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Protein Homeostasis in Health and Disease

  December 22, 2017  

Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
April 17 - 21, 2018

Proper expression, folding, transport, and clearance of proteins are critical for cell function and organismal health. Chaperones and enzymes that post-translationally assist newly synthesized proteins help ensure that they are correctly folded and functional, or are degraded. Translocation machineries, proteasomes, and autophagic activities are critical for subcellular localization and for degradation as necessary. Stress and aging challenge the robustness of these chaperone and clearance networks leading to protein mismanagement, overload, and cellular dysfunction. In humans, this is associated with the accumulation and aggregation of misfolded and aggregation-prone proteins, a feature of numerous neurodegenerative, metabolic, and oncogenic diseases.  

You are invited to participate in the 2018 meeting on Protein Homeostasis in Health & Disease. Groundbreaking work - on molecular chaperones, the unfolded protein response, stress responses, and how these processes are implicated in disease - has first been presented at this meeting over the past three decades. The 2018 meeting provides an opportunity to showcase the latest research in this area and will feature talks by leading investigators.

The format of the meeting will include eight sessions consisting of invited and short talks, chosen from the submitted abstracts, and two poster sessions. All speakers and chairs are strongly encouraged to stay for the entire meeting. The organizers will decide the suitability of each abstract for oral or poster presentation, but please specify if you prefer a poster. Abstracts should contain only new and unpublished material and must be submitted electronically by the abstract deadline. Selection of material for oral and poster presentation will be made by the organizers and individual session chairs. Status (talk/poster) of abstracts will be posted on our web site as soon as decisions have been made by the organizers.

Organized by: Judith Frydman, F. Ulrich Hartl, Harm H. Kampinga, Richard Morimoto
Invited Speakers:
Proteostasis at the Ribosome 
Chairperson: Judith Frydman, Stanford University
Bernd Bukau, University of Heidelberg
Elke Deuerling, Universität Konstanz 

Chaperone Mechanisms I 
Chairperson: Johannes Buchner, Technical University, Munich
David Agard, University of California San Francisco/HHMI
Manajit Hayer-Hartl, Max Planck Institute of Biochemistry-Martinsried 
Rachel Klevit, University of Washington

Novel Mechanisms of Quality Control
Chairperson: Simon Alberti, Max Planck Institute, Dresden
Thomas Nystrom University of Gothenburg
Tony Hyman, MPI Dresden

Degradative Mechanisms
Chairperson: Yoshinori Ohsumi, Tokyo University of Technology 
Keiji Tanaka, RIKEN Brain Science Institute
Ivan Dikic, Goethe University Medical School

Chaperone Mechanisms II
Chairperson: Ulrich Hartl, Max Planck Institute of Biochemistry-Martinsreid
Lila Gierasch, University of Massachusetts-Amherst
Matthias Mayer, University of Heidelberg
Dan Southworth, University of Michigan

Pathogenic and Non-Pathogenic Aggregates and Amyloids
Chairperson: Ursula Jakob, University of Michigan
Chris Dobson, University of Cambridge
Margaret Sunde, The University of Sydney
David Eisenberg, University of California Los Angeles

Organellar Proteostasis and Spatial Quality Control
Chairperson: Ineke Braakman, Ultrecht University
Johnathan Weissman, University of California San Francisco
David Ron, Cambridge Institute for Medical Research
Kaz Nagata, Kyoto Sangyo University

Proteostasis Failure in Aging and Disease
Chairperson: Rick Morimoto, Northwestern University 
Jeff Kelly, The Scripps Research Institute
Len Neckers, NCI
Erich Wanker, Max Delbruck Centrum for Molecular Medicine

Panel Discussion - New Mechanisms for Disseminating Scientific Information
Chairperson: Lila Gierasch, University of Massachusetts-Amherst
Deadline for Abstracts: February 2 2018
Registration: Register here
E-mail: carr@cshl.edu
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