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In the present review, the subcellular localization, structural features, mutations within bclaf1 will be described, then the regulation of bclaf1 and its downstream targets will be analyzed

Furthermore, the different roles and possible mechanisms of bclaf1 in tumorigenesis will also be highlighted and discussed. Subsequently, employing coimmunoprecipitation and immunofluorescence, we validated the reciprocal interaction between bclaf1 and cullin 3 (cul3), through which bclaf1 actively upregulates the ubiquitination and degradation of phd2. Intriguingly, the targetome includes bclaf1 of which transcription is activated. Furthermore, by immunohistochemistry, immunofluorescence, and proximity ligation assay, bclaf1 was shown to colocalize (figure 4b) and associate (figure 4c) with bcl2, both in normal media and in plaques, particularly in the fibrous cap region.

Bclaf1 was originally identified as a protein that interacts with antiapoptotic members of the bcl2 family Initial studies indicated a role for this protein as an inducer of apoptosis and. (b) immunofluorescence was used to determine the subcellular locations of bclaf1 and ythdf2 in kyse150 and ec109 cells, with dapi for nuclear staining

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