Microscopy-guided proteomics at organelle-level resolution has the power to reveal unknown proteins in disease- or functional-specific regions.

We present a breakthrough method for spatial protein purification using in situ subcellular photo-biotinylation, allowing precise labeling of proteins in user-defined regions, fully automated across thousands of fields of view.

With mass spectrometry, Syncell’s Microscoop offers unmatched sensitivity, specificity, and resolution to uncover subcellular proteomes.

Join us to learn more about this innovative technology and how Optoproteomics unlocks spatial insights into chromatin biology.

Friday, March 21st
14:00 – 15:30

Amphi Broca Nouvelle-Aquitaine
146 rue Léo-Saignat, 33076 Bordeaux

Invitation and Organization by Dr. J. Ezan, Neurocentre Magendie.

 

Featured Speakers

Cristiana Lungo, IZI Stuttgart

Matteo Cattaneo, Syncell

 

Agenda

Friday 21st March 2025, 2-3:30pm CET

14:00 - 14:10 Welcome Jérome Ezan, PhD (Neurocentre Magendie, PostDoc, BioProt)
14:10 - 14:40  Microscopic Scooping for Unbiased, Subcellular, Spatial Optoproteomic Discovery (25min + 5min Q&A) Matteo Cattaneo, PhD (SynCell, Field Application Specialist)
14:40 - 15:25 Optoproteomics provides spatially resolved insights into chromatin biology (40min + 5min Q&A) Cristiana Lungo, PhD (IZI Stuttgart, PostDoc, Cell Biology and Immunology)
15:25 - 15:30 Wrap Up Jérome Ezan, PhD

 

 

Abstracts

Microscopic Scooping for Unbiased, Subcellular, Spatial Optoproteomic Discovery (Syncell)

The quest for unbiased spatial proteomic discovery is critical in understanding the complex microenvironments within biological tissues. Traditional methods like proximity labeling and Laser Capture Microdissection (LCM) have their limitations: proximity labeling suffers from sample restriction (non-human models) and can lead to biased results due to incomplete labeling, while LCM is laborious and often lacks the precision needed for single-cell resolution.

 


 

Optoproteomics provides spatially resolved insights into chromatin biology (IZI Stuttgart)

Polycomb Repressive Complex 2 (PRC2), a master regulator of chromatin organization and gene expression, is frequently deregulated in aggressive malignancies such as triple-negative breast cancer (TNBC). While cytoplasmic mistargeting of its catalytic subunit, Enhancer of Zeste Homolog 2 (EZH2), has been implicated in TNBC metastasis, whether this misregulation also extends to the spatial organization of nuclear PRC2 pools remains unexplored. Here, we uncover a novel mechanism of PRC2 regulation in TNBC cells, characterized by the accumulation of PRC2 in distinct, micron-sized nuclear bodies. By using unbiased spatial proteomics on these endogenous compartments, we identify a key molecular driver of this subnuclear compartmentalization and link this spatial organization to cellular processes critical for metastasis. These findings underscore the power of opto-proteomics in dissecting the local chromatin interactome, with high spatial resolution, and reveal an unrecognized layer of PRC2 regulation in TNBC, where subnuclear compartmentalization orchestrates functional outcomes essential for cancer progression.

 

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