FORMINS AND NATIVE COMPLEXES: REGULATION AND FUNCTION

福尔明和天然复合物：调节和功能

• 批准号: 8171242
• 负责人: Bruce L Goode
• 金额: $ 0.24万
• 依托单位: UNIVERSITY OF WASHINGTON
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-09-01 至 2011-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8171242
• 关键词: Actins; Affect; Affinity; Animal Model; Architecture; Biochemical Genetics; Cell Polarity; Cells; Complex; Computer Retrieval of Information on Scientific Projects Database; Environment; Funding; Goals; Grant; Institution; Life; Ligands; Morphogenesis; Myosin ATPase; Pathway interactions; Proteins; Regulation; Research; Research Personnel; Resources; Saccharomyces cerevisiae; Source; United States National Institutes of Health; attenuation; cell growth; in vivo; polarized cell; protein complex; research study; tandem mass spectrometry

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Our goal is to understand how formin activities are regulated in vivo spatially and temporally. Given the potent effects formins have on actin assembly, they must be tightly controlled in the environment of a living cell. Our hypothesis is that through controlled local activation and attenuation of formins, their activities are harnessed to produce actin networks with highly specialized architectures and functions. What are these regulatory mechanisms? We are approaching this question using the model organism S. cerevisiae. The two S. cerevisiae formins Bni1 and Bnr1 assemble sets of highly dynamic actin cables, which in turn direct myosin-dependent polarized cell growth and morphogenesis. To elucidate the pathways controlling Bni1 and Bnr1 activities, we are using a set of affinity tags on known cell polarity factors and formin ligands to isolate the native protein complexes they form, and tandem mass spectrometry to identify the components of these complexes. In parallel, we are performing biochemical and genetic experiments to determine precisely how these proteins affect formin activities and contribute to cell polarity.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 我们的目标是了解如何在空间和时间上在体内调节形成活动。鉴于形式对肌动蛋白组件的有效作用，必须在活细胞的环境中严格控制它们。我们的假设是，通过控制局部的局部激活和衰减，它们的活动被利用以产生具有高度专业的体系结构和功能的肌动蛋白网络。这些监管机制是什么？我们正在使用模型生物体S. cerevisiae来解决这个问题。两种酿酒酵母formins BNI1和BNR1组装了高度动态的肌动蛋白电缆，进而导致依赖肌球蛋白依赖性的极化细胞生长和形态发生。为了阐明控制BNI1和BNR1活性的途径，我们在已知的细胞极性因子和formin配体上使用一组亲和力标签来隔离它们形成的天然蛋白质复合物，并串联质谱来识别这些复合物的成分。同时，我们正在进行生化和遗传实验，以确切确定这些蛋白质如何影响甲素活性并有助于细胞极性。