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Life Science Research Foundation Fellow


I received my undergraduate degree from the University of Colorado Boulder, where I studied ER motility with Gia Voeltz. I then pursued my graduate training with Patrick Lusk in the Department of Cell Biology at Yale. Using budding yeast as a model for nuclear pore complex (NPC) assembly, I discovered an ESCRT-III and Vps4-mediated quality control mechanism that surveils NPC assembly.


My goal in the Dillin lab is to define mechanisms that promote secretory protein homeostasis and endomembrane compartmentalization with an emphasis on how the collapse of these mechanisms contributes to aging



Webster BM*, Thaller D*, Jäger J, Ochmann SE, Borah S, Lusk, CP. (2016) Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing. EMBO J 15, 2447-2467. PMID: 27733427

Webster, BM & Lusk, CP. (2016) Border safety: quality control at the nuclear envelope. Trends in Cell Biology 26, 29-39. PMID: 26437591


Webster, BM & Lusk, CP. (2015) ESCRTs breach the nuclear border. Nucleus 5, 1-6. PMID: 25942571


Webster, BM, Colombi, P, Jäger, J, Lusk, CP. (2014) Surveillance of nuclear pore complex assembly by ESCRT-III/Vps4. Cell 159, 388–401. PMID: 25303532


Colombi, P, Webster BM, Frolich, F, Lusk, CP. (2013) The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1. Journal of Cell Biology. 203, 215–232. PMID: 24165936


Friedman JR*, Webster BM*, Mastronarde, DN, Verhey KJ & Voeltz GK (2010). ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules. Journal of Cell Biology, 190: 363-375. PMID: 20696706

Brant Webster, Ph.D. TeamMember
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