@article {68020,
	title = {ESCRT-mediated membrane repair protects tumor-derived cells against T cell attack.},
	journal = {Science},
	volume = {376},
	year = {2022},
	month = {2022 Apr 22},
	pages = {377-382},
	abstract = {<p>Cytotoxic T lymphocytes (CTLs) and natural killer cells kill virus-infected and tumor cells through the polarized release of perforin and granzymes. Perforin is a pore-forming toxin that creates a lesion in the plasma membrane of the target cell through which granzymes enter the cytosol and initiate apoptosis. Endosomal sorting complexes required for transport (ESCRT) proteins are involved in the repair of small membrane wounds. We found that ESCRT proteins were precisely recruited in target cells to sites of CTL engagement immediately after perforin release. Inhibition of ESCRT machinery in cancer-derived cells enhanced their susceptibility to CTL-mediated killing. Thus, repair of perforin pores by ESCRT machinery limits granzyme entry into the cytosol, potentially enabling target cells to resist cytolytic attack.</p>
},
	keywords = {Endosomal Sorting Complexes Required for Transport, Granzymes, Membrane Glycoproteins, Perforin, Pore Forming Cytotoxic Proteins, T-Lymphocytes, Cytotoxic},
	issn = {1095-9203},
	doi = {10.1126/science.abl3855},
	author = {Ritter, Alex T and Shtengel, Gleb and Xu, C Shan and Weigel, Aubrey and Hoffman, David P and Freeman, Melanie and Iyer, Nirmala and Alivodej, Nensi and Ackerman, David and Voskoboinik, Ilia and Trapani, Joseph and Hess, Harald F and Mellman, Ira}
}
@article {67233,
	title = {ER-to-Golgi protein delivery through an interwoven, tubular network extending from ER.},
	journal = {Cell},
	volume = {184},
	year = {2021},
	month = {2021 Apr 29},
	pages = {2412},
	abstract = {<p>Cellular versatility depends on accurate trafficking of diverse proteins to their organellar destinations. For the secretory pathway (followed by approximately 30\% of all proteins), the physical nature of the vessel conducting the first portage (endoplasmic reticulum [ER] to Golgi apparatus) is unclear. We provide a dynamic 3D view of early secretory compartments in mammalian cells with isotropic resolution and precise protein localization using whole-cell, focused ion beam scanning electron microscopy with cryo-structured illumination microscopy and live-cell synchronized cargo release approaches. Rather than vesicles alone, the ER spawns an elaborate, interwoven tubular network of contiguous lipid bilayers (ER exit site) for protein export. This receptacle is capable of extending microns along microtubules while still connected to the ER by a thin neck. COPII localizes to this neck region and dynamically regulates cargo entry from the ER, while COPI acts more distally, escorting the detached, accelerating tubular entity on its way to joining the Golgi apparatus through microtubule-directed movement.</p>
},
	issn = {1097-4172},
	doi = {10.1016/j.cell.2021.03.035},
	author = {Weigel, Aubrey V and Chang, Chi-Lun and Shtengel, Gleb and Xu, C Shan and Hoffman, David P and Freeman, Melanie and Iyer, Nirmala and Aaron, Jesse and Khuon, Satya and Bogovic, John and Qiu, Wei and Hess, Harald F and Lippincott-Schwartz, Jennifer}
}
