STRUCTURAL BASIS OF CELL MEMBRANE TARGETING, ADHESION, AND SIGNALING

细胞膜靶向、粘附和信号传导的结构基础

• 批准号: 8362111
• 负责人: William I Weis
• 金额: $ 0.03万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362111
• 关键词: ATP phosphohydrolase; Actins; Adhesions; Apical; Cadherins; Cell Adhesion; Cell membrane; Complex; Couples; Cytoskeleton; Endoplasmic Reticulum; F-actin-binding proteins; Funding; Grant; Guanosine Triphosphate Phosphohydrolases; Intermediate Filaments; Length; Membrane; Membrane Fusion; Modeling; N-terminal; National Center for Research Resources; Principal Investigator; Radiation; Recycling; Regulation; Research; Research Infrastructure; Resources; SNAP receptor; Signal Transduction; Source; Specificity; Structure; Transport Vesicles; United States National Institutes of Health; alpha catenin; base; cost; desmoplakin; link protein; programs; protein misfolding; protein structure; structural biology; synchrotron radiation

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. This program aims to determine the structures of proteins involved in cell membrane targeting, adhesion, and signaling, in order to establish the mechanism and specificity of their interactions. There are currently four projects with crystals that require synchrotron radiation. 1. Structure of full-length alpha-catenin, an F-actin binding protein that couples cadherin-based cell adhesion to regulation of the actin cytoskeleton. 2. The N-terminal domain of desmoplakin, a large protein that links desmosomal cadherins to intermediate filaments. 3. The Rab11 GTPase effector FIP3, involved in regulating targeting of recycling endosomal transport vesicles to the apical plasma membrane. 4. p97, a AAA+ ATPase responsible for removing misfolded proteins from the endoplasmic reticulum membrane, which also serves a model for the ATPase NSF responsible for disassembling SNARE complexes after membrane fusion.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 该计划旨在确定参与细胞膜靶向，粘附和信号传导的蛋白质的结构，以建立它们相互作用的机制和特异性。 目前有四个晶体项目需要同步辐射。 1.全长α-连环蛋白的结构，它是一种F-肌动蛋白结合蛋白，将钙粘蛋白基细胞粘附与肌动蛋白细胞骨架的调节偶联。 2.桥粒斑蛋白的N端结构域，桥粒斑蛋白是一种将桥粒钙粘蛋白连接到中间丝的大蛋白。 3. Rab 11 GT3效应因子FIP 3参与调节内体转运囊泡向顶端质膜的再循环靶向。 4. p97是一种AAA+ ATP酶，负责从内质网膜上去除错误折叠的蛋白质，它也是ATP酶NSF的模型，负责在膜融合后分解SNARE复合物。