RNA Binding Motif Protein 42 (RBM42)

Rat Rbm42 interacted with human HNRNPK, and mutation analyses revealed that the C-terminal RRM of Rbm42 interacted with the C-terminal KH domain of HNRNPK. Epitope-tagged and endogenous human RBM42 isoforms and HNRNPK coimmunoprecipitated in reciprocal reactions using HEK293 and HeLa cell lysates, and both RBM42 and HNRNPK also independently bound RNA. The isolated C-terminal domains of human RBM42 and HNRNPK interacted in vitro. In vivo, however, RNA appeared to mediate the association of the full-length proteins, since RNase treatment disrupted their interaction. Immunofluorescence microscopy revealed that both proteins predominantly localized in the nucleus of MTD-1A mouse mammary tumor cells.