ASCB interviewed Patrick Lusk and Megan King to understand their interests and journeys in science.
- November 04, 2022
On Friday, October 28, Albertus Magnus College Professors Mark Barreuther and Rebecca Brogan brought 7 Albertus Magnus undergraduate students to Yale Cancer Center for the first Albertus Magnus Cancer Research Student Science Day.
- September 05, 2022Source: ASBMB Today
ASBMB highlights the LusKing and other jointly run laboratories.
- May 16, 2022
A diverse team of BRCA gene experts work together to unlock the secrets of DNA repair and develop better breast, ovarian and other cancer treatments.
- March 20, 2022
To celebrate Women's History Month, we want to highlight the female faculty in our department of Cell Biology at Yale.
- February 09, 2022
Yale Cancer Center is pleased to announce three new leadership appointments to continue to build and support our internationally-recognized cancer research program.
- February 08, 2022
Yale School of Medicine has extended its paid child rearing leave for eligible faculty from eight weeks to 12 weeks thanks to support from Valerie Horsley, PhD, and Megan King, PhD.
- October 31, 2021
How can a cytosolic autophagy machinery "eat" parts of the nucleus? New work from LusKing and Melia labs provide an answer.Source: Journal of Cell Biology
It is known that pathological protein aggregates can accumulate within the nucleus and can be cleared by a cytosolic autophagy machinery. However, the underlying mechanisms that allow the autophagosome to "see" aberrant proteins that are hidden by the double membrane of the nuclear envelope remains unknown. In a collaborative work, Sunandini Chandra, Philip Mannino and David Thaller provide compelling new evidence for an outside-in mechanism where a transmembrane cargo adaptor localizes at the outer nuclear membrane and reaches across the nuclear envelope lumen to capture the inner nuclear membrane into vesicles that can be ultimately captured by the autophagosome.
- February 07, 2021Source: BioRxiv
DNA nanotechnology provides a versatile and powerful tool to dissect the structure-function relationship of biomolecular machines like the nuclear pore complex (NPC), an enormous protein assembly that controls molecular traffic between the nucleus and cytoplasm. To understand how the intrinsically disordered, Phe-Gly-rich nucleoporins (FG-nups) within the NPC’s central transport channel impede the diffusion of macromolecules, Yale researchers built a DNA-origami NanoTrap. The NanoTrap comprises precisely arranged FG-nups in an NPC-like channel, which sits on a baseplate that captures macromolecules that pass through the FG network. The DNA-origami based nuclear pore mimics can now trap molecules and test how FG-nups form diffusion barriers within nanopore confinement. Published in the BioRxiv, Qi Shen leading the collaboration with Chenxiang Lin (Cell Biology & Nanobiology Institute) and Patrick Lusk (Cell Biology).
- December 13, 2020Source: BioRxiv
Small holes in the nuclear membranes lead to the recruitment of the endosomal sorting complexes required for transport (ESCRT), which seal the holes and protect the integrity of the nucleus. New work from the LusKing group has discovered that a key element of this surveillance pathway is the directly binding of a key nuclear envelope ESCRT, Chm7 to phosphatidic acid rich membranes.