This proposal is a request for partial financial support for a meeting on Molecular Chaperones and Stress Responses to be held from May 4 - 8, 2010 at Cold Spring Harbor Laboratory. This meeting is the premier international format for presentation of new results in this area, and is attended by representatives from virtually every major laboratory in the field. The explosion of new information on how the folded state of proteins is acquired and maintained in vivo and the involvement of this process in an increasing number of disease states and in normal aging guarantees the excitement of this meeting. Among the highlights of the meeting will be sessions devoted to: (1) Protein misfolding and disease, emphasizing the role of alternative folding pathways in protein biogenesis and lifecycle and mounting evidence for chaperone involvement in Alzheimer's Disease, polyglutamine diseases and the aging process (2) new structural and mechanistic information on some intensively studied chaperones, (3) the role of chaperones in diverse cellular transactions and the signal transduction pathways that integrate them, (4) the crosstalk between protein folding and proteolysis mediated by chaperones, (5) how the various protein folding and quality control systems in a cell function together to provide a robust protein folding environment and how the breakdown of such protein homeostasis (proteostasis) contributes to disease and normal aging, (6) the diverse protein quality control strategies used by a cell to ensure the integrity of the secretory pathway during times of protein folding stress. The field of heat shock proteins and molecular chaperones has grown rapidly and draws interest not only from traditional scientific disciplines in the basic sciences but also from numerous areas of biomedical research including neurodegenerative disease, infectious diseases, cancer, heart disease and aging. The meeting will include seven lecture and three poster sessions. The proposed sessions include: I- Chaperone Biochemistry &Protein Folding, II- Chaperone Function in Disease and Development, III- Diseases of Protein Misfolding IV- Quality Control &Protein Trafficking V- Evolution and Regulation of Protein Folding Machines, VI- Chaperones and Proteolysis, and VII- Manipulating Chaperone Networks and Protein Folding Pathways. Each session will consist of eight to nine oral presentations and will be chaired by an invited speaker. A maximum of two additional speakers will be pre-invited per session and the remainder will be selected from submitted abstracts. This balance of talks allows the meeting to feature presentations by leading scientists, to be responsive to exciting new developments, to encourage diverse participation and to recognize new investigators. The subsequent meetings (2012 and 2014) will follow a similar format and will include topics highly relevant to the current research at the time of the meeting.
Proteins are composed of polymers of amino acids (or polypeptides) and execute essential tasks in all living organisms. Protein function is critically dependent on the folding of their constituent polypeptides into active three-dimensional objects and experimental evidence accumulated in the recent past has drawn attention to contribution that failure of this process (protein misfolding) makes to some of the most important diseases affecting humanity. The latter include common neurodegenerative disorders, such as Parkinson's disease and Alzheimer's disease, common metabolic disorders such as Diabetes Mellitus and a host of other conditions liked to the aging process. The Cold Spring Harbor Meeting on Molecular Chaperones and Stress Responses brings together experts in diverse aspects of protein folding and the cellular response to protein misfolding. As such it serves as the premier clearinghouse for ideas on how to eventually translate the basic discoveries in the area to future treatments of recalcitrant diseases.
