CONF ON PROTEIN FOLDING/TRANSPORT IN SECRETORY PATHWAY

在真核细胞中，被指定为细胞表面或外部的 环境首先转移到内质网(ER)，在内质网中 最初的蛋白质折叠和修饰发生在 蛋白质以达到其适当的功能构象。最近， 我们对这一问题的理解有了重大突破。 指导蛋白质折叠的细胞机械，控制后- 新生多肽的翻译修饰及其识别 突变的蛋白质，并针对它们进行降解。这些过程是 确保最终蛋白质产品的保真度所必需的。一批 Er分子伴侣已被鉴定为可瞬时相互作用 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成为 下定决心。这次会议将聚焦于基因， 目前正在采用的生化和细胞生物学方法 用来阐明蛋白质生物合成的初始步骤 分泌途径。因为许多疾病都可以归因于 在这些过程中，将有几次会议专门讨论 蛋白质折叠异常及其监控和调控的细胞机制 对错误折叠或组装的蛋白质作出反应。更直接地 解决蛋白质折叠异常导致疾病的作用，那里 将讨论特定的蛋白质，当这些蛋白质发生突变时，会导致 错误折叠的蛋白质是疾病的核心 进程。我们的意图将会结合基本 正在探索蛋白质折叠和蛋白质折叠机制的研究人员 与更多的应用或临床研究人员进行伴侣互动 在蛋白质中识别各种疾病的潜在原因 水平。我们认为，这些团体之间的这种互动将提供 了解目前已知情况的应用研究人员 关于蛋白质如何通过分泌途径折叠和运输 被控制，并将为基础研究人员提供生物学上的 相关的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带来新的 合作和更好地了解某些疾病状态和 可能最终导致新的干预和治疗方法。

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.