Rati Verma
Amgen, Thousand Oaks, California, USA
I received my Ph.D. in Biochemistry from Rutgers University. My first postdoctoral mentor was Arthur Pardee at the Dana Farber Cancer Institute, Harvard Medical School who introduced me to the intricacies of the cell cycle. Subsequently, at California Institute of Technology, Ray Deshaies opened up the field of ubiquitin-dependent proteolysis for me and I had the great fortune of participating in the discovery of the SCF ubiquitin ligase. Reconstituting degradation of a Cdk inhibitor I developed a one-step affinity purification of the 2.5 MDa proteasomal complex that was active in degrading the SCF-ubiquitinated substrate. I then went on to show that the proteasomal subunit Rpn11 was the essential deubiquitinase of the proteasome that removes the ubiquitin chain en bloc prior to substrate degradation. In a 17-year collaboration with Ray as a Howard Hughes Research Specialist, I identified intrinsic ubiquitin receptors of the proteasome as well as shuttle receptors such as the ATPase p97. This essential ATPase, together with its adaptor Vms1, plays a major role in maintaining cellular homeostasis by releasing nascent peptides on stalled ribosomes and recycling subunits. Currently, I am a Principal Scientist in Precision Oncology at Amgen where I lead a high performing team in both discovery stage as well as preclinical oncology programs.
I received my Ph.D. in Biochemistry from Rutgers University. My first postdoctoral mentor was Arthur Pardee at the Dana Farber Cancer Institute, Harvard Medical School who introduced me to the intricacies of the cell cycle. Subsequently, at California Institute of Technology, Ray Deshaies opened up the field of ubiquitin-dependent proteolysis for me and I had the great fortune of participating in the discovery of the SCF ubiquitin ligase. Reconstituting degradation of a Cdk inhibitor I developed a one-step affinity purification of the 2.5 MDa proteasomal complex that was active in degrading the SCF-ubiquitinated substrate. I then went on to show that the proteasomal subunit Rpn11 was the essential deubiquitinase of the proteasome that removes the ubiquitin chain en bloc prior to substrate degradation. In a 17-year collaboration with Ray as a Howard Hughes Research Specialist, I identified intrinsic ubiquitin receptors of the proteasome as well as shuttle receptors such as the ATPase p97. This essential ATPase, together with its adaptor Vms1, plays a major role in maintaining cellular homeostasis by releasing nascent peptides on stalled ribosomes and recycling subunits. Currently, I am a Principal Scientist in Precision Oncology at Amgen where I lead a high performing team in both discovery stage as well as preclinical oncology programs.
