When a cellular protein has done its job or lost its utility, it should be removed, recycled, or remodeled. These tasks are performed by members of the ubiquitous family of AAA ATPases (ATPases associated with diverse cellular activities) that convert the energy of ATP hydrolysis into mechanical forces that can unfold protein aggregates, degrade unwanted proteins, and remodel protein complexes. Continue reading → Structures and Mechanisms of Protein Remodeling Machines
The kidney senses and responds to physiological changes, such as pH, ionic strength, pressure, and nutrient levels. Sensing is mediated by a coupled sensor/ion channel complex called the Polycystic Kidney Disease Channel, which is composed of two subunits, the PKD1 (the primary sensor) and PKD2 (the channel). Continue reading → Structure and Function of the Polycystic Kidney Disease Channel
Biochemical and structural studies from Bass, Shen, Iwasa, and colleagues revealed how Dicer-2, an RNA processing, and antiviral defense enzyme, distinguishes and differentially processes double-stranded RNA (dsRNA) substrates by sensing the unique chemistry at their termini. Continue reading → Identifying RNAs from Invading Viruses
Our lab is motivated by a common cause to understand how life works at the atomic scale. All cells depend on a healthy balance of protein synthesis, folding, trafficking, and turnover. We specialize in using cryo-EM to visualize these processes. Our efforts to resolve mechanisms underlying protein homeostasis will teach us the principles of how cells stay healthy and how the breakdown of these processes cause human disease.