μMap-Interface: Temporal Photoproximity Labeling Identifies F11R as a Functional Member of the Transient Phagocytic
Sean W Huth1,2, Jacob B Geri1,2, James V Oakley1,2
1Merck Center for Catalysis at Princeton University, Princeton, New Jersey 08544, United States.
Journal of the American Chemical Society
|November 12, 2024
Summary
We developed a new method, μMap-Interface, to map proteins involved in phagocytosis, revealing new therapeutic targets like F11R which influences cancer activity.
Area of Science:
- Proteomics
- Cell Biology
- Biochemistry
Background:
- Phagocytosis is crucial for immune response and tissue repair.
- Identifying transient surface proteins in phagocytosis is challenging.
- Understanding these proteins can offer new therapeutic strategies.
Purpose of the Study:
- To introduce a novel photocatalytic proximity labeling method, μMap-Interface.
- To enable spatiotemporal mapping of the phagocytic interactome.
- To profile the dynamic surface proteome of human macrophages during engulfment.
Main Methods:
- Utilized photocatalyst-conjugated IGG-opsonized beads for synchronized phagocytosis.
- Captured protein interaction "snapshots" at the phagocyte-target interface.
- Employed super-resolution microscopy for validation.
Main Results:
- Identified known and novel protein interactors in phagocytosis.
- Discovered F11R as a potential novel interactor and cancer target.
- Demonstrated that F11R knockdown enhances phagocytosis, suggesting oncogenic links.
- Captured distinct surfaceomes from macrophages and neutrophil-like cells.
Conclusions:
- μMap-Interface provides spatiotemporal insights into phagocytosis.
- The method identified F11R, a protein with implications for cancer.
- This technique can advance understanding of phagocytic processes across various cellular contexts.
