Peroxisomes articles within Nature Communications

Featured

  • Article
    | Open Access

    Import of proteins into peroxisomes depends on PEX5, PEX13 and PEX14. Here the authors obtain crystal structures and NMR data to show the recognition of diaromatic peptide motifs on a noncanonical surface of the PEX13 SH3 domain, revealing a dynamic network which modulates peroxisomal matrix import.

    • Stefan Gaussmann
    • , Rebecca Peschel
    •  & Michael Sattler

  • Article
    | Open Access

    Hunt et al. identify the protein sets that are modulated by RNAi for each E2 ubiquitin-conjugating enzyme in human cells. By analyzing the UBA1/E2-sensitive proteome, they report an adaptive stress response that preserves peroxisomal protein import in cells with decreased ubiquitination capacity.

    • Liam C. Hunt
    • , Vishwajeeth Pagala
    •  & Fabio Demontis

  • Article
    | Open Access

    The AAA ATPase Pex1/Pex6 fuels the enzyme import across the peroxisomal membrane. Defects in either ATPase in humans result in severe disorders and early death. Here, the authors provide a detailed cryo-EM structures of the complex in the process of translocating an endogenous substate.

    • Maximilian Rüttermann
    • , Michelle Koci
    •  & Christos Gatsogiannis

  • Article
    | Open Access

    Artificial organelles can potentially be used support cellular functions, but there is a trade-off between cellular uptake and cellular retention. Here, the authors report the dynamic assembly of DNA-ceria-based artificial peroxisomes in cells, and show they can be used to reduce intracellular ROS.

    • Chi Yao
    • , Yuwei Xu
    •  & Dayong Yang

  • Article
    | Open Access

    Peroxisomes are organelles compartmentalising metabolic reactions such as the breakdown of fats, and are commonly thought of as single membrane-bound compartments. Here the authors show that Arabidopsis peroxisomes contain extensive internal vesicles that form from the bounding membrane in an ESCRT-dependent process.

    • Zachary J. Wright
    •  & Bonnie Bartel

  • Article
    | Open Access

    Pexophagy removes damaged peroxisomes, which are particularly prone to ROS formation. Here, the authors use light to induce peroxisome turnover by local ROS generation, showing STUB1 translocation is critical and might contribute to human disease.

    • Bo-Hua Chen
    • , Yao-Jen Chang
    •  & Wei Yuan Yang

  • Article
    | Open Access

    Import of proteins into specific cellular compartments is critical for organelle function and several proteins are known to be imported into multiple compartments. Here, the authors report that the protein Ptc5 is first sorted to and processed in the mitochondria before being targeted to peroxisomes, which may influence mitochondria-peroxisome interorganellar contact.

    • Thorsten Stehlik
    • , Marco Kremp
    •  & Johannes Freitag

  • Article
    | Open Access

    Drp1 and Dnm2 have been implicated in mitochondrial fission events, although their specific activities in constriction and scission have been unclear. Here, the authors demonstrate that Drp1 is sufficient to constrict and sever mitochondrial and peroxisomal membranes in the absence of Dnm proteins.

    • Sukrut C. Kamerkar
    • , Felix Kraus
    •  & Michael T. Ryan

  • Article
    | Open Access

    Mitochondria and peroxisomes require a dynamin-like GTPase to remodel membranes during division. Here the authors identify DYNAMO1, a nucleoside diphosphate kinase-like protein that generates a local source of GTP to promote constriction of the division machinery and produce daughter organelles.

    • Yuuta Imoto
    • , Yuichi Abe
    •  & Yukio Fujiki

  • Article
    | Open Access

    Lipid droplets (LDs) and peroxisomes are both generated by budding off the endoplasmic reticulum (ER). Here, the authors show that the yeast protein Pex30 marks ER subdomains where both LD and peroxisome biogenesis occurs, and identify MCTP2 as the putative mammalian Pex30 ortholog.

    • Amit S. Joshi
    • , Benjamin Nebenfuehr
    •  & William A. Prinz

  • Article
    | Open Access

    The internal organization of the cell has been enriched by the discovery that organelles establish membrane contact sites, however the entire repertoire of these contacts is still being explored. Here the authors systematically identify the landscape of cellular contact sites in yeast, discovering four potential novel contact sites and two tether proteins for the peroxisome-mitochondria contact site.

    • Nadav Shai
    • , Eden Yifrach
    •  & Einat Zalckvar

  • Article
    | Open Access

    Pex1 and Pex6 form a heterohexameric Type-2 AAA-ATPase motor whose function in peroxisomal matrix-protein import is still debated. Here, the authors combine structural, biochemical, and cell-biological approaches to show that Pex1/Pex6 is a protein unfoldase, which supports a role in mechanical unfolding of peroxin proteins.

    • Brooke M. Gardner
    • , Dominic T. Castanzo
    •  & Andreas Martin

  • Article
    | Open Access

    Compartmentalization of enzymes into cellular organelles is a promising strategy for improving pathway efficiency. Here, the authors use a high-throughput assay to identify enhanced peroxisomal targeting signals in yeast, and study the effects of peroxisomal compartmentalization on the performance of a model pathway.

    • William C. DeLoache
    • , Zachary N. Russ
    •  & John E. Dueber

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