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Published on: December 21, 2011
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Proximity-dependent biotin identification (BioID) screening identified novel layilin-proximal proteins
Atsuhiro Tsutiya1, Kouhei Nagai2, Masaaki Sato1
1Clinical Proteomics and Molecular Medicine, St. Marianna University Graduate School of Medicine, 2-16-1 Sugao, Miyamae, Kawasaki, Kanagawa, 216-8511, Japan.
Biochemical and Biophysical Research Communications
|August 9, 2025
Summary
This study identified 18 proteins interacting with layilin using proximity-dependent biotin identification (BioID). These findings offer new insights into layilin
Area of Science:
- Cell Biology
- Molecular Biology
- Proteomics
Background:
- Layilin, a transmembrane protein, is involved in cell motility, mitochondrial regulation, immune responses, and ciliogenesis.
- Understanding layilin's functions requires identifying its interacting proteins, but this information is limited.
- This study aimed to comprehensively identify layilin-interacting proteins.
Purpose of the Study:
- To identify proteins that interact with layilin using proximity-dependent biotin identification (BioID).
- To gain insights into the intracellular network and functions of layilin.
Main Methods:
- A BioID2-layilin fusion protein was expressed in HEK293 cells to biotinylate proximal proteins.
- Biotinylated peptides were purified and analyzed using liquid chromatography-tandem mass spectrometry (LC-MS/MS).
- Identified proteins underwent Gene Ontology (GO) enrichment analysis.
Main Results:
- 173 proteins were identified in the BioID2-layilin group, with 19 exclusively identified.
- 18 layilin-proximal proteins were identified, excluding the bait protein.
- GO analysis indicated enrichment in protein folding and localization pathways.
Conclusions:
- BioID screening successfully identified potential layilin interactors.
- These findings provide a foundation for future research on layilin's molecular mechanisms and functions.

