RAF1 REGULATION BY O-GLCNAC MODIFICATION

O-GLNAC 修饰对 RAF1 的调节

• 批准号: 6138341
• 负责人: KEITH VOSSELLER
• 金额: $ 3.92万
• 依托单位: JOHNS HOPKINS UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-09-01 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/6138341
• 关键词: G protein; N acetylglucosamine; N acylation; binding sites; biological signal transduction; cell line; enzyme induction /repression; enzyme mechanism; glycoprotein structure; glycoproteins; immunoprecipitation; intracellular transport; mass spectrometry; phosphorylation; posttranslational modifications; protein kinase; protein localization; protein protein interaction; protein structure function; protein transport; protooncogene; site directed mutagenesis

O-GlcNAc addition to serines and threonines of cytosolic and nuclear proteins is a unique carbohydrate modification with no known function. This proposal addresses the potential for O-GlcNAc to be a dynamic switch mechanism controlling the functional states of proteins (analogous to regulated phosphorylation in signal transduction). In the context of signaling, the role of O-GlcNAc in regulating various functional aspects of Raf-1 will be examined. The potential for O-GlcNAc to regulate kinase activity or interaction of Raf-1 with key proteins such as Ras and 14-3-3 in a basal or inducible way will be studied.

O-GlcNAc 添加到胞质和核蛋白的丝氨酸和苏氨酸中是一种独特的碳水化合物修饰，其功能尚不清楚。该提案提出了 O-GlcNAc 作为控制蛋白质功能状态的动态开关机制的潜力（类似于信号转导中的调节磷酸化）。在信号传导方面，将检查 O-GlcNAc 在调节 Raf-1 的各个功能方面的作用。将研究 O-GlcNAc 以基础或诱导方式调节激酶活性或 Raf-1 与 Ras 和 14-3-3 等关键蛋白相互作用的潜力。