Зюдоф Томас

Личная информация


1982-1983 Postdoctoral Fellow;

Max-Planck-Institut für Biophysikalische Chemie, Göttingen, Germany (mentor: Dr. V. P. Whittaker)

1983-1986 Postdoctoral Fellow; Dept. of Molecular Genetics, UT Southwestern Medical Center at Dallas, Texas (mentors: Drs. M.S. Brown and J.L. Goldstein)

1986-1989 Assistant Investigator, Howard Hughes Medical Institute at Dallas, UT Southwestern

1987-1989 Assistant Professor, Department of Molecular Genetics, UT Southwestern

1989-1991 Associate Professor, Department of Molecular Genetics, and Associate Investigator, Howard Hughes Medical Institute, UT Southwestern

1991-2008 Professor, Department of Molecular Genetics, UT Southwestern Medical Center at Dallas

1991-present Investigator, Howard Hughes Medical Institute

1995-2008 Gill Distinguished Chair in Neuroscience Research, UT Southwestern

1995-1998 Director, Abt. Molekulare Neurobiologie, Max-Planck-Institut für experimentelle Medizin; Göttingen, Germany, and Scientific Member of the Max-Planck-Society

1999-2001 Chair, Graduate Program in Neuroscience, UT Southwestern

1997-2008 Lloyd B. Sands Distinguished Chair in Neuroscience, UT Southwestern

1997-2006 Director, Center for Basic Neuroscience, UT Southwestern

2007-2008 Chair, Department of Neuroscience, UT Southwestern

2008-present Avram Goldstein Professor, Dept. of Molecular & Cellular Physiology; by courtesy, Depts. of Neurology and of Psychiatry & Behavioral Sciences, Stanford University School of Medicine

2008-present Adjunct Professor of Neuroscience, UT Southwestern


Период обученияСтрана, городУчебное заведениеДополнительная информация
1975–1977 University of Aachen Medical School
1979 Harvard Medical School Visiting student
1977–1982 University of Göttingen Medical School
1978–1982 Max-Planck-Institut für biophysikalische Chemie in Göttingen Assistant scientist

Премии и заслуги

1993 W. Alden Spencer Award from Columbia University (shared with Richard Scheller)

1994 Wilhelm Feldberg Award

1997 Roger Eckert Award Lecture, Göttingen

1997 U.S. National Academy Award in Molecular Biology (shared with Richard Scheller)

2000-2010 1st Merit Award, NIMH

2002 Elected to the National Academy of Sciences of the U.S.A.

2004 MetLife Award (shared with Roberto Malinow)

2004 Bristol-Myers Squibb Award for Distinguished Achievement in Neuroscience Research

2007 Elected to the Institute of Medicine

2008 Bernhard Katz Award, Biophysical Society (shared with Reinhard Jahn)

2008 Passano Foundation Award

2010 Elected to the American Academy of Arts & Sciences

2010-2020 2nd Merit Award, NIMH

2010 Kavli Prize in Neuroscience (shared with James Rothman and Richard Scheller)

2010 Elected Foreign Member of the Norwegian Academy of Arts and Sciences

2010 Albert Einstein Professorship, Chinese Academy of Sciences, Beijing

Членство в научных обществах

1994 Member of the NIMH Evaluation Panel on Neuroscience

1995-present Editorial Board, Neuron

1995-2006 Editorial Board, Journal of Biological Chemistry

1995-1998 Member, Cellular and Developmental Neurobiology Study Section, NIMH Program

1998-2003 Member, Molecular and Cellular Developmental Neuroscience 1 Study Section

1996-2003 Associate Member, Neurosciences Research Program, San Diego, CA

1997-2001 Receiving Editor, European Journal of Neuroscience

2000-present Editorial Board, Neuroscience

2000-2001 Co-Editor, European Journal of Cell Biology

2000-present Editorial Board, Journal of Molecular Neuroscience

2001-present Editorial Board, European Journal of Neuroscience

2004-2009 Editorial Board, Journal of Neuroscience

2006-present Editorial Board, Proc. Natl. Acad. Sciences U.S.A.

2008 Chair, Neurobiology of Disease Gordon Conference, Oxford UK

2008-2012 Member, Cellular and Molecular Biology of Neurodegeneration Study Section (CMND) Scientific Advisory Boards and Consultancies:

2002-present REATA Pharmaceuticals, Inc., Dallas, TX

2008-2010 Pfizer Neuroscience Review Board,

2010-present Gallo Clinic and Research Center, UCSF, San Francisco, CA

2011-present Circuit Therapeutics Inc., Menlo Park, CA

2012-present Center of Excellence in Genomic Medicine Research, King Abdulaziz University, Jeddah, Saudi Arabia

2012-present Picower Center at MIT, Cambridge, MA

2013-present Genentech Neuroscience, South San Francisco, CA 

Избранные публикации

  1. Petrenko A.G., Ullrich B., Missler M., Krasnoperov V., Rosahl T.W., Südhof T.C. (1996). Structure and evolution of neurexophilin. J. Neurosci. 16 (14), 4360–9 [+]

    Using affinity chromatography on immobilized alpha-latrotoxin, we have purified a novel 29 kDa protein, neurexophilin, in a complex with neurexin l alpha. Cloning revealed that rat and bovine neurexophilins are composed of N-terminal signal peptides, nonconserved N-terminal domains (20% identity over 80 residues), and highly homologous C-terminal sequences (85% identity over 169 residues). Analysis of genomic clones from mice identified two distinct neurexophilin genes, one of which is more homologous to rat neurexophilin and the other to bovine neurexophilin. The first neurexophilin gene is expressed abundantly in adult rat and mouse brain, whereas no mRNA corresponding to the second gene was detected in rodents despite its abundant expression in bovine brain, suggesting that rodents and cattle primarily express distinct neurexophilin genes. RNA blots and in situ hybridizations revealed that neurexophilin is expressed in adult rat brain at high levels only in a scattered subpopulation of neurons that probably represent inhibitory interneurons; by contrast, neurexins are expressed in all neurons. Neurexophilin contains a signal sequence and is N-glycosylated at multiple sites, suggesting that it is secreted and binds to the extracellular domain of neurexin l alpha. This hypothesis was confirmed by binding recombinant neurexophilin to the extracellular domains of neurexin l alpha. Together our data suggest that neurexophilin constitutes a secreted glycoprotein that is synthesized in a subclass of neurons and may be a ligand for neurexins.

  2. Ushkaryov Y.A., Petrenko A.G., Geppert M., Südhof T.C. (1992). Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin. Science 257 (5066), 50–6 [+]

    A family of highly polymorphic neuronal cell surface proteins, the neurexins, has been identified. At least two genes for neurexins exist. Each gene uses alternative promoters and multiple variably spliced exons to potentially generate more than a 100 different neurexin transcripts. The neurexins were discovered by the identification of one member of the family as the receptor for alpha-latrotoxin. This toxin is a component of the venom from black widow spiders; it binds to presynaptic nerve terminals and triggers massive neurotransmitter release. Neurexins contain single transmembrane regions and extracellular domains with repeated sequences similar to sequences in laminin A, slit, and agrin, proteins that have been implicated in axon guidance and synaptogenesis. An antibody to neurexin I showed highly concentrated immunoreactivity at the synapse. The polymorphic structure of the neurexins, their neural localization, and their sequence similarity to proteins associated with neurogenesis suggest a function as cell recognition molecules in the nerve terminal.

  3. Brose N., Petrenko A.G., Südhof T.C., Jahn R. (1992). Synaptotagmin: a calcium sensor on the synaptic vesicle surface. Science 256 (5059), 1021–5 [+]

    Neurons release neurotransmitters by calcium-dependent exocytosis of synaptic vesicles. However, the molecular steps transducing the calcium signal into membrane fusion are still an enigma. It is reported here that synaptotagmin, a highly conserved synaptic vesicle protein, binds calcium at physiological concentrations in a complex with negatively charged phospholipids. This binding is specific for calcium and involves the cytoplasmic domain of synaptotagmin. Calcium binding is dependent on the intact oligomeric structure of synaptotagmin (it is abolished by proteolytic cleavage at a single site). These results suggest that synaptotagmin acts as a cooperative calcium receptor in exocytosis.

  4. Petrenko A.G., Perin M.S., Davletov B.A., Ushkaryov Y.A., Geppert M., Südhof T.C. (1991). Binding of synaptotagmin to the alpha-latrotoxin receptor implicates both in synaptic vesicle exocytosis. Nature 353 (6339), 65–8 [+]

    A vertebrate neurotoxin, alpha-latrotoxin, from black widow spider venom causes synaptic vesicle exocytosis and neurotransmitter release from presynaptic nerve terminals. Although the mechanism of action of alpha-latrotoxin is not known, it does require binding of alpha-latrotoxin to a high-affinity receptor on the presynaptic plasma membrane. The alpha-latrotoxin receptor seems to be exclusively at the presynaptic plasmamembrane. Here we report that the alpha-latrotoxin receptor specifically binds to a synaptic vesicle protein, synaptotagmin, and modulates its phosphorylation. Synaptotagmin is a synaptic vesicle-specific membrane protein that binds negatively charged phospholipids and contains two copies of a putative Ca(2+)-binding domain from protein kinase C (the C2-domain), suggesting a regulatory role in synaptic vesicle fusion. Our findings suggest that a physiological role of the alpha-latrotoxin receptor may be the docking of synaptic vesicles at the active zone. The direct interaction of the alpha-latrotoxin receptor with a synaptic vesicle protein also suggests a mechanism of action for this toxin in causing neurotransmitter release.