ArticleJournal of cell science2022
The Hob proteins are novel and conserved lipid-binding proteins at ER-PM contact sites.
Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- Hoi1 targets BLTP2 to ER-PM contact sites to regulate lipid homeostasis.The Journal of cell biology · 2026Article
- Mechanistic dissection of BLTP2 targeting to ER-PM contact sites.bioRxiv : the preprint server for biology · 2026Article
- Endoplasmic reticulum patterns insect cuticle nanostructure.The Journal of cell biology · 2026Article
- The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Multiple interactions recruit BLTP2 to ER-PM contacts to control plasma membrane dynamics.The Journal of cell biology · 2025Article
- Neurodegenerative and Neurodevelopmental Roles for Bulk Lipid Transporters VPS13A and BLTP2.Movement disorders : official journal of the Movement Disorder Society · 2025Article
- The Vps13-like protein BLTP2 regulates phosphatidylethanolamine levels to maintain plasma membrane fluidity and breast cancer aggressiveness.Nature cell biology · 2025Article
- VPS13 and bridge-like lipid transporters, mechanisms, and mysteries.Frontiers in neuroscience · 2025Review
- ER-plasma membrane contact sites deliver ER lipids and proteins for rapid cell surface expansion.The Journal of cell biology · 2024Article
- Article
- The Endoplasmic Reticulum and Its Contacts: Emerging Roles in Axon Development, Neurotransmission, and Degeneration.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024Review
- Bridge-like lipid transfer protein family member 2 suppresses ciliogenesis.Molecular biology of the cell · 2024Article
- The bridge-like lipid transfer protein (BLTP) gene group: introducing new nomenclature based on structural homology indicating shared function.Human genomics · 2022Review
- Systematic analysis of membrane contact sites ineLife · 2022Article
- A novel superfamily of bridge-like lipid transfer proteins.Trends in cell biology · 2022Review
- Structural and biochemical insights into lipid transport by VPS13 proteins.The Journal of cell biology · 2022Article
- Vps13-like proteins provide phosphatidylethanolamine for GPI anchor synthesis in the ER.The Journal of cell biology · 2022Article
- A possible role for VPS13-family proteins in bulk lipid transfer, membrane expansion and organelle biogenesis.Journal of cell science · 2022Review
- Sequence Analysis and Structural Predictions of Lipid Transfer Bridges in the Repeating Beta Groove (RBG) Superfamily Reveal Past and Present Domain Variations Affecting Form, Function and Interactions of VPS13, ATG2, SHIP164, Hobbit and Tweek.Contact (Thousand Oaks (Ventura County, Calif.)) · 2022Article
- The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi Apparatus.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Membrane contact sites are critical junctures for organelle signaling and communication. Endoplasmic reticulum-plasma membrane (ER-PM) contact sites were the first membrane contact sites to be described; however, the protein composition and molecular function of these sites is still emerging. Here, we leverage yeast and Drosophila model systems to uncover a novel role for the Hobbit (Hob) proteins at ER-PM contact sites. We find that Hobbit localizes to ER-PM contact sites in both yeast cells and the Drosophila larval salivary glands, and this localization is mediated by an N-terminal ER membrane anchor and conserved C-terminal sequences. The C-terminus of Hobbit binds to plasma membrane phosphatidylinositols, and the distribution of these lipids is altered in hobbit mutant cells. Notably, the Hobbit protein is essential for viability in Drosophila, providing one of the first examples of a membrane contact site-localized lipid binding protein that is required for development.
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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.