ArticlePLoS biology2024
Proteins that carry dual targeting signals can act as tethers between peroxisomes and partner organelles.
Article in PLoS biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- TOR and heat shock response pathways regulate peroxisome biogenesis during proteotoxic stress.Nature communications · 2025Article
- Three-stage sequential targeted nasal drops for correcting abnormal mitochondrial division in microglia.Bioactive materials · 2025Article
- Spatial protein redistribution: wandering but not lost.Cellular and molecular life sciences : CMLS · 2025Review
- Using chanarin-dorfman syndrome patient fibroblasts to explore disease mechanisms and new treatment avenues.Orphanet journal of rare diseases · 2025Article
- Peroxisomal core structures segregate diverse metabolic pathways.Nature communications · 2025Article
- Organelle activity organized by the endoplasmic reticulum-mitochondria encounter structure -ERMES- is essential forMicrobial cell (Graz, Austria) · 2025Article
- Mitochondria, Peroxisomes and Beyond-How Dual Targeting Regulates Organelle Tethering.Contact (Thousand Oaks (Ventura County, Calif.))Review
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 3 countries.
Funding
Abstract
Peroxisomes are organelles with crucial functions in oxidative metabolism. To correctly target to peroxisomes, proteins require specialized targeting signals. A mystery in the field is the sorting of proteins that carry a targeting signal for peroxisomes and as well as for other organelles, such as mitochondria or the endoplasmic reticulum (ER). Exploring several of these proteins in fungal model systems, we observed that they can act as tethers bridging organelles together to create contact sites. We show that in Saccharomyces cerevisiae this mode of tethering involves the peroxisome import machinery, the ER-mitochondria encounter structure (ERMES) at mitochondria and the guided entry of tail-anchored proteins (GET) pathway at the ER. Our findings introduce a previously unexplored concept of how dual affinity proteins can regulate organelle attachment and communication.
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Registered trials
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