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Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
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Exploring the CD38-associated surfaceome via nanobody-targeted TurboID.

Kangze Feng1, Ying Wei1, Shangcheng Yu1

  • 1MOE Key Laboratory of Bioinformatics, Center for Synthetic and Systematic Biology, State Key Laboratory of Complex, Severe, and Rare Diseases, School of Life Sciences, Tsinghua University, Beijing, China.

Molecular & Cellular Proteomics : MCP
|July 14, 2026
PubMed
Summary

Researchers developed nanobody-targeted TurboID (NBID) to map proteins near CD38 on cell surfaces. This revealed a CD38-associated adhesion network crucial for tumor cell migration and interactions with endothelial cells.

Keywords:
CD38Proximity labelingcell migrationnanobodysurfaceome nanoscale organizations

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Area of Science:

  • Cell Biology
  • Proteomics
  • Cancer Research

Background:

  • CD38 is a cell-surface glycoprotein with poorly understood molecular functions.
  • Understanding the CD38-proximal surfaceome is crucial for elucidating its biological roles.
  • Current methods lack the ability to comprehensively map proteins in close proximity to CD38 on live cells.

Purpose of the Study:

  • To develop and validate a novel proximity labeling method to characterize the CD38-proximal surfaceome.
  • To identify proteins associated with CD38 in different cell types, including lung cancer cells.
  • To investigate the functional role of CD38 in cell migration and tumor-endothelial interactions.

Main Methods:

  • Development of nanobody-targeted TurboID (NBID) using protein-of-interest (POI)-specific nanobody-TurboID chimeras (NTCs).
  • Application of NBID to A549 lung cancer cells and THP-1 monocytic leukemia cells.
  • Validation using EGFR-targeting NTCs and combination with SILAC (stable isotope labeling by amino acids in cell culture).
  • Total internal reflection fluorescence microscopy and functional assays for cell migration.

Main Results:

  • NBID successfully identified known EGFR-associated proteins, validating the approach.
  • Enrichment of proteins involved in adhesion, ECM organization, and lipid raft domains around CD38.
  • Identification of CD38-associated cadherin adhesion complexes (CDH2, DSG2) at the tumor-endothelial interface.
  • Demonstration of CD38's contribution to transendothelial migration of A549 cells.

Conclusions:

  • NBID is a robust platform for studying surface protein environments and intercellular interactions in native conditions.
  • A CD38-associated membrane adhesion network was revealed, involving cadherins.
  • CD38 plays a significant role in tumor cell migration and tumor-endothelial interactions.