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. cAMP-dependent protein kinase (PKA) is one of the simplest and best studied protein kinases which has broad substrate specificity. Using the N-terminal 39 residues of PKA catalytic subunit in a yeast two hybrid assay, we have identified a novel protein, A Kinase Interacting Protein (AKIP) which may interact with the catalytic subunit of PKA. We have raised various antibodies to AKIP including two against peptides as well as a polyclonal antibody to the full length protein. Immunohistochemistry and confocal microscopy were used this last year to begin to analyze the localization and function of this protein. The antibodies have been purified and proven to be specific for AKIP. We are beginning to use transfected and untransfected cultured cells as well as animal tissue slices to detect the sub-cellular localization of this protein as well as to elucidate its function. Our first goal will be to use confocal microscopy to confirm that AKIP1 and PKA catalytic subunit are co-localized within the cell.
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