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Peer-reviewedCC BYMicroPublication biology

The C. elegans pharyngeal basement membrane has a high affinity for binding agrin.

  • C Teresa Ibeanu1
  • Sandhya Srinivasan1
  • Qiuyi Chi1
  • David R Sherwood1
  1. 1Biology, Duke University, Durham, NC, United States.
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Abstract

Basement membranes (BMs) are dense, sheet-like extracellular matrices that surround animal tissues and provide mechanical and signaling functions. Tissue BMs are compositionally unique, with the presence and abundance of numerous components tailored to meet tissue-specific needs. How BMs establish and maintain distinct compositions remains poorly understood. Here, we investigate how the BM protein agrin is uniquely concentrated in the C. elegans pharyngeal BM. Through tissue-specific expression and live imaging, our results suggest that a combination of pharyngeal-specific expression and high BM affinity for binding agrin ensures the unique enrichment of agrin in the pharyngeal BM.

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Cite

BibTeXRIS
BibTeX
@article{ibeanu2026elegans,
  title = {{The C. elegans pharyngeal basement membrane has a high affinity for binding agrin.}},
  author = {C Teresa Ibeanu and Sandhya Srinivasan and Qiuyi Chi and David R Sherwood},
  journal = {MicroPublication biology},
  year = {2026},
  month = oct,
  doi = {10.17912/micropub.biology.002449},
  url = {https://europepmc.org/article/MED/42997129},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - The C. elegans pharyngeal basement membrane has a high affinity for binding agrin.
AU  - C Teresa Ibeanu
AU  - Sandhya Srinivasan
AU  - Qiuyi Chi
AU  - David R Sherwood
PY  - 2026
DA  - 2026/10/21
JO  - MicroPublication biology
DO  - 10.17912/micropub.biology.002449
UR  - https://europepmc.org/article/MED/42997129
AB  - Basement membranes (BMs) are dense, sheet-like extracellular matrices that surround animal tissues and provide mechanical and signaling functions. Tissue BMs are compositionally unique, with the presence and abundance of numerous components tailored to meet tissue-specific needs. How BMs establish and maintain distinct compositions remains poorly understood. Here, we investigate how the BM protein agrin is uniquely concentrated in the C. elegans pharyngeal BM. Through tissue-specific expression and live imaging, our results suggest that a combination of pharyngeal-specific expression and high BM affinity for binding agrin ensures the unique enrichment of agrin in the pharyngeal BM.
SN  - 2578-9430
ER  -