PHOSPHORYLATION OF GAP JUNCTION PROTEINS

间隙连接蛋白的磷酸化

• 批准号: 2910306
• 负责人: PAUL D. LAMPE
• 金额: $ 23.73万
• 依托单位: FRED HUTCHINSON CANCER RESEARCH CENTER
• 依托单位国家: 美国
• 财政年份: 1997
• 资助国家: 美国
• 起止时间: 1997-05-01 至 2001-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2910306
• 关键词: Golgi apparatus; HeLa cells; SDS polyacrylamide gel electrophoresis; animal tissue; biological signal transduction; cell cell interaction; confocal scanning microscopy; endoplasmic reticulum; flow cytometry; gap junctions; high performance liquid chromatography; image processing; membrane channels; mitogen activated protein kinase; northern blottings; phosphorylation; protein biosynthesis; protein degradation; protein folding; protein kinase C; protein metabolism; restriction endonucleases; site directed mutagenesis; tissue /cell culture; western blottings

The general hypothesis to be tested is that phosphorylation of connexin43 and/or Cx45 regulates a variety of cellular functions. The experiments will address whether: (1) phosphorylation of Cx43 and Cx45 regulates the kinetics of connexin trafficking and/or oligomerization into connexons; (2) connexin phosphorylation regulates the intra- and intermembrane interactions that lead to gap junction channel formation; and (3) phosphorylation of Cx43 and Cx45 regulates gap junction degradation.

要测试的一般假设是 connexin43 的磷酸化 和/或Cx45调节多种细胞功能。 实验 将解决是否：(1) Cx43 和 Cx45 的磷酸化调节 连接蛋白运输和/或寡聚成连接子的动力学； (2) 连接蛋白磷酸化调节膜内和膜间 导致间隙连接通道形成的相互作用；和（3） Cx43 和 Cx45 的磷酸化调节间隙连接的降解。