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Cited by 7Cellular transport and secretionLipid metabolism and biosynthesisFungal and yeast genetics research

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Pex30-dependent membrane contact sites maintain ER lipid homeostasis

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Ferreira, Joana Veríssimo, Ahmed, Yara, Heunis, Tiaan, Jain, Aamna, Johnson, Errin, Räschle, Markus, Ernst, Robert, Vanni, Stefano, Carvalho, Pedro·2025·Journal of Cell Biology
DOI 10.1083/jcb.202409039PMC PMC12101078

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Abstract

In eukaryotic cells, communication between organelles and the coordination of their activities depend on membrane contact sites (MCS). How MCS are regulated under the dynamic cellular environment remains poorly understood. Here, we investigate how Pex30, a membrane protein localized to the endoplasmic reticulum (ER), regulates multiple MCS in budding yeast. We show that Pex30 is critical for the integrity of ER MCS with peroxisomes and vacuoles. This requires the dysferlin (DysF) domain on the Pex30 cytosolic tail. This domain binds to phosphatidic acid (PA) both in vitro and in silico, and it is important for normal PA metabolism in vivo. The DysF domain is evolutionarily conserved and may play a general role in PA homeostasis across eukaryotes. We further show that the ER–vacuole MCS requires a Pex30 C-terminal domain of unknown function and that its activity is controlled by phosphorylation in response to metabolic cues. These findings provide new insights into the dynamic nature of MCS and their coordination with cellular metabolism.

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Metadata

Authors
Ferreira, J. V., Ahmed, Y., Heunis, T., Jain, A., Johnson, E., Räschle, M., Ernst, R., Vanni, S., & Carvalho, P.
Affiliations
  • University of Oxford (GB)
  • University of Fribourg (CH)
  • Saarland University (DE)
  • University of Kaiserslautern (DE)
Corresponding author
Carvalho, Pedro
ORCID
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2025-05-23
Volume
224
Issue
7
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.202409039
PMC
PMC12101078
OpenAlex
W4410656207
Cited by
7
References
4
Citations by year
2026: 3 · 2025: 4
FWCI
3.47
Type
journal article
Language
en
Open access
Licence
Locations
  • The Journal of Cell Biology (publishedVersion, other-oa)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
Funders
  • Oxford-EP Abraham Research Fund
  • Biotechnology and Biological Sciences Research Council (BB/W015722/1)
  • Wellcome Trust (223153/Z/21/Z)
  • European Research Council (803952)
  • Swiss National Supercomputing Centre (s1176, s1269)
  • University of Oxford
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords
membrane contact sites, endoplasmic reticulum, phosphatidic acid, phosphorylation, Saccharomyces cerevisiae, organelle communication, lipid metabolism
MeSH terms
Protein Domains, Endoplasmic Reticulum, Homeostasis, Intracellular Membranes, Membrane Proteins, Phosphatidic Acids, Phosphorylation, Saccharomyces cerevisiae, Vacuoles, Peroxisomes, Saccharomyces cerevisiae Proteins, Lipid Metabolism

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