Aging Research at the 2010 through 2014 ASHEcon Biennial Conferences

摘要 这项提案是为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。这次会议是介绍这一领域新成果的主要国际形式，来自该领域几乎所有主要实验室的代表都出席了会议。关于蛋白质折叠状态是如何在体内获得和保持的新信息的爆炸性增长，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，确保了这次会议的兴奋。会议的亮点包括：(1)蛋白质错误折叠与疾病，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，以及越来越多的证据表明伴侣参与阿尔茨海默病、聚谷氨酰胺疾病和衰老过程；(2)关于一些深入研究的伴侣的新结构和机制信息；(3)伴侣在不同细胞交易中的作用和整合它们的信号转导途径；(4)伴侣介导的蛋白质折叠和蛋白降解之间的串扰，(5)细胞中不同的蛋白质折叠和质量控制系统如何共同作用，以提供一个强大的蛋白质折叠环境，以及这种蛋白质稳态的破坏如何导致疾病和正常衰老，(6)细胞在蛋白质折叠应激期间使用的各种蛋白质质量控制策略，以确保分泌途径的完整性。热休克蛋白和分子伴侣的领域发展迅速，不仅引起了基础科学中传统科学学科的兴趣，也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众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作用，III-蛋白质错误折叠的疾病IV-质量控制和蛋白质运输V-蛋白质折叠机器的进化和调控，VI-伴侣和蛋白质分解，以及VII-操纵伴侣网络和蛋白质折叠途径。每期会议由8至9名口头陈述组成，由一名特邀发言者主持。每届会议最多只能再邀请两名发言者，其余发言者将从提交的摘要中选出。这种讨论的平衡使会议能够以顶尖科学家的陈述为特色，对令人兴奋的新发展做出反应，鼓励多样化的参与，并表彰新的研究人员。 随后的会议(2012年和2014年)将采用类似的形式，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.