PREDICTION OF TORC2 PHOSPHORYLATION SITES AND ASSOCIATED PROTEINS

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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.