@article {70323,
	title = {Endocytome profiling uncovers cell-surface protein dynamics underlying neuronal connectivity.},
	journal = {Neuron},
	year = {2026},
	month = {2026 Mar 12},
	abstract = {<p>Endocytosis actively remodels the neuronal surface proteome to drive diverse cellular processes, yet its global extent and effects on neural circuit development have defied comprehensive interrogation. Here, we introduce endocytome profiling: a systematic, cell-type-specific approach for mapping cell-surface protein (CSP) dynamics in situ. Quantitative proteomic analysis of developing Drosophila olfactory receptor neuron (ORN) axons generated an endocytic atlas comprising over 1,000 proteins and revealed the extent to which the cell-surface proteome is remodeled to meet developmental demands. Targeted interrogation of a junctional CSP showed that its endosome-to-surface ratio is precisely balanced to enable developmental axon pruning while preserving mature axon integrity. Multi-omic integration uncovered widespread transcellular signaling and identified a growth factor secreted by neighboring neurons to direct ORN axon targeting via endocytic regulation of its receptor. Endocytome profiling provides unprecedented access to cell-surface proteome dynamics and offers a platform to dissect proteome-scale remodeling across diverse cell types and contexts.</p>
},
	issn = {1097-4199},
	doi = {10.1016/j.neuron.2026.01.027},
	url = {https://doi.org/10.1016/j.neuron.2026.01.027},
	author = {McLaughlin, Colleen N and Ji, Hui and Dong, Katherine X and Xu, Chuanyun and Wong, Kenneth Kin Lam and Li, Zhuoran and Luginbuhl, David J and Xu, Charles and Lyu, Cheng and Qin, Wei and Li, Jiefu and Udeshi, Namrata D and Carr, Steven A and Ting, Alice Y and Luo, Liqun}
}
@article {69570,
	title = {Cell-surface Milieu Remodeling in Human Dendritic Cell Activation.},
	journal = {J Immunol},
	year = {2024},
	month = {2024 Aug 12},
	abstract = {<p>Dendritic cells (DCs) are specialized sentinel and APCs coordinating innate and adaptive immunity. Through proteins on their cell surface, DCs sense changes in the environment, internalize pathogens, present processed Ags, and communicate with other immune cells. By combining chemical labeling and quantitative mass spectrometry, we systematically profiled and compared the cell-surface proteomes of human primary conventional DCs (cDCs) in their resting and activated states. TLR activation by a lipopeptide globally reshaped the cell-surface proteome of cDCs, with \&gt;100 proteins upregulated or downregulated. By simultaneously elevating positive regulators and reducing inhibitory signals across multiple protein families, the remodeling creates a cell-surface milieu promoting immune responses. Still, cDCs maintain the stimulatory-to-inhibitory balance by leveraging a distinct set of inhibitory molecules. This analysis thus uncovers the molecular complexity and plasticity of the cDC cell surface and provides a roadmap for understanding cDC activation and signaling.</p>
},
	issn = {1550-6606},
	doi = {10.4049/jimmunol.2400089},
	url = {https://doi.org/10.4049/jimmunol.2400089},
	author = {Udeshi, Namrata D and Xu, Charles and Jiang, Zuzhi and Gao, Shihong Max and Yin, Qian and Luo, Wei and Carr, Steven A and Davis, Mark M and Li, Jiefu}
}
