
Session details
Evening session (19.45 - 22.00) (chaired by Didier Picard)
19.45 Opening remarks by Didier Picard (Université de Genève, Switzerland)
Chaperone machines
20.00 Bernd Bukau (Zentrum für Molekulare Biologie Heidelberg, Germany). Mechanisms of substrate recognition by Hsp70 chaperones.
20.30 Johannes Buchner (Technische Universität München, Garching, Germany). The Hsp90 ATPase and chaperone cycle.
21.00 Chris Prodromou (Institute of Cancer Research, London, UK). Crystal structure of the N-terminal domain of Aha1 in complex with the middle domain of Hsp90 and regulation of the ATPase activity of Hsp90.
21.30 Sophie E. Jackson (Cambridge University, UK). Biophysical studies on human Hsp90 and a new model.
Morning sessions (08.30 - 12.15) (chaired by Johannes Buchner)
Prokaryotic Hsp90 (htpG)
08.30 Pierre Goloubinoff (Université de Lausanne, Switzerland). Hsp90 and htpG: are they true molecular chaperones?
09.00 Hitoshi Nakamoto (Saitama University, Japan). Identification of htpG interacting targets in Cyanobacteria.
09.15 Laurence H. Pearl (Institute of Cancer Research, London, UK). Structure and function of Hsp90 complexes.
09.45 David A. Agard (University of California, San Francisco, CA, USA). The three dimensional structure of htpG.
10.15 - 10.45 Break
Hsp90 clients #1
10.45 Maciej Zylicz (International Institute of Molecular and Cell Biology, Warszawa, Poland). Unfoldase activity of Hsp90; is the MDM2 oncogene a new cochaperone of Hsp90?
11.15 Ami Citri (Weizmann Institute of Science, Rehovot, Israel). Hsp90 limits the signaling potential of ErbB receptor tyrosine kinases.
11.30 Jürgen Beck (University Hospital, Freiburg, Germany). Differential effects of Bag1 on the Hsc70- vs. Hsp90-mediated activation of duck Hepatitis B virus reverse transcriptase in vitro.
11.45 Peter W. Piper (The University of Sheffield, UK). A genome-wide screen for two-hybrid interactors with the Hsp90 molecular chaperone uncovers an Hsp90 requirement for the activity of a stress-activated MAP kinase.
12.00 Hélène Gaude (Université de Lyon 1, France). Hsp90/Cdc37 and the ubiquitin-ligase CHIP regulate stability of the oncosuppressive kinase LKB1.
Evening sessions (19.30 - 22.15) (chaired by Charles Erlichman)
Drugs and disease
19.30 Len Neckers (NCI, NIH, Rockville, MD, USA). HSP90 inhibition disrupts the unfolded protein response and sensitizes the endoplasmic reticulum to vacuolization in response to proteasome inhibition.
20.00 Paul Workman (The Institute for Cancer Research, Sutton, Surrey, UK). Design and development of Hsp90 inhibitors for cancer therapy: From bench to bedside and back.
20.30 John Price (St. Vincent's Institute, Melbourne, Australia). The Hsp90 pharmacological inhibitor, 17-AAG, enhances breast-bone metastasis in a nude mouse model and stimulates in vitro and in vivo osteoclast formation.
20.45 - 21.15 Break
21.15 Francis Burrows (Conforma Therapeutics, San Diego, CA, USA). Hsp90 activation in tumor and normal cells.
Co-chaperones #1
21.45 David O. Toft (Mayo Clinic, Rochester, MN, USA). The Hsp90 co-chaperone GC UNC-45 participates in chaperoning the progesterone receptor.
Evening sessions (19.30 - 22.00) (chaired by Sue Cotterill)
Co-chaperones #2
19.30 Gunter Fischer (Max-Planck-Institut, Halle/Saale, Germany). Biochemical profiles of proteins assisting folding of polypeptide chains.
20.00 Jill L. Johnson (University of Idaho, Moscow, ID, USA). Genetic and physical interactions between Hsp90 and the DNA helicase Ssl2.
20.15 Greg L. Blatch (Rhodes University, Grahamstown, South Africa). Organizing chaperone machinery in the cytoplasm and the nucleus: the Hop connection.
20.30 - 21.00 Break
21.00 Brian C. Freeman (University of Illinois, Urbana, IL, USA). Molecular chaperones promote telomerase dynamics.
21.30 David F. Smith (Mayo Clinic, Scottsdale, AZ, USA). Reproductive defects in FKBP52 knockout mice.
Morning sessions (08.30 - 12.15) (chaired by Thomas Ratajczak)
Co-chaperones #3
08.30 Didier Picard (Université de Genève, Switzerland). p23 in yeast and mice.
09.00 Gro Gausdal (University of Bergen, Norway). Caspase-dependent and geldanamycin enhanced cleavage of co-chaperone p23 in leukemic apoptosis.
09.15 Ken Shirasu (The Sainsbury Laboratory, Norwich, UK). Chaperone complex in the early stage of plant disease resistance signalling.
09.45 Adina Breiman (Tel Aviv University, Israel). The plant co chaperones FKBPs are heat stress induced and their over expression affects expression profiles and plant phenotype.
10.00 Emmanuel De Billy (European Institute of Oncology, Milano, Italy). HARC, a new Hsp90 co-chaperone, regulates the Cdk4/cyclin D/PRB pathway.
10.15 - 10.45 Break
Hsp90 clients #2
10.45 Theo Rein ( Max-Planck-Institut für Psychiatrie, München, Germany). FKBP51 as a marker for drug responsiveness in major depression and its role for glucocorticoid receptor function in mammalian cells.
11.00 Yair Argon (Children's Hospital of Philadelphia and The University of Pennsylvania, Philadelphia, PA, USA). Peptide binding and mouse knock-out.
11.30 Christopher V. Nicchitta (Duke University Medical Center, Durham, NC, USA). Regulation of Grp94-client (poly)peptide interactions by adenosine nucleotides: implications for a stress sensor function for GRP94.
12.00 Daniel T. Gewirth (Duke University Medical Center, Durham, NC, USA). The structural basis for ligand regulation in Grp94, the endoplasmic reticulum Hsp90 chaperone.
Late afternoon sessions (17.15 - 19.15) (chaired by Yoshihiko Miyata)
Hsp90 and relatives in cell biology
17.15 William E. Balch (The Scripps Research Institute, La Jolla, CA, USA). Hsp90 chaperone function in membrane traffic.
17.30 Linda M. Hendershot (St. Jude Children’s Research Hospital, Memphis, TN, USA). Organization of ER chaperones and implications for protein folding.
17.45 Katsumi Kitagawa (St. Jude Children’s Research Hospital, Memphis, TN, USA). The human Sgt1-Hsp90 complex is required for the assembly of kinetochore protein complexes.
Organismic Hsp90 biology
18.00 Christine Queitsch (Bauer Center for Genomics Research, Harvard University, Cambridge, MA, USA). Under Cover: Hsp90 buffers genetic variation.
18.30 Todd A. Sangster (Whitehead Institute for Biomedical Research, Cambridge, MA, USA). Hsp90-mediated buffering of genetic variation.
18.45 Joachim Clos (Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany). A pivotal role for HSP90 in the protozoan parasite Leishmania donovani.