Vishva M. Dixit

Genentech


Election Year: 2013
Primary Section: 41, Medical Genetics, Hematology, and Oncology
Secondary Section: 43, Immunology and Inflammation
Membership Type: Member

Biosketch

Vishva M. Dixit is Vice President of Discovery Research at Genentech. A pathologist by training, he has studied molecular mechanisms that underlie cell death and inflammatory signaling.  In particular, he is known for the breakthrough discovery that a cysteine protease (caspase) is a component of the death receptor-induced apoptotic pathway - a finding that allowed his laboratory and others to then elucidate the entire 'death cascade'.  Vishva was born in Kenya in 1956 and became a US citizen in 1987.  He went to medical school at the University of Nairobi and, after clinical work at the Kenyatta National Hospital, pursued a residency in Pathology at Washington University in St. Louis.  He joined the Department of Pathology at the University of Michigan in 1986 as an Assistant Professor.  After rising through ranks to Professor, he left in 1997 to join Genentech as Director of Oncology.

Research Interests

Vishva Dixit studies the molecular events required for programmed cell death and pro-inflammatory signaling.  His laboratory was among the first to:  (i) Show that a cysteine protease (now termed caspase) was a component of the death receptor-induced apoptotic pathway.   (ii) Discover the death domain-containing adapter protein (FADD), which is the key conduit for the flow of death signals from death receptors to the cell's interior.  (iii) Demonstrate that death receptors signal by a novel mechanism of recruiting and activating a death protease (caspase-8).  (iv) Identify the mammalian death protease equivalent to the CED3 protein in worms (caspase-3) as well as other pro-apoptotic caspases including caspases 6, 7 and 9.  (v) Show that the death-domain containing molecule MyD88 was a key adaptor in innate immune signaling.  (vi) Discover two ancient families of caspase-related proteins, the paracaspases and metacaspases, with the former playing a central role in lymphoma.  (vii) Identify the existence of an ubiquitin editor (A20) and the phenomenon of ubiquitin editing, which is a process of fundamental importance to the regulation of death and cytokine receptor signaling.  (viii) Discover the non-canonical inflammasome pathway that responds to the presence of intracellular LPS independent of toll-like receptors.

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