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. 1996 Oct 1;24(19):3821–3828. doi: 10.1093/nar/24.19.3821

The mouse poly(C)-binding protein exists in multiple isoforms and interacts with several RNA-binding proteins.

B Funke 1, B Zuleger 1, R Benavente 1, T Schuster 1, M Goller 1, J Stévenin 1, I Horak 1
PMCID: PMC146158  PMID: 8871564

Abstract

The murine poly(C)-binding protein (mCBP) was previously shown to belong to the group of K-homology (KH) proteins by virtue of its homology to 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 of mCBP. The characterization of a partial genomic clone enabled us to propose a model for the generation of the second variable region by the use of a putative alternative splice signal. The mCBP mRNA is expressed ubiquitously and the protein is found predominantly in the nucleus 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 splicing factor 9G8. The interaction between mCBP and splicing factor 9G8 was confirmed in vivo. These results suggest a function of mCBP in RNA metabolism.

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Selected References

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