Professor of Biological Engineering
"The focus of research in our laboratory is the identification of protein phosphorylation events regulating signal transduction cascades associated with cancer and other biological processes. With our mass spectrometry-based technology, identification of protein phosphorylation occurs on a global scale, allowing for mapping of complex signal transduction cascades in a variety of biological samples."
Forest White is a professor of biological engineering at MIT, a member of the Koch Institute and a member of the MIT Center for Precision Cancer Medicine. He earned his bachelor’s degree in chemistry from Framingham State College in 1993, and a doctorate in analytical chemistry from Florida State University in 1997. Following postdoctoral research in bioanalytical chemistry in the laboratory of Donald Hunt at the University of Virginia, he joined MDS Proteomics, Inc. as a research scientist working his way up to group leader. Forest White joined MIT in 2003 as an assistant professor and was awarded the Mitsui Career Development Professorship (2005-2008). In 2010, he received the Ruth and Joel Spira Award for Excellence in Teaching.
Forest White's research seeks to develop a detailed understanding of the signaling networks that allow cells to respond to external stimuli. Receptors on the surface of cells interact with molecules, or ligands, in the extracellular environment, and the receptors must then communicate information to the inside of a cell. The most common way to transmit these signals is by covalent modification of target proteins within the signaling pathway, most often adding a phosphate group (phosphorylation) or removing a phosphate group. Phosphorylation is performed by enzymes called “kinases,” and dephosphorylation is performed by “phosphatases.” Both failure and overactivity of kinases and phosphatases can lead to human diseases such as cancer, diabetes, and autoimmune disorders. Most studies of these signaling networks have been constrained by the need to focus on a single enzyme or phosphorylation site. White has developed a new methodology, taking advantage of mass spectrometry, to examine large portions of the networks at once, while still being able to examine individual sites. White is using this technology to study the mechanisms underlying the progression of breast, prostate, brain, and lung cancers. The goal of White's research is to deepen the understanding of how cells respond to their environment, as well as to develop new ways to detect malfunctions in the cellular networks and develop corresponding therapies.
Johnson H, White FM. 2018. Quantitative Analysis of Tyrosine Kinase Signaling Across Differentially Embedded Human Glioblastoma Tumors. Methods Mol Biol 1711: 149–164.
Emdal KB, Dittmann A, Reddy RJ, Lescarbeau RS, Moores SL, Laquerre S, White FM. 2017. Characterization of In Vivo Resistance to Osimertinib and JNJ-61186372, an EGFR/Met Bispecific Antibody, Reveals Unique and Consensus Mechanisms of Resistance. Mol Cancer Ther 16: 2572–2585.
Reddy RJ, Gajadhar AS, Swenson EJ, Rothenberg DA, Curran TG, White FM. 2016. Early signaling dynamics of the epidermal growth factor receptor. Proc Natl Acad Sci USA 113: 3114–3119.
Lescarbeau RS, Lei L, Bakken KK, Sims PA, Sarkaria JN, Canoll P, White FM. 2016. Quantitative Phosphoproteomics Reveals Wee1 Kinase as a Therapeutic Target in a Model of Proneural Glioblastoma. Mol Cancer Ther 15: 1332–1343.
Gajadhar AS, Johnson H, Slebos RJC, Shaddox K, Wiles K, Washington MK, Herline AJ, Levine DA, Liebler DC, White FM, et al. 2015. Phosphotyrosine signaling analysis in human tumors is confounded by systemic ischemia-driven artifacts and intra-specimen heterogeneity. Cancer Res 75: 1495–1503.
Curran TG, Zhang Y, Ma DJ, Sarkaria JN, White FM. 2015. MARQUIS: a multiplex method for absolute quantification of peptides and posttranslational modifications. Nat Commun 6: 5924.
Arneja A, Johnson H, Gabrovsek L, Lauffenburger DA, White FM. 2014. Qualitatively different T cell phenotypic responses to IL-2 versus IL-15 are unified by identical dependences on receptor signal strength and duration. J Immunol 192: 123–135.
Johnson H, Del Rosario AM, Bryson BD, Schroeder MA, Sarkaria JN, White FM. 2012. Molecular characterization of EGFR and EGFRvIII signaling networks in human glioblastoma tumor xenografts. Mol Cell Proteomics 11: 1724–1740.
Carlson SM, Chouinard CR, Labadorf A, Lam CJ, Schmelzle K, Fraenkel E, White FM. 2011. Large-scale discovery of ERK2 substrates identifies ERK-mediated transcriptional regulation by ETV3. Sci Signal 4: rs11.
Huang PH, Miraldi ER, Xu AM, Kundukulam VA, Del Rosario AM, Flynn RA, Cavenee WK, Furnari FB, White FM. 2010. Phosphotyrosine signaling analysis of site-specific mutations on EGFRvIII identifies determinants governing glioblastoma cell growth. Mol Biosyst 6: 1227–1237.