ArticleThe Journal of cell biology2020
The Pex3-Inp1 complex tethers yeast peroxisomes to the plasma membrane.
Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Visualisation of peroxisomes: a journey through seven decades.Histochemistry and cell biology · 2026Review
- Evolutionary remodeling of a remnant GET pathway factor into PEX38, an essential peroxin.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The yeast peroxisomal proteome at absolute quantitative scale.Histochemistry and cell biology · 2026Article
- Pex3 promotes formation of peroxisome-peroxisome and peroxisome-lipid droplet contact sites.Scientific reports · 2025Article
- Pex30-dependent membrane contact sites maintain ER lipid homeostasis.The Journal of cell biology · 2025Article
- STED super-resolution microscopy unveils the dynamics of Atg30 on yeast Pex3-labeled peroxisomes.iScience · 2024Article
- Spindle Position Checkpoint Kinase Kin4 Regulates Organelle Transport inBiomolecules · 2023Article
- Systematic multi-level analysis of an organelle proteome reveals new peroxisomal functions.Molecular systems biology · 2022Article
- Yeast Vps13 is Crucial for Peroxisome Expansion in Cells With Reduced Peroxisome-ER Contact Sites.Frontiers in cell and developmental biology · 2022Article
- Peroxisomal Membrane Contact Sites in Yeasts.Frontiers in cell and developmental biology · 2021Review
- Dynamic Regulation of Peroxisomes and Mitochondria during Fungal Development.Journal of fungi (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A subset of peroxisomes is retained at the mother cell cortex by the Pex3-Inp1 complex. We identify Inp1 as the first known plasma membrane-peroxisome (PM-PER) tether by demonstrating that Inp1 meets the predefined criteria that a contact site tether protein must adhere to. We show that Inp1 is present in the correct subcellular location to interact with both the plasma membrane and peroxisomal membrane and has the structural and functional capacity to be a PM-PER tether. Additionally, expression of artificial PM-PER tethers is sufficient to restore retention in inp1Δ cells. We show that Inp1 mediates peroxisome retention via an N-terminal domain that binds PI(4,5)P2 and a C-terminal Pex3-binding domain, forming a bridge between the peroxisomal membrane and the plasma membrane. We provide the first molecular characterization of the PM-PER tether and show it anchors peroxisomes at the mother cell cortex, suggesting a new model for peroxisome retention.
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Registered trials
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.