CONF ON PROTEIN FOLDING/TRANSPORT IN SECRETORY PATHWAY

分泌途径中蛋白质折叠/运输的配置

• 批准号: 2766097
• 负责人: Linda M Hendershot
• 金额: $ 0.5万
• 依托单位: KEYSTONE SYMPOSIA
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-01-15 至 1999-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2766097
• 关键词: meeting /conference /symposium; molecular chaperones; protein biosynthesis; protein folding; protein protein interaction; protein transport; secretory protein; travel

In eucaryotic cells, destined for the cell surface or for the external milieu are first translocated into the endoplasmic reticulum (ER) where initial protein folding and modifications occur that are essential for the protein to attain its appropriate functional conformation. Recently, there have been significant breakthroughs in our understanding of the cellular machinery that direct protein folding, that control the post- translational modification of nascent polypeptides, and that recognize aberrant proteins and target them for degradation. These processes are necessary to ensure fidelity of the final protein product. A number of ER molecular chaperones have been identified that interact transiently with folding intermediates and their roles in facilitating and monitoring these processes during protein biosynthesis are rapidly being determined. This conference will focus on the combinations of genetic, biochemical, and cell biological approaches that are currently being used to elucidate the initial steps in the biosynthesis of proteins in the secretory pathway. Because many diseases can be attributed to aberrations in these processes, several sessions will be devoted to abnormal protein folding and the cellular mechanisms for monitoring and responding to incorrectly folded or assembled proteins. To more directly address the role of abnormal protein folding leading to disease, there will be talks dealing with specific proteins that when mutated result in incorrectly folded proteins which are at the heart of the disease process. It is our intention that will meeting will combine basic researchers who are probing the mechanisms of protein folding and chaperone interactions with more applied or clinical researchers who are identifying the underlying cause of various diseases at the protein level. We feel that this interaction between the groups will provide applied researchers with an understanding of what is currently known about how protein folding and transport through the secretory pathway are controlled and will provide basic researcher with biologically relevant model systems to study these processes. We anticipate that the interaction of these two groups of researchers will lead to new collaborations and better understanding of certain disease states and may ultimately lead to new approaches for intervention and treatment.

在真核细胞中，目的地为细胞表面或外部 环境首先转移到内质网（ER）中， 最初的蛋白质折叠和修饰发生， 蛋白质以获得其适当的功能构象。最近， 在我们对宇宙的理解上有了重大突破， 指导蛋白质折叠的细胞机制，控制后 新生多肽的翻译修饰， 异常蛋白质并将其作为降解目标。这些过程 这是确保最终蛋白质产品的保真度所必需的。一些 ER分子伴侣已被鉴定为瞬时相互作用 折叠中间体及其在促进和 在蛋白质生物合成过程中监测这些过程正在迅速地被 测定本次会议将重点讨论基因， 生物化学和细胞生物学方法， 用于阐明蛋白质生物合成的初始步骤， 分泌途径。因为很多疾病都可以归因于 在这些过程中的偏差，几个会议将专门讨论 异常蛋白质折叠和细胞机制， 对错误折叠或组装的蛋白质做出反应。更直接地 解决异常蛋白质折叠导致疾病的作用， 将讨论特定的蛋白质，当突变时， 错误折叠的蛋白质是疾病的核心 过程我们的意图是将会议联合收割机基本 研究人员正在探索蛋白质折叠的机制， 与更多的应用或临床研究人员的伴侣互动， 在蛋白质中识别各种疾病的根本原因 水平我们认为，各集团之间的这种互动将提供 应用研究人员了解目前已知的 关于蛋白质如何通过分泌途径折叠和运输 并将为基础研究人员提供生物学上的 相关模型系统来研究这些过程。我们预计 这两组研究人员的互动将导致新的 合作和更好地了解某些疾病状态， 可能最终导致新的干预和治疗方法。