ROLE OF HSP90 IN POLARIZED CELL MORPHOGENESIS IN SCEREVISIAE & C ALBICANS

HSP90 在酿酒酵母偏振细胞形态发生中的作用

• 批准号: 7381180
• 负责人: JILL L JOHNSON
• 金额: $ 10.31万
• 依托单位: UNIVERSITY OF IDAHO
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-06-01 至 2007-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7381180
• 关键词: ROLE; HSP90; POLARIZED; CELL; MORPHOGENESIS

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. The abundant cytoplasmic molecular chaperone Hsp90 and its co-chaperones are critical for the activity of steroid receptors, oncogenic tyrosine kinases and additional diverse proteins involved in signaling pathways and cell cycle control. Hsp90 and co-chaperones interact in an ATP-dependent pathway that facilitates the folding of substrate proteins to their native state. Hsp90 inhibitors have been shown to slow the ability of Candida albicans to develop drug resistance. A focus of our work is to characterize the interaction of Hsp90 with yeast-specific proteins, first in S. cerevisiae and then in C. albicans. We developed an assay that allows us to isolate native yeast Hsp90 complexes that contain both known co-chaperone proteins and novel presumed client proteins. Using peptide mass mapping we identified four novel Hsp90 interacting proteins and confirmed another interaction. In our efforts to determine how Hsp90 interacts with diverse client proteins, we will examine the interaction of Hsp90 and co-chaperones with these and other proteins in order to develop a more comprehensive picture of the in vivo mechanisms of the Hsp90 molecular machine.

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。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。列出的机构适用于该中心，这不一定是调查员的机构。丰富的细胞质分子伴侣HSP90及其辅助蛋白对于类固醇受体，致癌酪氨酸激酶以及参与信号通路和细胞周期控制的其他多种蛋白质至关重要。 HSP90和共伴侣在ATP依赖性途径中相互作用，该途径促进了底物蛋白向其天然状态的折叠。 HSP90抑制剂已被证明会减慢白色念珠菌发展耐药性的能力。我们工作的重点是表征Hsp90与酵母特异性蛋白的相互作用，首先是在酿酒酵母中，然后在白色念珠菌中。我们开发了一种使我们能够分离出包含已知共蛋白蛋白和新型推测客户蛋白的天然酵母HSP90复合物的测定法。使用肽质量映射，我们确定了四个新型的HSP90相互作用蛋白，并确认了另一种相互作用。为了确定HSP90如何与多样化的客户蛋白相互作用，我们将研究HSP90和辅助酮与这些蛋白质和其他蛋白质的相互作用，以便开发出HSP90分子机器人体内机制的更全面的图景。