Cold Spring Harbor Laboratory Conference on The Ubiquitin Family

冷泉港实验室泛素家族会议

• 批准号: 7405473
• 负责人: TERRI I. GRODZICKER
• 金额: $ 0.5万
• 依托单位: COLD SPRING HARBOR LABORATORY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-04-11 至 2012-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7405473
• 关键词: Area; Biochemical; Biological Process; Cell Cycle Progression; Cell physiology; Circadian Rhythms; Complex; Development; Fostering; Knowledge; Laboratories; Learning; Light; Link; Memory; Metabolic Control; Modification; Operating System; Participant; Physiological Processes; Postdoctoral Fellow; Property; Proteins; Proteomics; Research; Research Personnel; Role; Scientist; Site-Directed Mutagenesis; Students; System; Time; Translating; Ubiquitin; Ubiquitin family; Work; abstracting; enzyme substrate; functional genomics; graduate student; meetings; novel; polypeptide; posters; programs; symposium; system architecture; three dimensional structure; tool

DESCRIPTION (provided by applicant): Modification of target proteins by ubiquitin and ubiquitin-like polypeptides has emerged as a major mechanism for regulating many cellular processes ranging from metabolic control to cell cycle progression. In turn, these intracellular functions translate into key roles for ubiquitin modification systems in the control of complex regulatory programs at the organismal level including differentiation, development, circadian rhythms, and storage of memories. Although our knowledge of the biological functions of ubiquitin modification systems has exploded over the past decade, our understanding of how these systems operate at a biochemical level remains relatively modest. However, the past few years have witnessed a tremendous surge in the availability of three dimensional structures of components of these modification systems, which is beginning to foster a deeper understanding of how these proteins work. In addition, novel proteomic and functional genomic tools are revealing new functions for components of ubiquitin modification systems, and shedding light on how modification enzymes and substrates are linked together into networks. The objective of the third Cold Spring Harbor meeting on Ubiquitin is to bring together investigators who study the biochemical and structural properties of ubiquitin modification systems with investigators who focus on their biological functions and systems architecture. Given the rapid developments over the past two years, this meeting presents a exciting opportunity for participants to learn about recent developments that will be relevant to their own research. The program will include 8 sessions covering the components of ubiquitin modification systems and the cellular and organismal processes that they control. The sessions will be led by two outstanding and well-known investigators in these areas. With the exception of overview talks presented by the session chairs, all of the talks and posters to be presented will be selected from submitted abstracts, and most of the talks will be given by students, postdoctoral fellows and other younger investigators. It is expected that more than 275 scientists will attend. Of these, over half are likely to be graduate students and postdoctoral fellows. The subsequent meetings (2009 and 2011) will follow a similar format which will include topics that are highly relevant to the current research at the time of the meeting.

描述（由申请人提供）：泛素和泛素样多肽对靶蛋白的修饰已成为调节从代谢控制到细胞周期进程的许多细胞过程的主要机制。 反过来，这些细胞内功能转化为泛素修饰系统在生物体水平控制复杂调控程序（包括分化、发育、昼夜节律和记忆储存）中的关键作用。 尽管我们对泛素修饰系统的生物学功能的了解在过去十年中已经爆炸，但我们对这些系统在生化水平上如何运作的理解仍然相对有限。 然而，在过去的几年里，这些修饰系统的组件的三维结构的可用性出现了巨大的增长，这开始促进对这些蛋白质如何工作的更深入的理解。 此外，新的蛋白质组学和功能基因组学工具正在揭示泛素修饰系统组分的新功能，并揭示修饰酶和底物如何连接在一起形成网络。 第三届冷泉港泛蛋白会议的目标是将研究泛蛋白修饰系统的生物化学和结构特性的研究人员与专注于其生物功能和系统架构的研究人员聚集在一起。 鉴于过去两年的快速发展，本次会议为与会者提供了一个令人兴奋的机会，以了解与他们自己的研究相关的最新发展。 该计划将包括8次会议，涵盖泛素修饰系统的组成部分以及它们控制的细胞和生物过程。 这些会议将由这些领域的两名杰出和知名的调查员主持。 除了会议主席提出的概述性演讲外，所有演讲和海报都将从提交的摘要中选出，大部分演讲将由学生，博士后研究员和其他年轻的研究人员提供。 预计将有超过275名科学家参加。 其中，一半以上可能是研究生和博士后研究员。 随后的会议（2009年和2011年）将遵循类似的形式，其中将包括与会议召开时的当前研究高度相关的议题。