Philip Stork earned his M.D. at Columbia University in 1984 and went on to a residency in Pathology at Harvard Medical School and a fellowship at Tufts-New England Medical Center. He became an assistant professor in the Department of Pathology at Tufts in 1988. Stork was appointed as an assistant scientist at the Vollum Institute in 1990, was promoted to scientist in 1997 and senior scientist in 2005. He holds a joint appointment in the Department of Cell, Developmental and Cancer Biology in OHSU's School of Medicine.
Dr. Stork and his colleagues use molecular and biochemical approaches to understand how hormones and growth factors convey signals from the outside of a cell to the nucleus to induce cellular responses. Over the past few years, the Stork laboratory has tried to understand a fundamental question in the field of signal transduction: how can qualitative changes in the magnitude and duration of a single signaling cascade lead to qualitative changes in the cellular response?
Areas of interest
- small G proteins
- MAP kinase
- M.S., Stanford University, Stanford California 1978
- B.S., Harvard University, Cambridge Massachusetts 1977
- M.D., Columbia University, New York New York 1984
Memberships and associations
- Editorial Board, Molecular Cell Biology, 2008-2020
Takahashi M, Li Y, Dillon TJ, Stork PJ. (2017) Phosphorylation of Rap1 by cAMP-dependent protein pinase (PKA) creates a binding site for KSR to sustain ERK activation by cAMP. J. Biol. Chem. 292(4): 1449-1461.
Li Y, Dillon TJ, Takahashi M, Earley KT, Stork PJ. (2016) PKA-independent Ras activation cooperates with Rap1 to mediate activation of ERKs by cAMP. J. Biol. Chem. 291(41): 21584-21595.
Hu J, Stites EC, Yu H, Germino EA, Meharena HS, Stork PJ, Kornev AP, Taylor SS, Shaw AS. (2013) Allosteric activation of functionally asymmetric RAF kinase dimers. Cell 154:1036-1046.
Takahashi M, Dillon TJ, Liu C, Kariya Y, Wang Z, Stork PJ. (2013) PKA-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration. J. Biol. Chem. 288:27712-27723.