Skip to content
DraconiticResearch
Search Sources API
190,860 studies31 sourcesUpdated 36 min ago
Peer-reviewedCC BY 4.0Nature Communications

Identification of TMEM263 as an ER-resident protein that controls early stages of lipid droplet biogenesis

  • Katy Yalci1,2
  • Nafsika Chala1
  • Joanna Moss1
  • Connor MacDonald3
  • Przemysław Zakrzewski1
  • Phineas Smith1
  • Rabia Sevil1
  • Lana Willoughby1
  • Seren Wonklyn1
  • Thomas Andrews1
  • Chrissy L. Hammond1
  • Robin A. Corey3
1 more authors
  • Bernadette Carroll1
  1. 1School of Biochemistry and Biomedical Sciences, University of Bristol, Biomedical Science Building, Bristol, UK
  2. 2Present Address: Department of Physiology, Anatomy and Genetics, University of Oxford, Oxford, UK
  3. 3School of Psychology and Neuroscience, University of Bristol, Biomedical Science Building, Bristol, UK
Read full textPDFDOICite

Abstract

Cell and organismal growth is controlled not only by the availability of nutrients, but also the ability to dynamically sense and respond to changes in metabolic demand. We have identified a protein, TMEM263 (also known as C12orf23) as a mechanistic link between growth and lipid metabolism. TMEM263 was discovered in a screen as an ER-resident protein, and we have characterised its role as both necessary and sufficient for lipid droplet formation. TMEM263 has two transmembrane domains that fold into a dynamic alpha hairpin which are essential for its localisation to the ER and to support lipid droplet accumulation. Functionally, we propose that TMEM263 can interact with and support the condensation of neutral lipids in a bilayer to promote lipid droplet formation and growth. Consistently, loss of TMEM263 in cells and in zebrafish significantly impairs lipid droplet accumulation. Loss of TMEM263 protein function in vivo is associated with organismal growth defects and proportional dwarfism and our study provides a mechanistic understanding linking these phenotypes to impaired lipid droplet biology.

Related

  1. Lactate promotes mitochondrial biogenesis and fusion via GPR81 to enhance synaptic plasticity-related protein expression in hippocampal cells
    Qinghui Shang, Xuepeng Bian, Shujie Lou
    Frontiers in cell and developmental biologyPeer-reviewedCC BYFull textGeneral biochemistryEurope PMC
  2. Semidilute Polymer Scaling Controls PEG-induced Protein Phase Separation
    M. Ahmad, H. Ouzon-Shubeita, M. Whende +2
    bioRxivPreprintCC BY-NCFull textBiophysicsbioRxiv
  3. An intrinsically disordered adaptor protein controls the size and composition of EGFR condensates on membranes
    M. F. Ullo, D. E. Tillman, H. Coban +4
    bioRxivPreprintCC BY-NC-NDFull textBiophysicsbioRxiv
  4. Hierarchical cysteine oxidation controls reversible amyloid formation in an ankyrin repeat protein
    A. Sethi, H. Darroch, N. J. Magon +9
    bioRxivPreprintCC BYFull textMolecular biology & gene regulationbioRxiv
  5. Sample preparation for direct nanopore based protein identification via tryptic peptide recognition
    C. Hensel, C. Kleber, I. Suppanz +9
    bioRxivPreprintAll rights reservedFull textGeneral biochemistrybioRxiv

Cite

BibTeXRIS
BibTeX
@article{yalci2026identification,
  title = {{Identification of TMEM263 as an ER-resident protein that controls early stages of lipid droplet biogenesis}},
  author = {Katy Yalci and Nafsika Chala and Joanna Moss and Connor MacDonald and Przemysław Zakrzewski and Phineas Smith and Rabia Sevil and Lana Willoughby and Seren Wonklyn and Thomas Andrews and Chrissy L. Hammond and Robin A. Corey and Bernadette Carroll},
  journal = {Nature Communications},
  year = {2026},
  month = sep,
  doi = {10.1038/s41467-026-78093-9},
  url = {https://doi.org/10.1038/s41467-026-78093-9},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Identification of TMEM263 as an ER-resident protein that controls early stages of lipid droplet biogenesis
AU  - Katy Yalci
AU  - Nafsika Chala
AU  - Joanna Moss
AU  - Connor MacDonald
AU  - Przemysław Zakrzewski
AU  - Phineas Smith
AU  - Rabia Sevil
AU  - Lana Willoughby
AU  - Seren Wonklyn
AU  - Thomas Andrews
AU  - Chrissy L. Hammond
AU  - Robin A. Corey
AU  - Bernadette Carroll
PY  - 2026
DA  - 2026/09/28
JO  - Nature Communications
DO  - 10.1038/s41467-026-78093-9
UR  - https://doi.org/10.1038/s41467-026-78093-9
AB  - Cell and organismal growth is controlled not only by the availability of nutrients, but also the ability to dynamically sense and respond to changes in metabolic demand. We have identified a protein, TMEM263 (also known as C12orf23) as a mechanistic link between growth and lipid metabolism. TMEM263 was discovered in a screen as an ER-resident protein, and we have characterised its role as both necessary and sufficient for lipid droplet formation. TMEM263 has two transmembrane domains that fold into a dynamic alpha hairpin which are essential for its localisation to the ER and to support lipid droplet accumulation. Functionally, we propose that TMEM263 can interact with and support the condensation of neutral lipids in a bilayer to promote lipid droplet formation and growth. Consistently, loss of TMEM263 in cells and in zebrafish significantly impairs lipid droplet accumulation. Loss of TMEM263 protein function in vivo is associated with organismal growth defects and proportional dwarfism and our study provides a mechanistic understanding linking these phenotypes to impaired lipid droplet biology.
SN  - 2041-1723
ER  -