Optimized method for isolation of immature intracytoplasmic retroviral particles from mammalian cells

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.

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Various AKIP1 Expression Levels Affect Its Subcellular Localization but Have no Effect on NF-κB Activation

Keprová

Kořínková

Křížová

et al. 2019

Physiol Res

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Optimized method for isolation of immature intracytoplasmic retroviral particles from mammalian cells

Cited by 1 publication

References 33 publications

Various AKIP1 Expression Levels Affect Its Subcellular Localization but Have no Effect on NF-κB Activation

Various AKIP1 Expression Levels Affect Its Subcellular Localization but Have no Effect on NF-κB Activation

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