@article {70178,
	title = {ER-to-Golgi Trafficking is a Nutrient-Sensitive Checkpoint Linking Glucose Starvation to Cell Surface Remodeling},
	journal = {bioRxiv},
	year = {2025},
	month = {2025 October 31},
	abstract = {<p>Cancer cells adapt to nutrient stress by remodeling the repertoire of proteins on their surface, enabling survival and progression under starvation conditions. However, the molecular mechanisms by which nutrient cues reshape the cell surface proteome to influence cell behavior remain largely unresolved. Here, we show that acute glucose starvation, but not amino acid deprivation or mTOR inhibition, selectively impairs ER-to-Golgi export of specific cargoes, such as E-cadherin, in a SEC24C-dependent manner. Quantitative cell surface proteomics reveal that glucose deprivation remodels the cell surface proteome, notably reducing surface expression of key adhesion molecules. This nutrient-sensitive reprogramming enhances cell migration in vitro and promotes metastasis in vivo. Mechanistically, we show that AMPK and ULK1 signaling orchestrate this process independent of autophagy, with ULK1-mediated phosphorylation of SEC31A driving SEC24C-dependent COPII reorganization. These findings establish ER-to-Golgi trafficking as a nutrient-sensitive regulatory node that links metabolic stress to cell surface remodeling and metastatic potential.</p>
},
	doi = {10.1101/2025.10.31.685804},
	url = {https://www.biorxiv.org/content/early/2025/11/01/2025.10.31.685804},
	author = {Joo, Joung Hyuck and Kasberg, William and Douglas, Spencer and Udoh, Uwemedimo and Carisey, Alexandre and Messing, James and Wang, Yong-Dong and Narina, Shilpa and Pruett-Miller, Shondra M. and Labelle, Myriam and Lippincott-Schwartz, Jennifer and Chang, Chi-Lun and Kundu, Mondira}
}
@article {69945,
	title = {Macrophages release neuraminidase and cleaved calreticulin for programmed cell removal.},
	journal = {Proc Natl Acad Sci U S A},
	volume = {122},
	year = {2025},
	month = {2025 May 27},
	pages = {e2426644122},
	abstract = {<p>Calreticulin (CALR) is primarily an endoplasmic reticulum chaperone protein that also plays a key role in facilitating programmed cell removal (PrCR) by acting as an "eat-me" signal for macrophages, directing their recognition and engulfment of dying, diseased, or unwanted cells. Recent findings have demonstrated that macrophages can transfer their own CALR onto exposed asialoglycans on target cells, marking them for PrCR. Despite the critical role CALR plays in this process, the molecular mechanisms behind its secretion by macrophages and the formation of binding sites on target cells remain unclear. Our findings show that CALR undergoes C-terminal cleavage upon secretion, producing a truncated form that functions as the active eat-me signal detectable on target cells. We identify cathepsins as potential proteases involved in this cleavage process. Furthermore, we demonstrate that macrophages release neuraminidases, which modify the surface of target cells and facilitate CALR binding. These insights reveal a coordinated mechanism through which lipopolysaccharide (LPS)-activated macrophages regulate CALR cleavage and neuraminidase activity to mark target cells for PrCR. How they recognize the cells to be targeted remains unknown.</p>
},
	keywords = {Animals, Apoptosis, Calreticulin, Humans, Lipopolysaccharides, Macrophages, Mice, Neuraminidase},
	issn = {1091-6490},
	doi = {10.1073/pnas.2426644122},
	url = {https://doi.org/10.1073/pnas.2426644122},
	author = {Banuelos, Allison and Baez, Michelle and Zhang, Allison and Y{\i}lmaz, Leyla and Kasberg, William and Volk, Regan and Georgeos, Nardin and Koren-Sedova, Elle and Le, Uyen and Burden, Andrew T and Marjon, Kristopher D and Lippincott-Schwartz, Jennifer and Zaro, Balyn W and Weissman, Irving L}
}
