STRUCTURE OF THE SIGMA ISOFORM OF THE PHOSPHOPEPTIDE-BINDING PROTEIN 14-3-3

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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. The seven mammalian isoforms of 14-3-3 family of proteins play diverse roles in intracellular signaling. Most 14-3-3 proteins form homodimers and mixed heterodimers between different isotypes, with overlapping roles in ligand binding. One mammalian isoform, 14-3-3 sigma, appears to play a unique role in the cellular response to DNA damage and in human oncogenesis. The biological and structural basis for these 14-3-3 sigma-specific functions is unknown. To understand the basis for preferential homodimerization of 14-3-3 sigma and to shed light on mechanisms of its unique functional specificity we have conducted biochemical and structural studies on the sigma isoform. The paper on this work was published in J. Biol. Chem.