B. Funke et al., THE MOUSE POLY (C)-BINDING PROTEIN EXISTS IN MULTIPLE ISOFORMS AND INTERACTS WITH SEVERAL RNA-BINDING PROTEINS, Nucleic acids research, 24(19), 1996, pp. 3821-3828
The murine poly(C)-binding protein (mCBP) was previously shown to belo
ng to the group of K-homology(KH) proteins by virtue of its homology t
o hnRNP-K. We have isolated cDNA-splice variants of mCBP which differ
by two variable regions of 93 bp and/or 39 +/- 3 bp respectively. Both
variable regions are located between the second and third KH-domain o
f mCBP. The characterization of a partial genomic clone enabled us to
propose a model for the generation of the second variable region by th
e use of a putative alternative spl ice signal. The mCBP mRNA is expre
ssed ubiquitously and the protein is found predominantly in the nucleu
s with the exception of the nucleoli. We have identified five proteins
which interact with mCBP in the yeast two hybrid system: mouse y-box
protein 1 (msy-1), y-box-binding protein, hnRNP-L, filamin and splicin
g factor 9G8. The interaction between mCBP and splicing factor 9G8 was
confirmed in vivo. These results suggest a function of mCBP in RNA me
tabolism.