Homodimerization of Cell Adhesion Protein CD44 Modulated by Palmitoylated Modifications and Membrane Environments
编号:52 访问权限:仅限参会人 更新:2021-08-03 19:13:27 浏览:710次 张贴报告

报告开始:2021年08月07日 15:40(Asia/Shanghai)

报告时间:20min

所在会场:[S2] Poster session [Po] Poster session

视频 无权播放 演示文件

提示:该报告下的文件权限为仅限参会人,您尚未登录,暂时无法查看。

摘要
The homodimerization of CD44 plays a key role in intercellular-to-extracellular signal transduction and tumor progression. Acylated modification and specific membrane environments have been reported to mediate translocation and oligomerization of CD44, however, the underlying molecular mechanism remains elusive. In this study, Martini coarse-grained dynamic simulations are performed to characterize the dimerization of palmitoylated CD44 variants in different bilayer environments. CD44 forms homodimer depending on transmembrane domains, and the dimerization efficiency and packing configurations are defected by palmitoylated modifications. In the presence of lipid raft, homodimerization of the palmitoylated CD44 is hardly observed, whereas PIP2 addition compensates to realize dimerization. The results unravel a delicate competitive relationship between PIP2 and palmitoylation in mediating protein homodimerization, which helps to clarify the inside-out signal transduction of CD44 likewise proteins.
关键词
CD44,Palmitoylated,Homodimerization,Membrane Environments
报告人
马子祎
学生 河北工业大学

稿件作者
孙夫德 河北工业大学
马子祎 河北工业大学
发表评论
验证码 看不清楚,更换一张
全部评论
重要日期
  • 会议日期

    08月06日

    2021

    08月09日

    2021

  • 08月09日 2021

    注册截止日期

主办单位
中国神经科学学会离子通道与受体分会
承办单位
河北工业大学
历届会议
移动端
在手机上打开
小程序
打开微信小程序
客服
扫码或点此咨询