53rd Rosenstiel Award awarded to Wolfgang Baumeister

The 53rd Rosenstiel Award for Distinguished Work in Basic Medical Research has been awarded to Wolfgang Baumeister for his pioneering work in the Development of cryo-electron tomography and for his insights into the structures and functions of the protein quality control machinery.

Dr. Baumeister’s visionary drive to find a way to study molecular machines in their native contexts has made it possible to study cells in a close-to-living state in three dimensions with resolution approaching the sub-nanometer range. This is a revolutionary advance that will allow us to understand the cellular milieu in a way never before possible. In particular, his lab has explored in near-atomic detail the proteasome complex that is responsible for the targeted degradation of proteins, and has led the way to the study of other macromolecular assemblies and their arrangement within the cell.

Professor Baumeister is Director Emeritus and Scientific Member of the Max-Planck Institute in Martinsreid, Germany. His laboratory has been at the forefront of the identification and structural analysis of the molecular machinery involved in both the proper folding and the degradation of proteins. Insights from his laboratory about a novel structural motif in some proteases has led to the development of inhibitors that block the proliferation of several cancers. More recently, his ability to locate precisely individual protein structures has made it possible to begin the description of the “molecular sociology” of proteins in specific subcellular environments such as neurons. Professor Baumeister is a Member of the German Academy of Sciences Leopoldina, a Foreign Honorary Fellow of the American Academy of Arts and Sciences, and a Foreign Member of the U.S. National Academy of Sciences. He is a recipient of many awards, including the Alexander Hollander Award in Biophysics and the Louis-Jeantet Prize for Medicine. He is a member of the Chan Zuckerberg Initiative Steering Committee and Editor-in-Chief of Biochemical and Biophysical Research Communications.

Dr. Baumeister will present his Rosenstiel Award lecture at Brandeis on April 18, 2024.

The Rosenstiel Award has had a distinguished record of identifying and honoring pioneering scientists who subsequently have been honored with the Lasker and Nobel Prizes. In 2022, the Rosenstiel Award was presented to Christine Holt and Erin Schuman. In 2021, Robert Singer was honored for his studies of the ways messenger RNAs are transcribed and transported to specific locations in the cytoplasm of cells, often far from the nucleus. In 2020, the Rosenstiel Award was the first of now many prizes conferred on Katalin Karikó and Drew Weismann for their pioneering work in the development of RNA vaccines. Karikó and Weismann received the 2023 Nobel Prize in Physiology or Medicine. In 2019, David Julius and Ardem Patapoutian were honored for their identification and characterization of ion channels that enable the perception of touch, temperature and pain. Julius and Patapoutian were the 2021 Nobel laureates in Physiology and Medicine. In 2018, Stephen C. Harrison was honored for his elucidation of protein structures using x-ray crystallography. In 2017, Titia de Lange was named for her pioneering work on how cells preserve the integrity of their chromosomes. In 2016, Susan Lindquist was cited for her work on the association of protein aggregation and neurological disease. In 2015, Yoshinori Ohsumi was the recipient, for his description of protein degradation through the process of autophagy. Ohsumi was awarded the Nobel Prize in 2016. Forty of 95 Rosenstiel Award winners have subsequently been awarded the Nobel Prize in Medicine or Physiology or in Chemistry.

A full list of awardees can be found on the Rosenstiel Award website.

2022 Rosenstiel Award Recipients Receive 2023 Brain Prize

Christine Holt (left) and Erin Schuman (right)

Christine Holt, Professor emerita of Developmental Neuroscience at the University of Cambridge and Erin Schuman, Professor of Neurobiology at the Max Planck Institute for Brain Research have been named the 2023 Brain Prize Winners. Both Holt and Schuman received the Rosenstiel Award for Distinguished Work in Basic Medical Research award in 2022. Michael Greenberg from the Harvard Medical School also received Brain Prize. The Brain Prize is an international scientific award that honors scientists for their outstanding contribution to neuroscience.

The Lunkbeck Foundation noted that the 2023 recipients of the Brain Prize have “made ground-breaking discoveries by showing how the synthesis of new proteins is triggered in different parts of the neuron, thereby guiding brain development and plasticity in ways that impact our behaviour for a lifetime.”

The following is the program and speakers for the Brain Prize Webinar Series that will be held from October 25, 2023 through March 27, 2024. The series is online and free to attend.

Leslie Griffith, Nancy Lurie Marks Professor of Neuroscience and the Director of the Volen National Center for Complex Systems will be participating in this series on December 7, 2023.

HMS Professor Stephen Harrison to Receive 48th Rosenstiel Award

Prof. Stephen C. Harrison will receive the 48th Rosenstiel Award for Distinguished Work in Basic Medical Research on March 25, 2019. He is being honored for his studies of protein structure using X-ray crystallography.  His work has ranged from the landmark elucidation of the structure of viruses, to understanding the recognition of DNA sequences by transcription factors, to the regulation of protein kinases implicated in cancer. The event will take place from 4:00 to 5:00 PM on Monday, March 25 in Gerstenzang 123.

Harrison is the Giovanni Armenise-Harvard Professor of Basic Medical Sciences and Director of the Center for Molecular and Cellular Dynamics at the Harvard Medical School.  He is also Head of the Laboratory of Molecular Medicine at Boston Children’s Hospital and an Investigator of the Howard Hughes Medical Institute.   He has been elected a member of the US National Academy of Sciences, the American Academy of Arts and Sciences,  the American Philosophical Society; he is a foreign member of the Royal Society and the European Molecular Biology Organization.

Dr. Harrison’s initial studies of virus structure provided an understanding of how viruses invade cells and how virus particles are assembled.  He has extended his work to reveal the structures of many viruses, including influenza, HIV, ebola and dengue.  Knowledge of these structures is guiding the development of new vaccines against these viruses.  Moreover, the methodology that he and his colleagues developed to visualize virus structure has made it possible to learn about the molecular architecture of other very large assemblies of proteins.

Harrison’s lab has also revealed the ways that proteins recognize specific DNA sequences to regulate gene expression.  More recently his lab has been exploring the complex structure of the many proteins that are assembled in the kinetochore, which anchors the centromeres of chromosomes to microtubules, to permit their proper segregation in mitosis.

“Steve Harrison has done much more than giving us astonishing pictures of proteins at the atomic level; he has used this structural information to show us how these proteins perform their precise functions,” said James E. Haber, Director of the Rosenstiel Center for Basic Medical Sciences.

The Rosenstiel Award has had a distinguished record of identifying and honoring pioneering scientists who subsequently have been honored with the Lasker and Nobel Prizes. Awards are given to scientists for recent discoveries of particular originality and importance to basic medical research.

View full list of awardees.

 

 

Titia de Lange to receive 47th Rosenstiel Award

Professor Titia de Lange

The 47th Lewis S. Rosenstiel Award for Distinguished Work in Basic Medical Research has been awarded to Professor Titia de Lange of Rockefeller University for her studies on the protection of chromosome ends (telomeres) from degradation and rearrangement. Professor de Lange will receive the award on April 12, 2018 at Brandeis University where de Lange will present a public lecture.

Dr. de Lange’s laboratory identified and characterized the roles of proteins that compose the shelterin complex, which binds specifically to the special telomeric DNA sequences and maintains the stability of these ends.  Dr. de Lange’s work has shown that the shelterin complex and the unusual telomere-loop structure of telomere DNA prevent these ends from being detected as broken chromosome ends and thus protect telomeres from being degraded and rearranged as are the ends at chromosome breaks.  De Lange’s work has further shown that disabling different components of shelterin triggers different cellular alarms designed to detect broken and degraded DNA ends and leads to lethal chromosome rearrangements such as the fusion of chromosomes.  In addition, her lab has gained critical insights into the mechanisms of cellular response to the presence of DNA damage and recently has defined processes that lead to massive chromosome rearrangements (chromothripsis) associated with many human cancers.

She is the Leon Hess Professor and director of the Anderson Center for Cancer Research at Rockefeller University, as well as an American Cancer Society Research Professor.  Her honors include: the Life Sciences Breakthrough Prize, the Rosalind E. Franklin Award from the National Cancer Institute, the Vilcek Prize in Biomedical Sciences, election as a foreign member of the US National Academy of Sciences and as Fellow of the American Academy of Arts and Sciences.

The Rosenstiel Award has had a distinguished record of identifying and honoring pioneering scientists who subsequently have been honored with the Lasker and Nobel Prizes.  Professor de Lange joins a long list of past awardees.

Rosenstiel Award lectures on Mar 22 to honor Susan Lindquist

James Haber, Director of the Rosenstiel Center, writes:

The 46th annual Rosenstiel Award for Distinguished Work in Basic Medical Research was awarded last October to Susan Lindquist (MIT), one of the most inventive and influential life scientists of our generation.  Sue tragically passed away a few weeks thereafter; in her honor we have arranged a symposium to celebrate her lab’s great legacy.  The Award talks will be held in next Wednesday, March 22, in Gerstenzang 123 from 3:30 PM to 5:30 PM, followed by a reception open to all in the Shapiro Science Center atrium.  We hope you will all come to honor Sue Lindquist and to be edified by the excellent work carried out by her former colleagues.

Angelika Amon  (Massachusetts Institute of Technology)
“The Remarkable Scientific Life of Susan Lindquist”

Leah Cowen (University of Toronto)
“Harnessing Evolution to Thwart Microbial Drug Resistance and Treat Infectious Disease”

Daniel Jarosz (Stanford University)
“Remembering the Past: A New Form of Protein-Based Inheritance”

Sandro Santagata (Brigham and Women’s Hospital)
“Heat Shock Factor (HSF1): A Powerful Driver of Malignancy”

 

Yoshinori Ohsumi to Receive Rosenstiel Award Wednesday, April 6

Biologist Yoshinori Ohsumi will receive the 45^th Rosenstiel Award for Distinguished Work in Biomedical Science this Wednesday, April 6^th at 4:00 pm in Gerstenzang 123. At that time, he will present a lecture titled, “Lessons from yeast: Cellular recycling system, autophagy”.

Ohsumi is a cell biologist and professor at the Tokyo Institute of Technology’s Frontier Research Center in Japan. He is one of leading experts in the world on autophagy, a process that allows for the degradation and recycling of cellular components. The Rosenstiel Award is being given to Ohsumi in recognition of his pioneering discoveries in autophagy.

Learn more about Professor Ohsumi and his research at BrandeisNow.

Rosenstiel Award 2012- Dr. Steven J. Elledge

The 2012 Rosenstiel award is being awarded to Dr. Steven J. Elledge of Harvard University and the Howard Hughes Medical Institute for his seminal contributions towards understanding the eukaryotic DNA damage response[1] [2] .
Cells are constantly challenged by damage to their DNA. It of no surprise therefore, that both prokaryotic and eukaryotic cells have evolved sophisticated and remarkably complex responses to deal with damaged DNA. It is for elucidating these mechanisms that Dr. Elledge is being honored with the Rosenstiel award this year.
Dr. Elledge’s interest with the DNA damage response began as a graduate student at MIT in the laboratory of Graham Walker, where he identified and cloned genes involved in DNA repair mechanism known as the SOS reponse in the bacterium E.coli[3, 4] . It was during this time that Dr. Elledge also invented an extremely useful molecular biology tool known as ‘phasmids’ which allowed for the ability to rapidly clone E.coli genes by packaging them in phages[5].
After MIT, Dr Elledge began his postdoctoral work at Stanford University where he discovered the Ribonucleotide reductase(RNR) genes in budding yeast[6, 7]. These genes are induced following DNA damage to promote the synthesis of deoxyribonucleotides which helps facilitate DNA repair. Dr. Elledge followed up on this work as a professor at Baylor University by a series of important papers that shed light on how cells arrest division after DNA damage. Most notably in 1994, his group identified the Rad53 checkpoint kinase that is activated after DNA damage and contributes to cell cycle arrest [8]. In 1998, his group also identified the mammalian homolog of Rad53 (Chk2) [9, 10].In 1999, the Elledge group reported that the DNA damage checkpoint in yeast occurs in two parallel pathways laying the foundation of our understanding of the DNA damage checkpoint[11]. More recently, work from the Elledge lab identified novel factors in the DNA damage response by performing a siRNA screen in mammalian cells[12].
Dr Steve Elledge has been an investigator of the Howard Hughes Medical Institute since 1993. In 2003 he moved to Harvard Medical School as Professor in the Departments of Genetics and as a Geneticist in the Department of Medicine, Brigham and Women’s Hospital. Dr. Elledge was elected in 2003 to both the U.S. National Academy of Sciences and the American Academy of Arts and Sciences. In addition to the Rosenstiel award, he has received the DAMD Breast Cancer Innovator Award (2003), the National Academy of Sciences Award in Molecular Biology (2002), the John B. Carter, Jr. Technology Innovation Award (2002), and the Paul Marks Prize for Cancer Research (2001[2]).

Editor’s Note: On Mar 20, 2013, Elledge was named to receive a 2013 Canada Gairdner International Award.

1. Brownlee, C., Biography of Stephen J. Elledge. Proc Natl Acad Sci U S A, 2004. 101(10): p. 3336-7.
2. Haber, J.E., The 2005 Genetics Society of America Medal. Steven J. Elledge. Genetics, 2005. 169(2): p. 506-7.
3. Elledge, S.J. and G.C. Walker, Proteins required for ultraviolet light and chemical mutagenesis. Identification of the products of the umuC locus of Escherichia coli. J Mol Biol, 1983. 164(2): p. 175-92.
4. Elledge, S.J. and G.C. Walker, The muc genes of pKM101 are induced by DNA damage. J Bacteriol, 1983. 155(3): p. 1306-15.
5. Elledge, S.J. and G.C. Walker, Phasmid vectors for identification of genes by complementation of Escherichia coli mutants. J Bacteriol, 1985. 162(2): p. 777-83.
6. Elledge, S.J. and R.W. Davis, Identification of the DNA damage-responsive element of RNR2 and evidence that four distinct cellular factors bind it. Mol Cell Biol, 1989. 9(12): p. 5373-86.
7. Elledge, S.J. and R.W. Davis, DNA damage induction of ribonucleotide reductase. Mol Cell Biol, 1989. 9(11): p. 4932-40.
8. Allen, J.B., et al., The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast. Genes Dev, 1994. 8(20): p. 2401-15.
9. Hirao, A., et al., DNA damage-induced activation of p53 by the checkpoint kinase Chk2. Science, 2000. 287(5459): p. 1824-7.
10. Matsuoka, S., M. Huang, and S.J. Elledge, Linkage of ATM to cell cycle regulation by the Chk2 protein kinase. Science, 1998. 282(5395): p. 1893-7.
11. Sanchez, Y., et al., Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms. Science, 1999. 286(5442): p. 1166-71.
12. Adamson, B., et al., A genome-wide homologous recombination screen identifies the RNA-binding protein RBMX as a component of the DNA-damage response. Nat Cell Biol, 2012. 14(3): p. 318-28.

Elledge wins Rosenstiel Award

Professor Stephen J. Elledge of the Harvard Medical School and the Howard Hughes Medical Institute has been awarded the 42nd Rosenstiel Award For Distinguished Work in Basic Medical Science  for “elucidating how eukaryotic cells sense and respond to DNA damage”. He identified key DNA damage response genes both in yeast and mammalian cells, showed how the pathway is activated by DNA lesions, and made key contributions to defining the cascade of phosphorylation events that enforces cell cycle arrest and controls DNA repair. Dr. Elledge’s work is also marked by the development of powerful research tools to uncover the network of genes involved in sensing and repairing DNA damage. His pioneering work laid the foundation for our current understanding of how failures in DNA damage sensing relate to the medically important field of genome instability.

The Rosenstiel Award consists of a cash prize and a medal, to be awarded at a dinner at Brandeis on March 14, 2013.

• For a recent review, see The DNA Damage Response: Making it safe to play with knives
  
• see story at BrandeisNOW

 

2012 Rosenstiel Award Recipient, Dr. Nahum Sonenberg

2012 Rosenstiel Award Lecture
Thursday, March 29, 2012, 4:00 PM
Gerstanzang 123

The 2012 Rosenstiel award winner, Dr. Nahum Sonenberg of McGill University, is a well-deserving recipient of this honor. Dr. Sonenberg received his Ph.D. in 1976 at the Weizman Institute of Science.  He then worked with Aaron Shatkin, where he discovered the translation initiation factor responsible for binding the 5’ cap of mRNA, eukaryotic Initiation Factor 4E (eIF4E); He has studied translation ever since.  Although his lab focuses on understanding how the cell achieves precise control of translation initiation, this line of investigation has led to discoveries affecting a wide variety of systems.  His lab has made key discoveries in cancer, obesity, virology, memory consolidation and how translation control plays a role in regulating these disparate processes.

In 1988, the Sonenberg lab made the groundbreaking discovery (Nature 1988, http://www.ncbi.nlm.nih.gov/pubmed/2839775) that the uncapped viral mRNA from poliovirus recruits the ribosome to internal regions of the 5’ untranslated region (UTR).  These sites have since been renamed internal ribosomal entry sites (IRESs). This finding was exciting since eukaryotic translation initiation typically requires the 5’ cap on an mRNA for eIF4E binding which subsequently recruits translation initiation machinery.  Until this time, the only mechanism of translation initiation was through the binding of eIF4E to the 5’ cap of mRNAs.  Sonenberg’s discovery that some mRNA has a mechanism to bypass the need for eIF4E binding and thereby avoiding translation control mechanisms started a new line of investigation in the translation field.  Along with discovering IRESs, this paper established an in vitro and an in vivo assay to study cap-independent translation initiation.  These assays are still used widely to test for IRES activity of mRNA UTRs.

Since that initial discovery, it has been found that many viruses contain IRES sequences in the UTR of mRNA that direct translation of viral proteins.  Some viruses, including poliovirus, are able to hijack eukaryotic translation machinery by cleaving factors necessary for canonical cap-dependent translation initiation, but dispensable for IRES translation. In this way, viral mRNAs are able to outcompete eukaryotic mRNAs for ribosome binding and in many cases become the most abundant transcript being translated.

Since the discovery of viral IRESs, many labs, including the Sonenberg lab, have discovered that some cellular genes also use IRESs to bypass the typical translation initiation control mechanisms. These genes are capable of translating even when the cell is actively shutting down translation.  One such cellular IRES-containing mRNA is the insulin receptor message, the IRES I study in the Marr lab.  Using assays similar to those first used in the 1988 paper published by the Sonenberg lab, I am exploring the necessity for the various initiation factors and IRES sequences required for efficient translation of insulin receptor in Drosophila melanogaster and mammalian cells.

The discovery that Dr. Sonenberg made in 1988 is only one example of the elegant research his lab has produced and continues to pursue.

Allis, Grunstein to receive 2011 Rosenstiel Award

The 2011 recipients of the Lewis S. Rosenstiel Award for Distinguished Work in Basic Medical Science are C. David Allis (Rockefeller Univ.) and Michael Grunstein (UCLA) for their discovery that histones and histone acetylation directly regulate transcription.  There will be lectures and an award ceremony at Brandeis University on April 14, 2011 at 3:30 pm in the Carl J. Shapiro Theater, Shapiro Campus Center

C. David Allis (Tri-Institutional Professor, Joy and Jack Fishman Professor, Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University)

Beyond the Double Helix: Varying the ‘Histone Code’

Michael Grunstein (Distinguished Professor , Department of Biological Chemistry , University of California, Los Angeles )

Towards histone function

A reception will follow in the Shapiro Science Center Atrium for all attendees of the talk, from roughly 5:30 until 7 pm.

For more information, see Brandeis NOW and the Rosenstiel Award website.