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To celebrate Women's History Month, we want to highlight the female faculty in our department of Cell Biology at Yale.

Yale Cancer Center is pleased to announce three new leadership appointments to continue to build and support our internationally-recognized cancer research program.

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.

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.

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).

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.

Dr. Lusk and Dr. King, co-leaders of the "LusKing Lab" in the Department of Cell Biology were awarded Yale's Postdoctoral Mentoring prize for their commitment to the success of their trainees.

Megan C. King, PhD, associate professor of cell biology and of molecular, cellular and developmental biology, and Simon Mochrie, PhD, professor of physics and of applied physics, have been named Allen Distinguished Investigators by The Paul G. Allen Frontiers Group, a division of the Allen Institute.

Collaborative projects funded by the awards will address important questions about neurodegenerative disease, nucleus biology, and protein turnover