Richard O. Hynes, PhD, FRS

Richard O. Hynes, PhD, FRS
Daniel K. Ludwig Professor for Cancer Research at the Koch Institute and Department of Biology
​Massachusetts Institute of Technology
Cambridge, Massachusetts

Richard Hynes is the Daniel K. Ludwig Professor for Cancer Research at the Koch Institute and Department of Biology at MIT, Investigator of the Howard Hughes Medical Institute and Senior Associate Member of the Broad Institute.  He was formerly Associate Head and then Head of the Biology department and was Director of the MIT Center for Cancer Research for 10 years.  He is a Fellow of the Royal Society (FRS) of London and a Member of the US National Academy of Sciences, National Academy of Medicine, the American Academy of Arts and Sciences and the AACR Academy.

Dr. Hynes was born in Nairobi, Kenya and grew up in Liverpool, England. He did his undergraduate work in Biochemistry at Trinity College, Cambridge, UK, and his PhD in Biology at MIT working with Paul Gross, on the segregation of maternal mRNAs in early sea urchin embryos.  He then returned to the UK as a postdoctoral fellow at Imperial Cancer Research Fund in London.  By investigating the molecular changes on cell surfaces that distinguish cancer cells from normal cells, he discovered fibronectin, a cell adhesion protein present on normal cells but noticeably absent on cancer cells.

Dr. Hynes returned to MIT in 1975 as an Assistant Professor and one of the founding members of the MIT Cancer Center.  There he continued to work out the biology of fibronectin, showing that fibronectin affects cellular adhesion, migration, morphology and cytoskeleton and that fibronectin and actin fibrils coalign across the cell surface.  These discoveries established the extracellular matrix (ECM), previously viewed largely as a structural entity, as having a vital role in controlling cell adhesion, morphology and migration.  Dr. Hynes also made major contributions to the discovery and first cloning of integrins, a family of protein receptors that bind fibronectin and other cell adhesion molecules and form transmembrane links to the cytoskeleton.  He and his colleagues also discovered the activation of FAK through integrins, thereby establishing integrins as true signaling receptors.  The Hynes laboratory cloned and analyzed many of the key molecules involved in cell adhesion (e.g., fibronectin, thrombospondin, integrins, talin, plakoglobin) and generated the first knockout mice lacking adhesion molecules (fibronectin, a5 integrin, P-selectin) and subsequently many others (e.g., other integrins and selectins, cadherins and multiple ECM proteins) and exploited them to dissect the roles of cell adhesion in normal development, hemostasis, thrombosis, inflammation, angiogenesis and cancer).  Most recently Hynes has focused on metastasis, particularly the contributions of platelet-tumor cell interactions and ECM in promoting metastasis and has developed methods for systematic characterization and analysis of ECM changes in vivo. 

Dr. Hynes' work over the past 40 years has played a major role in establishing the molecular basis of cell adhesion and its many diverse and important effects on cells both in vitro and in vivo.  This molecular understanding has formed the basis for development of antibodies and drugs that modulate cell adhesion and are in clinical use against thrombosis, inflammation and autoimmune diseases and under investigation for efficacy against cancers.  Molecular understanding of cell-ECM interactions is also being exploited in tissue engineering and regenerative medicine.

Dr. Hynes has received numerous awards including the Gairdner International Award, a Guggenheim Fellowship, the Pasarow Award and the E.B. Wilson medal of the American Society for Cell Biology, in recognition of his research on extracellular matrix, integrins and cell adhesion.  He has served as President of the American Society for Cell Biology, chaired the NAS committees that established Guidelines for Human Embryonic Stem Cell Research and is currently a Governor of the Wellcome Trust.