates mitofusin activity in outer membrane fusion and how this may impact on neurodegeneration.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Escobar-Henriques, MafaldaUNSPECIFIEDorcid.org/0000-0002-0879-3119UNSPECIFIED
Anton, VincentUNSPECIFIEDorcid.org/0000-0003-3008-6346UNSPECIFIED
URN: urn:nbn:de:hbz:38-320330
DOI: 10.3390/ijms21186841
Journal or Publication Title: Int. J. Mol. Sci.
Volume: 21
Number: 18
Date: 2020
Publisher: MDPI
Place of Publication: BASEL
ISSN: 1422-0067
Language: English
Faculty: Faculty of Mathematics and Natural Sciences
Divisions: Faculty of Mathematics and Natural Sciences > Department of Biology > Institute for Genetics
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
UBIQUITIN-PROTEASOME SYSTEM; AAA-ATPASE P97; QUALITY-CONTROL; VMS1 TRANSLOCATION; STRUCTURAL BASIS; GTP HYDROLYSIS; MITOFUSIN FZO1; VCP MUTATIONS; PROTEIN; ERMultiple languages
Biochemistry & Molecular Biology; Chemistry, MultidisciplinaryMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/32033

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