Friday Evening Lecture Series – Porter Lecture – Richard Hynes – Massachusetts Institute of Technology; HHMI “The Intelligent Glue that Holds us Together”

Date(s) - 07/25/2014
8:00 pm - 9:00 pm
Lillie Auditorium

Friday Evening Lecture SeriesPorter Lecture – “The Intelligent Glue that Holds us Together”
Richard Hynes, Massachusetts Institute of Technology; HHMI
July 25, 2014, 8:00 PM, Lillie Auditorium

Introduction by Dr. Joan Ruderman, President and Director, MBL

Richard HynesLecture Abstract:
Fundamental to the evolution and physiology of metazoa is the fact that the cells of the body are organized into tissues by specific adhesions between individual cells and between cells and the extracellular matrix (ECM), a complex network of proteins providing structure to tissues.  Those adhesions rely on specific cell surface receptor proteins.  Thus, any given cell has specific receptors that maintain its adhesion to its neighbors ensuring coherent layers of cells and other receptors that ensure its adhesion to the underlying ECM so that the cell layers do not detach.  Furthermore, adhesion receptors transmit signals into and out of cells controlling their proliferation, survival and differentiation.  Cells also use adhesion receptors to direct cell migration during normal development and physiological processes such as immune cell traffic in the body and blood platelet adhesion preventing bleeding.  When everything is working as it should, these receptors ensure appropriate adhesion – not too much and not too little and specific for the correct sites.  However, in disease, too little adhesion can cause bleeding or immune deficiency and too much can cause thrombosis, inflammation, autoimmune disease or skin blistering.  In cancer, aberrant adhesion is involved in the anomalous proliferation of cancer cells and in their invasion and metastasis to inappropriate locations.  The receptors and ECM proteins underlying these highly regulated adhesion phenomena are ancient and complex proteins whose structure and function has become understood over recent decades providing insights into how we are held together, how that can go wrong and how we can exploit those insights.

Dr. Richard Hynes was educated at Cambridge University (B.A, M.A) and MIT (Ph.D.).  He 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 Cancer Center for 10 years.  He is a Fellow of the Royal Society (FRS) of London and a Member of the US National Academy of Sciences, the Institute of Medicine and the American Academy of Arts and Sciences.

Dr. Hynes was born in Nairobi, Kenya and grew up in Liverpool, England. He did his undergraduate work at Trinity College in Cambridge, UK, and his Ph.D. at MIT with Paul Gross, separating different cell types from early sea urchin embryos and studying the complexity of their RNA sequences. He then returned to the UK as a postdoctoral fellow at the 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 that was noticeably absent on cancer cells. Dr. Hynes then went back to become an Assistant Professor in the Cancer Center and Biology Department at MIT in 1975, where he continued to work out the biology of fibronectin, the discovery of which set into motion a string of studies that has helped to establish cell adhesion as its own field of investigation. He showed that the extracellular matrix was connected across the membrane to the actin cytoskeleton.  Dr. Hynes’s studies also contributed to the discovery and subsequent cloning of  integrins, a family of protein receptors that gives cells their stickiness by binding with fibronectin and other cell adhesion molecules. By forming a physical link between the extracellular environment and the cell’s interior, integrins help to control cell shape and movement as well as accurate cell adhesion and control cell behavior through the transmission of signals into and out of cells.

The Hynes laboratory continues to study actively the molecular and cellular basis of cell adhesion and its involvement in embryonic development, physiology and pathology (inflammation, thrombosis and cancer). Particular interests focus on cell-matrix adhesion and on the adhesion of cells in the vasculature, both involving integrin adhesion receptors and their ligands.  Current emphases are on vascular development and cancer metastasis with a focus on the contributions of platelets and extracellular matrix.  The laboratory uses mouse models of human diseases and applies cellular and molecular approaches to decipher the mechanisms underlying phenomena revealed in those mouse models. By studying the way cells stick together and migrate in both healthy and disease states, Dr. Hynes hopes his research will lay the foundation for scientists to develop new therapies for adhesion-related disorders.

Dr. Hynes has received numerous awards in recognition of his research on extracellular matrix, integrins and cell adhesion, including the Gairdner International Award, the Pasarow Award and the E.B. Wilson medal, the highest award given by the American Society for Cell Biology.  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, UK.


About the Porter Lecture:
The annual Porter Lecture is held in honor of Dr. Keith Roberts Porter, a former Director of the MBL considered by many to be the “Father” of the field of cell biology. It is sponsored by the Keith R. Porter Endowment whose goal is to support communication and education in cell biology.


Share ThisShare on FacebookTweet about this on TwitterPin on PinterestShare on Google+Email this to someonePrint this page