Necdin interacts with the ribonucleoprotein hnRNP U in the nuclear matrix.

Necdin is expressed predominantly in terminally differentiated neurons, and its ectopic expression suppresses cell proliferation. We screened a cDNA library from neurally differentiated embryonal carcinoma P19 cells for necdin-binding proteins by the yeast two-hybrid assay. One of the positive clones contained cDNA encoding a carboxyl-terminal portion of heterogeneous nuclear ribonucleoprotein ...
U (hnRNP U), a nuclear matrix-associated protein that interacts with chromosomal DNA. We isolated cDNA encoding full-length mouse hnRNP U to analyze its physical and functional interactions with necdin. The necdin-binding site of hnRNP U was located near a carboxyl-terminal region that mediated the association between hnRNP U and the nuclear matrix. In postmitotic neurons, endogenously expressed necdin and hnRNP U were detected in the nuclear matrix and formed a stable complex. Ectopically expressed necdin was concentrated in the nucleoli, but coexpressed hnRNP U recruited necdin to the nucleoplasmic compartment of the nuclear matrix. Furthermore, under the same conditions necdin and hnRNP U cooperatively suppressed the colony formation of transfected SAOS-2 cells. These results suggest that necdin suppresses cell proliferation through its interaction with hnRNP U in the specific subnuclear structure.
Mesh Terms:
Animals, Binding Sites, Cell Division, Heterogeneous-Nuclear Ribonucleoprotein U, Heterogeneous-Nuclear Ribonucleoproteins, Mice, Microscopy, Fluorescence, Nerve Tissue Proteins, Neurons, Nuclear Matrix, Nuclear Proteins, Protein Structure, Tertiary, Protein Transport, Ribonucleoproteins, Tumor Cells, Cultured, Two-Hybrid System Techniques
J. Cell. Biochem.
Date: Jan. 29, 2002
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