PREDICTION OF TORC2 PHOSPHORYLATION SITES AND ASSOCIATED PROTEINS

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。 在以前的研究中，我们的特点是一个家庭的CREB辅激活剂被称为换能器的调节CREB活性（TORCs）。三个TORC家族成员共享高度保守的N-末端卷曲螺旋结构域，其介导与CREB的bZIP结构域的直接关联。在没有信号的情况下，TORC 2作为潜在的共激活剂存在于细胞质中，并响应cAMP和钙信号而被输入到细胞核中。 TORC 2的穿梭是由相反的信号调节激酶和磷酸酶活性以及通过与14-3-3蛋白的相互作用来控制的。最近的研究发现TORC 2与细胞骨架和内质网有关，但还不清楚它们的具体作用。这项合作的目的是确定组成和调节的磷酸化位点内Torc 2的影响其细胞质/核穿梭，并确定相关的蛋白质在细胞骨架和内质网使用质谱。

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. In previous studies, we characterized a family of CREB coactivators referred to as transducers of regulated CREB activity (TORCs). The three TORC family members share a highly conserved N-terminal coiled-coil domain that mediates a direct association with the bZIP domain of CREB. In the absence of signal, TORC2 resides in the cytoplasm as a latent co-activator and is imported into the nucleus in response to cAMP and calcium signals. TORC2 shuttling is controlled by opposing signal regulated kinase and phosphatase activites and through an interaction with 14-3-3 proteins. In recent study, we found TORC2 is associated with cytoskeleton and endoplasmic reticulum, although we do not know their exact roles. The purpose of this collaboration is to identify constitutive and regulated phosphorylation sites within Torc2 that effect its cytoplasmic/nuclear shuttling and to identify the associated proteins in cytoskeleton and endoplasmic reticulum using mass spectrometry.