In new findings published in Science, the Rapoport Lab, with the help of the lab of Maofu Liao, used cryo-electron microscopy to determine the architecture of the entire active Hrd1 complex.
A team led by Robert Farese, Tobias Walther, and Jeeyun Chung (HMS/HSPH) discovered that a complex of lipid droplet assembly factor 1 in interaction with seipin, an endoplasmic reticulum (ER) protein, is the core protein machinery that drives the formation of LDs and determines where they form in the ER.
Assistant Professor Sichen (Susan) Shao was announced as one of 22 early-career scientists and engineers in the 2019 class of Packard Fellows for Science and Engineering from the David and Lucile Packard Foundation.
In their recent study published in Cell Reports, the Haigis Lab identified extracellular alanine as one of the extracellular nutrients required to support T cell activation.
Structural analyses, functional characterizations and computational studies reveal the ion-translocation pathway, ion-binding sites and key residues for transport activity.
This study reveals the assembly principles of a thermostable T=4 shell topology and its catalytic ferroxidase cargo and show interactions underlying cargo-shell co-assembly.
