Spatial mapping of cell-surface protein glycosylation at molecular resolution
Moonnukandathil Joseph, D.; Sison, N. L.; Yurekli, N.; Culpepper, S.; Moeckl, L.
Show abstract
Cell-surface protein glycosylation is a fundamental post-translational modification that plays a crucial role in membrane protein function and cellular behavior. However, elucidating the molecular spatial organization of the cell-surface glycoproteome within the native cellular context has remained challenging due to its structural complexity and density. Here, we introduce a super-resolution microscopy-based approach that enables the spatial analysis of a protein and its glycosylation pattern directly in the cellular environment. Our strategy relies on a combination of lectin-based labeling, metabolic oligosaccharide engineering, and immunocytochemistry. This allows for the mapping of individual protein glycoforms as well as sialylation states of single proteins. By providing access to the spatial axis of the cell-surface glycoproteome, our technique opens up new avenues for understanding the molecular architecture of protein glycosylation in biological processes of central relevance, including, but not limited to, development, signaling, and immune system regulation.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscs 93%
- Mass-sensitive particle tracking (MSPT) to elucidate the membrane-associated MinDE reactioncycle 93%
- O-Pair Search with MetaMorpheus for O-glycopeptide Characterization 93%
Similar papers in this journal
- Detecting nanoscale distribution of protein pairs by proximity dependent super-resolution microscopy 93%
- Probing nanoscale diffusional heterogeneities in cellular membranes through multidimensional single-molecule and super-resolution microscopy 93%
- Bottom-up investigation of spatiotemporal glycocalyx dynamics with interferometric scattering microscopy 93%
Similar papers in this journal
- One-Step Selective Labeling of Native Cell-Surface Sialoglycans by Exogenous α2,8-Sialylation 95%
- Spatiotemporal proximity labeling tools to track GlcNAc sugar-modified functional protein hubs during cellular signaling 94%
- Multiplex, quantitative, high-resolution imaging of protein:protein complexes via hybridization chain reaction 93%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.