ArticleThe Journal of biological chemistry2011
Distinct functions of evolutionary conserved MSF1 and late embryogenesis abundant (LEA)-like domains in mitochondria.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics.Frontiers in plant science · 2023Review
- Article
- Lipid metabolism-related proteins of relevant evolutionary and lymphoid interest (PRELI) domain containing family proteins in cancer.American journal of translational research · 2020Review
- Identification of novel and robust internal control genes from Volvariella volvacea that are suitable for RT-qPCR in filamentous fungi.Scientific reports · 2016Article
- Phosphatidylserine transport by Ups2-Mdm35 in respiration-active mitochondria.The Journal of cell biology · 2016Article
- Structural basis of intramitochondrial phosphatidic acid transport mediated by Ups1-Mdm35 complex.EMBO reports · 2015Article
- Group 1 LEA proteins, an ancestral plant protein group, are also present in other eukaryotes, and in the archeae and bacteria domains.Molecular genetics and genomics : MGG · 2013Article
- Late embryogenesis abundant proteins protect human hepatoma cells during acute desiccation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Spare PRELI gene loci: failsafe chromosome insurance?PloS one · 2012Article
- Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
PRELID1, the only late embryogenesis abundant (LEA) domain-containing protein in humans, exerts cytoprotective effects through its LEA domain within the mitochondria. Although PRELID1 homologs in vertebrates contain the LEA domain, homologs in lower eukaryotes are thought to lack this domain. In this study, we identify a novel LEA-like domain in a yeast PRELID1 homolog, Ups2p, which contains sequence conservation with the LEA domain of human PRELID1. PRELID1 homologs, including Ups2p, are known to contain the PRELI/MSF1 domain. Our study reveals that the MSF1 domain of Ups2p maintains proper mitochondrial electron transport chain function, respiratory competency, and mitochondrial phosphatidylethanolamine metabolism. The Ups2p MSF1 domain mediates cardiolipin depletion in the absence of Ups1p. However, the Ups2p LEA-like domain is responsible for cardiolipin depletion resulting from UPS2 overexpression. The regulation of phosphatidylethanolamine levels by the MSF1 domain is antagonized by the Ups2p LEA-like domain. We demonstrate that the yeast LEA-like domain protects cells from oxidative stress and can be functionally replaced by the human LEA domain. Together our studies suggest distinct roles of MSF1 and LEA-like domains in mitochondrial function and resistance to oxidative stress.
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