POST TRANSLATIONAL MODIFICATION OF RHOA

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 小分子GTP酶RhoA是细胞质分裂的关键开关蛋白。在最近的一系列实验中，我们发现异位表达的(和内源性的，程度较小的)RhoA是共价修饰的，并在SDS凝胶上以大约4kd的位移迁移到较慢的迁移形式。RhoA是额外修改的目标，其中许多修改提供了重要的见解。我们建议用质谱学来表征这一修饰。

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 small GTPase RhoA is a critical switch protein for cytokinesis. In a recent set of experiments, we found that ectopically expressed (and endogenous, to a lesser extent) RhoA is covalently modified and migrates with about a 4kd shift to a slower mobility form on a SDS gel. RhoA is a target for additional modifications and many of these have provided significant insight. We propose to characterize this modification by mass spectrometry.