A-kinase interacting protein 1 (AKIP1) has been shown to interact
with a broad range of proteins involved in various cellular
processes, including apoptosis, tumorigenesis, and oxidative
stress suggesting it might have multiple cellular functions. In this
study, we used an epitope-tagged AKIP1 and by combination of
immunochemical approaches, microscopic methods and reporter
assays we studied its properties. Here, we show that various
levels of AKIP1 overexpression in HEK-293 cells affected not only
its subcellular localization but also resulted in aggregation. While
highly expressed AKIP1 accumulated in electron-dense
aggregates both in the nucleus and cytosol, low expression of
AKIP1 resulted in its localization within the nucleus as a free,
non-aggregated protein. Even though AKIP1 was shown to
interact with p65 subunit of NF-κB and activate this transcription
factor, we did not observe any effect on NF-κB activation
regardless of various AKIP1 expression level.