IDENTIFICATION OF PROTEIN COMPLEXES AND PHOSPHORYLATION SITES OF PROTEINS

蛋白质复合物和蛋白质磷酸化位点的鉴定

• 批准号: 8171261
• 负责人: DANNEL MCCOLLUM
• 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/8171261
• 关键词: Binding; Complex; Computer Retrieval of Information on Scientific Projects Database; Cytokinesis; Fission Yeast; Funding; Grant; Homologous Gene; Human; Institution; Lead; Mass Spectrum Analysis; Mitosis; Pathway interactions; Phosphorylation; Phosphorylation Site; Phosphotransferases; Play; Proteins; Regulation; Research; Research Personnel; Resources; Role; Signal Pathway; Site; Source; Tumor Suppression; United States National Institutes of Health; Yeasts; protein complex

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 McCollum lab studies a signaling pathway in the fission yeast S. pombe, termed the septation initiation network (SIN), which functions at the end of mitosis to trigger initiation of cytokinesis. Most of the components of the SIN pathway have been identified, however their precise molecular interactions and the role phosphorylation plays in their regulation have not been determined. We have been using mass spectrometry to characterize molecular interactions among SIN components and identify sites of regulatory phosphorylation. These studies have focused on the Sid2-Mob1 kinase complex and a positive (Clp1) and negative regulator (Dma1) of the SIN. All of the components of this pathway are conserved in humans and function in cytokinesis and in tumor suppression. We have initiated studies to identify proteins that interact with the human homolog of Sid2, called Lats2. These studies should lead to a more comprehensive understanding of the SIN pathway in yeast, which we hope will help in the characterization of tumor suppression pathways in humans.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 麦科勒姆实验室研究了分裂酵母S.粟酒裂殖酵母，称为分隔起始网络（SIN），其在有丝分裂结束时起作用以触发胞质分裂的起始。SIN途径的大多数组分已经被鉴定，但是它们精确的分子相互作用和磷酸化在它们的调节中所起的作用尚未确定。 我们一直在使用质谱来表征SIN组分之间的分子相互作用，并确定调节磷酸化的位点。 这些研究集中在Sid 2-Mob 1激酶复合物和SIN的正调节因子（Clp 1）和负调节因子（Dma 1）上。该途径的所有组分在人类中是保守的，并且在胞质分裂和肿瘤抑制中起作用。我们已经启动了研究，以确定与Sid 2的人类同源物（称为Lats 2）相互作用的蛋白质。 这些研究应该导致对酵母中SIN途径的更全面的理解，我们希望这将有助于描述人类肿瘤抑制途径。