Keynote Lectures Detailed Information Print E-mail

Kim Nasmyth

University of Oxford, UK

Kim Nasmyth joined the Department of Biochemistry in January 2006 holding the position of the Whitley Chair and on 1st October 2006 took over the position of Head of the Department. He was a Ph.D. student in Mitchison's lab in Edinburgh (1974-77), a post doc in Seattle Washington (1978-1980), a Robertson research fellow at Cold Spring for molecular biology in Cambridge (1982-87) before moving to the Research Institute of Molecular Pathology (I.M.P.), where he was a senior scientist from 1988-1997 and Director from 1997-2006. He is on the scientific advisory boards of numerous research institutes and companies and has been heavily involved in establishing a new exhibition about Mendel's life and work at St Thomas's monastery in Brno. He has recently had an important role in establishing the Institute of Molecular Biotechnology (IMBA) next to the IMP. His scientific work has addressed the mechanisms by which genes are turned on and off during development, how DNA replication is controlled, and how chromosomes ensure their segregation during mitosis and meiosis. It has been recognised by several awards most recently the Gairdner International Award (2007) for a series of discoveries pinpointing the novel mechanisms in cell division that are essential to life. Also, the Boveri award for Molecular Cancer Genetics (2003), the Croonian lecture/Medal of the Royal Society (2002), the Austrian Wittgenstein prize (1999), the Louis-Jeantet prize for Medicine (1997), the Unilever Science prize (1996), and the FEBS Silver Medal (1995). He is a fellow of the Royal Society (1989), a member of the Austrian Academy of Sciences (1999), and a foreign honorary member of the American Academy of Arts and Sciences (1999).


Title & synopsis
How do cells hold sister chromatids together during mitosis and meiosis?

Synopsis to follow

Rudolf Jaenisch

Whitehead Institute, US


Rudolf Jaenisch is a Founding Member of the Whitehead Institute for Biomedical Research and a Professor of Biology at MIT. In 2005 he established the Human Stem Cell Facility at the Whitehead.

He is a pioneer in making transgenic mice, leading to some important advances in understanding cancer, neurological and connective tissue diseases, and developmental abnormalities. These mice have been used to explore basic questions such as the role of DNA modification, genomic imprinting, X chromosome inactivation, nuclear cloning, and, most recently, the nature of stem cells. The Jaenisch laboratory has used therapeutic cloning and gene therapy to rescue mice having a genetic defect and more recently, using a technique for turning skin cells into stem cells, they have cured mice of sickle cell anemia -- the first direct proof that these easily obtained cells can reverse an inherited disease.

Title & synopsis
Stem cells, pluripotency & nuclear reprogramming

One of the key issues raised by nuclear cloning is the question of genomic reprogramming, i.e. the mechanism of resetting the epigenetic modifications that are characteristics of the adult donor nucleus to ones that are appropriate for an embryonic cell. The mechanisms by which embryonic stem (ES) cells self-renew while maintaining the ability to differentiate into virtually all adult cell types are not well understood. Major progress has been achieved to understand the molecular circuitry of pluripotency and self-renewal. This information provides crucial insights into mechanisms by which pluripotent cells may be stimulated to differentiate into different cell types or by which somatic cells might be reprogrammed back to the pluripotent state by exposure of the somatic nucleus to the egg cytoplasm. The recent demonstration of in vitro reprogramming using transduction of 4 transcription factors by Yamanaka and colleagues represents a major advance in the field. Major questions regarding the mechanism of in vitro reprogramming need to be understood and will be one focus of the talk. Also, our progress in using iPS cells for therapy and for the study of complex human will be summarised.

sponsored by


Louis-Jeantet Prize Lectures



University of Basel, CH


Michael Hall received his Ph.D. from Harvard University in 1981, and was a postdoctoral fellow at the Pasteur Institute (Paris, France) and the University of California, San Francisco. He joined the Biozentrum of the University of Basel (Switzerland) in 1987 where he is currently Professor and Chair of Biochemistry. He has a longstanding interest in signal transduction, in yeast and mammals, and is a world leader in the fields of TOR signaling and cell growth control. He discovered TOR (Target of Rapamycin) and subsequently elucidated its role as a central controller of cell growth. TOR is a conserved, nutrient- and insulin-activated protein kinase. The discovery of TOR led to a fundamental change in how one thinks of cell growth. It is not a spontaneous process that just happens when building blocks (nutrients) are available, but rather a highly regulated, plastic process controlled by TOR-dependent signaling pathways. As a central controller of cell growth, TOR plays a key role in development and aging, and is implicated in disorders such as cancer, cardiovascular disease, obesity, and diabetes.

Title & synopsis
TOR signalling & the control of cell & organism growth

TOR (target of rapamycin) is a highly conserved serine/threonine kinase that controls cell growth and metabolism in response to nutrients, growth factors, cellular energy, and stress. TOR was originally discovered in yeast but is conserved in all eukaryotes including plants, worms, flies, and mammals. The discovery of TOR led to a fundamental change in how one thinks of cell growth. It is not a spontaneous process that just happens when building blocks (nutrients) are available, but rather a highly regulated, plastic process controlled by TOR-dependent signaling pathways. TOR is found in two structurally and functionally distinct multiprotein complexes, TORC1 and TORC2. The two TOR complexes, like TOR itself, are highly conserved. Thus, the two TOR complexes constitute an ancestral signaling network conserved throughout eukaryotic evolution to control the fundamental process of cell growth. As a central controller of cell growth, TOR plays a key role in development and aging. The physiological consequences of mTORC1 dysregulation suggest that inhibitors of mTOR may be useful in the treatment of age-related diseases such as cancer, cardiovascular disease, and metabolic disorders.
While the role of TOR in controlling growth of single cells is relatively well understood, the challenge now is to understand the role of TOR signaling in coordinating and integrating overall body growth (and aging) in multicellular organisms. This will require elucidating the role of TOR signaling in individual tissues. Data on the role of mTORC1 and mTORC2 in specific tissues will be presented.


Peter Ratcliffe

University of Oxford, UK


Peter Ratcliffe is Nuffield Professor and head of the Department of Medicine at the University of Oxford. He studied medicine at Gonville & Caius College, Cambridge and St. Batholomew’s Hospital, London before moving to Oxford to complete specialist training as a Nephrologist. He became interested in the physiology of the renal circulation and its effects of intra-renal oxygenation before re-training in molecular biology in order to study the biology of hypoxia at the cellular level. In 1990 he obtained a Senior Fellowship from the Wellcome Trust to study mechanisms of cellular oxygen sensing and gene regulation in mammalian cells and has since directed the hypoxia biology laboratory at Oxford, now situated in the Henry Wellcome Building for Molecular Physiology. He is a fellow of the Royal Society, member of EMBO and a foreign honorary member of the American Academy of Arts and Sciences.

Title & synopsis
Signalling oxygen levels in cells


Hypoxia signalling pathways regulate an extensive range of genes via the post-translational hydroxylation of a transcription factor termed hypoxia inducible factor (HIF). HIF is an α/β heterodimeric complex that binds hypoxia response elements at target genes involved in angiogenesis, energy metabolism, matrix metabolism, pH regulation, cell survival and proliferation decisions. HIF prolyl hydroxylation governs proteolytic regulation of HIF whereas HIF asparaginyl hydroxylation modulates interaction with transcriptional co-activators. These hydroxylations are catalysed by a set of non-haem Fe(II) 2-oxoglutarate (2OG) dependent dioxygenases. During catalysis, the splitting of dioxygen is coupled to the hydroxylation of HIF and the oxidative decarboxylation of 2-oxoglutarate. Hydroxylation at two prolyl residues within the central ‘degradation domain’ of HIF-α determines binding to the von Hippel-Lindau (pVHL) E3 ligase complex, thus directing HIF-α polypeptides for proteolytic destruction by the ubiquitin/proteasome pathway. Since the HIF hydroxylases have an absolute requirement for dioxygen this process is suppressed in hypoxia allowing the HIF-α to escape destruction and activate transcription. Recent studies also suggest that the availability of other co-substrates and co-factors including Fe (II), ascorbate, and 2-oxoglutarate, modulate the rate of hydroxylation allowing the reaction to integrate, hypoxic, redox, and metabolic signals. Recent studies have also indicated that post-translational hydroxylation of intracellular proteins extends beyond the HIF pathway. The HIF asparaginyl hydroxylase hydroxylates asparaginyl residues within the consensus repeat in a wide range ankyrin repeat domain (ARD) containing proteins, indicating that post-translational hydroxylation of intracellular proteins is more widespread than has previously been considered. Potential functions of ARD hydroxylation will be discussed.