This proposal is a request for partial financial support for a meeting on Molecular Chaperones and Stress Responses to be held at Cold Spring Harbor Laboratory from April 29 - May 3, 2014. 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. Because of the recent developments that have identified new and emerging molecular machines and their mechanism of action, there will be two session devoted to mechanistic insight of protein folding machines. Additionally, it is becoming more clear that these machines do not work in isolation, but are orchestrated in a network of folding machineries. Therefore, for the first time we will have a session devoted to network evaluation of protein folding. Protein misfolding and disease will be heavily represented at the meeting and emerging principles that suggest the spread of misfolded disease causing proteins will be predominantly displayed and discussed in it own session. The diverse protein quality control strategies used by a cell to ensure the integrity of the secretory pathway during times of protein folding stress will be represented as well as a new emerging topic on spatial quality control within a cell. 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 nine lecture sessions and three poster sessions. The proposed sessions include: 1) Protein Folding machines, 2) Protein folding machines 2, 3) Networks of protein homeostasis, 4) Spatial quality control, 5) Protein misfolding diseases - infectious spreading, 6) ER quality control, 7) Protein degradation pathways, 8) Protein synthesis, 9) Functional aggregation. 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.
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.
