The lamin B receptor (p58) is an inner nuclear membrane protein that forms an in vivo complex with the nuclear lamins, a nuclear envelope kinase, and two other nuclear proteins with apparentM r of 18,000 (p18) and 34,000 (p34). We now report the isolation of p34 by partial dissociation of the immunoaffinity-purified p58 protein complex. Determination of the N-terminal amino acid sequence of purified p34 shows that this polypeptide is homologous to p32, a splicing factor 2 (SF2)-associated protein. The relatedness between p34 and p32 can be further established by showing that antibodies raised against N- and C-terminal peptides of p32 cross-react with purified p34. As the amino acid sequence of p58 contains an arginine/serine (RS)-rich region similar to the RS-rich region found in SF 2, we speculate that these domains provide binding sites for p34 and that this protein may be a linker between the nuclear membrane and intranuclear spliceosomal substructures.
