Aging Research at the 2010 through 2014 ASHEcon Biennial Conferences

摘要 本提案是为将于2010年5月4日至8日在冷泉港实验室举行的分子伴侣和应激反应会议提供部分资金支持的请求。该会议是介绍该领域新成果的首要国际形式，几乎所有主要实验室的代表都参加了该会议。关于蛋白质折叠状态如何在体内获得和维持的新信息的爆炸，以及这一过程在越来越多的疾病状态和正常衰老中的参与，保证了这次会议的兴奋。会议的重点将包括专门讨论以下问题的会议：（1）蛋白质错误折叠和疾病，强调替代折叠途径在蛋白质生物发生和生命周期中的作用，并增加了伴侣蛋白参与阿尔茨海默病、多聚谷氨酰胺疾病和衰老过程的证据。（3）分子伴侣在多种细胞事务中的作用以及整合它们的信号转导途径，（4）分子伴侣介导的蛋白质折叠和蛋白质水解之间的串扰，（五）细胞中的各种蛋白质折叠和质量控制系统如何共同发挥作用以提供稳健的蛋白质折叠环境，以及这种蛋白质如何分解稳态（蛋白质稳态）有助于疾病和正常衰老，（6）细胞使用的多种蛋白质质量控制策略，以确保蛋白质折叠应激期间分泌途径的完整性。热休克蛋白和分子伴侣领域发展迅速，不仅引起了基础科学中传统科学学科的兴趣，而且引起了包括神经退行性疾病、传染病、癌症、心脏病和衰老在内的许多生物医学研究领域的兴趣。会议将包括七个讲座和三个海报会议。拟议的会议包括：I-伴侣生物化学和蛋白质折叠，II-伴侣在疾病和发育中的功能，III-蛋白质错误折叠的疾病IV-质量控制和蛋白质运输V-蛋白质折叠机的进化和调节，VI-伴侣和蛋白质水解，以及VII-操纵伴侣网络和蛋白质折叠途径。每场会议将包括八至九次口头发言，并将由一名特邀发言者主持。每届会议最多将预先邀请两名发言者，其余发言者将从提交的摘要中选出。这种会谈的平衡使会议能够由领先的科学家进行演讲，对令人兴奋的新发展做出反应，鼓励多元化的参与并认识新的研究者。 随后的会议（2012年和2014年）将遵循类似的形式，并将包括与会议时的当前研究高度相关的议题。

ABSTRACT 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.