ArticleMolecular biology of the cell2010
Roles of the Mdm10, Tom7, Mdm12, and Mmm1 proteins in the assembly of mitochondrial outer membrane proteins in Neurospora crassa.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 62 citations in OpenAlex.
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- Transport of Proteins into Mitochondria.The protein journal · 2019Review
- Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017Review
- Identification of new channels by systematic analysis of the mitochondrial outer membrane.The Journal of cell biology · 2017Article
- Revisiting trends on mitochondrial mega-channels for the import of proteins and nucleic acids.Journal of bioenergetics and biomembranes · 2017Review
- Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10.Nature communications · 2016Article
- How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016Review
- Phosphatidylcholine affects the role of the sorting and assembly machinery in the biogenesis of mitochondrial β-barrel proteins.The Journal of biological chemistry · 2015Article
- The ubiquitous and ancient ER membrane protein complex (EMC): tether or not?F1000Research · 2015Article
- Does aberrant membrane transport contribute to poor outcome in adult acute myeloid leukemia?Frontiers in pharmacology · 2015Article
- Evidence supporting the 19 β-strand model for Tom40 from cysteine scanning and protease site accessibility studies.The Journal of biological chemistry · 2014Article
- Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Role of phosphatidylethanolamine in the biogenesis of mitochondrial outer membrane proteins.The Journal of biological chemistry · 2013Article
- Article
- Characterization of the insertase for β-barrel proteins of the outer mitochondrial membrane.The Journal of cell biology · 2012Article
- Mechanisms of protein sorting in mitochondria.Cold Spring Harbor perspectives in biology · 2012Review
- From evolution to pathogenesis: the link between β-barrel assembly machineries in the outer membrane of mitochondria and gram-negative bacteria.International journal of molecular sciences · 2012Review
- Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex.Molecular biology of the cell · 2011Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
The Mdm10, Mdm12, and Mmm1 proteins have been implicated in several mitochondrial functions including mitochondrial distribution and morphology, assembly of beta-barrel proteins such as Tom40 and porin, association of mitochondria and endoplasmic reticulum, and maintaining lipid composition of mitochondrial membranes. Here we show that loss of any of these three proteins in Neurospora crassa results in the formation of large mitochondrial tubules and reduces the assembly of porin and Tom40 into the outer membrane. We have also investigated the relationship of Mdm10 and Tom7 in the biogenesis of beta-barrel proteins. Previous work showed that mitochondria lacking Tom7 assemble Tom40 more efficiently, and porin less efficiently, than wild-type mitochondria. Analysis of mdm10 and tom7 single and double mutants, has demonstrated that the effects of the two mutations are additive. Loss of Tom7 partially compensates for the decrease in Tom40 assembly resulting from loss of Mdm10, whereas porin assembly is more severely reduced in the double mutant than in either single mutant. The additive effects observed in the double mutant suggest that different steps in beta-barrel assembly are affected in the individual mutants. Many aspects of Tom7 and Mdm10 function in N. crassa are different from those of their homologues in Saccharomyces cerevisiae.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.