Dual Role of Mitochondrial Porin in Metabolite Transport across the Outer Membrane and Protein Transfer to the Inner Membrane.
Antiporters
/ genetics
Carrier Proteins
/ genetics
Mitochondria
/ genetics
Mitochondrial Membrane Transport Proteins
/ genetics
Mitochondrial Membranes
/ metabolism
Mitochondrial Precursor Protein Import Complex Proteins
Mutation
Porins
/ genetics
Protein Binding
Protein Transport
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ genetics
membrane contact sites
metabolite carrier
mitochondria
protein sorting
protein translocation
Journal
Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571
Informations de publication
Date de publication:
07 03 2019
07 03 2019
Historique:
received:
17
06
2018
revised:
09
11
2018
accepted:
14
12
2018
pubmed:
11
2
2019
medline:
25
6
2019
entrez:
11
2
2019
Statut:
ppublish
Résumé
The mitochondrial inner membrane harbors a large number of metabolite carriers. The precursors of carrier proteins are synthesized in the cytosol and imported into mitochondria by the translocase of the outer membrane (TOM) and the carrier translocase of the inner membrane (TIM22). Molecular chaperones in the cytosol and intermembrane space bind to the hydrophobic precursors to prevent their aggregation. We report that the major metabolite channel of the outer membrane, termed porin or voltage-dependent anion channel (VDAC), promotes efficient import of carrier precursors. Porin interacts with carrier precursors arriving in the intermembrane space and recruits TIM22 complexes, thus ensuring an efficient transfer of the precursors to the inner membrane translocase. Porin channel mutants impaired in metabolite transport are not disturbed in carrier import into mitochondria. We conclude that porin serves distinct functions as outer membrane channel for metabolites and as coupling factor for protein translocation into the inner membrane.
Identifiants
pubmed: 30738704
pii: S1097-2765(18)31068-2
doi: 10.1016/j.molcel.2018.12.014
pii:
doi:
Substances chimiques
Antiporters
0
Carrier Proteins
0
Mitochondrial Membrane Transport Proteins
0
Mitochondrial Precursor Protein Import Complex Proteins
0
Por1 protein, S cerevisiae
0
Porins
0
Saccharomyces cerevisiae Proteins
0
TIM22 protein, S cerevisiae
0
TOM70 protein, S cerevisiae
0
Tim18 protein, S cerevisiae
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1056-1065.e7Informations de copyright
Copyright © 2018 Elsevier Inc. All rights reserved.