355 research outputs found
Progress and promise
No full textAs he prepares to step down as the Editor-in-Chief of eLife, Randy Schekman reflects on the origins of the journal, the eLife approach to peer review, and current challenges in scientific publishing
Reflection on the enduring impact of Prof. Luis Leloir’s discoveries that led to his 1970 Nobel Prize in Chemistry
No full textReflexiones del Premio Nobel Randy Schekman acerca del impacto de los descubrimientos de Luis Leloir que llevaron a recibir el Premio Nobel en 1970. Texto redactado en ocasión del 50º aniversario del otorgamiento del Premio Nobel de Química a Luis F. Leloir.originalFil: Schekman, Randy.1 página en papelLFL-CD-OTROS. Escritos de OtrosUnidad documental simpl
Cells, Genes and Discovery in Basic Science and Disease
No full textRandy Schekman, a co-recipient of the 2013 Nobel Prize in Physiology or Medicine, presents a lecture as part of the Oregon Nobel Laureate Symposium at Linfield University. Schekman shares special insights into the science and discovery of his Nobel award-winning research on cellular membranes and vesicle traffic, as well as its impact on life saving drugs, vaccines and genetic forms of Parkinson’s disease
General lecture: Budding Yeast and the Brain
No full textGeneral lecture delivered on November 13, 2003,Duration: 72 minutes.Speaker bio: Dr. Randy Schekman is a Professor in the Department of Molecular and Cell Biology, University of California, Berkeley, and an Investigator of the Howard Hughes Medical Institute. He studies the enzymology of DNA replication as a graduate student with Arthur Kornberg at Stanford University. His current interest in cellular membranes developed during a postdoctoral period with S.J. Singer at the University of California, San Diego. At Berkeley, he developed a genetic and biochemical approach to the study of eukaryotic membrane traffic. Among his awards are the Eli Lilly Award in microbiology and immunology, the Lewis S. Rosenstiel Award in basic biomedical science, the Gairdner International Award, the Amgen Award of the Protein Society, the Albert Lasker Award in Basic Medical Research and the Louisa Gross Horwitz Prize of Columbia University. He is a member of the National Academy of Sciences and the American Academy of Arts and Sciences. In 1999, he was the President of the American Society for Cell Biology and was appointed Editor of the Annual Review of Cell and Developmental Biology. In 2002, he was elected Chair of the Biochemistry Section of the National Academy of Sciences and was selected as Scientific Director of the Jane Coffin Childs Memorial Fund for Biomedical Research. Protein secretion is a fundamental and evolutionary conserved process in nucleated cells. Membrane traffic processes are responsible for cell growth compartmentation of metabolic pathways, and specialized activities such as hormone, growth factor, neurotransmitter, and antibody production. Beginning in 1976, Schekman and his co-workers used genetic approaches to study membrane traffic in yeast cells. Ingenious methods were devised for the detection and enrichment of conditional mutants defective in the secretory pathways (sec mutants). Many genes were defined that chart a pathway of membrane transport and protein sorting that is remarkably similar to the pathway defined by cytologic means in mammalian cells. Schekman was the first to recognize that the mechanism of this complex but ubiquitous process could be dissected using a combination of molecular biology and biochemistry, and that yeast would be the simplest model system where such techniques are readily available. Given the similarity in the transport processes across the evolutionary spectrum, the practical advantages of yeast fermentation have made this an important vehicle for the production and secretion of proteins important to the pharmaceutical industry. Recombinant hepatitis vaccine, the only commercial hepatitis vaccine on the market, is produced in yeast. One quarter of the current world supply of recombinant human insulin is produced by secretion in yeast. Much of the background for the applications was provided by Schekman’s elucidation of the secretory pathway in yeast.1_ytrra5e
Rothman and Schekman SNAREd by Lasker for Trafficking
No full textAbstractThis year, the recipients of the Lasker Award for Basic Medical Research are James Rothman and Randy Schekman. This highly anticipated honor highlights their unique contributions to our understanding of the mechanisms of membrane traffic
"Der Druck, in renommierten Magazinen veröffentlichen zu müssen, führt auch dazu, dass Wissenschaftler betrügen"
No full textSagt Medizin-Nobelpreisträger Randy Schekman im SPIEGEL-Interview: http://www.spiegel.de/wissenschaft/medizin/nobelpreistraeger-randy-schekman-kritisiert-science-und-nature-a-1154483.htm
"Der Druck, in renommierten Magazinen veröffentlichen zu müssen, führt auch dazu, dass Wissenschaftler betrügen"
No full textSagt Medizin-Nobelpreisträger Randy Schekman im SPIEGEL-Interview: http://www.spiegel.de/wissenschaft/medizin/nobelpreistraeger-randy-schekman-kritisiert-science-und-nature-a-1154483.htm
Author response
No full textPlanar cell polarity (PCP) requires the asymmetric sorting of distinct signaling receptors to distal and proximal surfaces of polarized epithelial cells. We have examined the transport of one PCP signaling protein, Vangl2, from the trans Golgi network (TGN) in mammalian cells. Using siRNA knockdown experiments, we find that the GTP-binding protein, Arfrp1, and the clathrin adaptor complex 1 (AP-1) are required for Vangl2 transport from the TGN. In contrast, TGN export of Frizzled 6, which localizes to the opposing epithelial surface from Vangl2, does not depend on Arfrp1 or AP-1. Mutagenesis studies identified a YYXXF sorting signal in the C-terminal cytosolic domain of Vangl2 that is required for Vangl2 traffic and interaction with the μ subunit of AP-1. We propose that Arfrp1 exposes a binding site on AP-1 that recognizes the Vangl2 sorting motif for capture into a transport vesicle destined for the proximal surface of a polarized epithelial cell.</p
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