High impact information on Hnrpc

• The hnRNP C1 and C2 proteins are among the most abundant proteins in the nucleus, and as ubiquitous components of RNP complexes, they have been implicated in many aspects of mRNA biogenesis [1].
• However, hnRNP C1 and C2 are not required for cell viability [1].
• Pretreatment of endothelial cells with the protein kinase CK1-specific inhibitor IC261 prevented the H(2)O(2)-stimulated phosphorylation of hnRNP-C [2].
• Protein kinase CK1alpha immunoprecipitated from primary human endothelial cell nuclei also phosphorylated the ACD of hnRNP-C at these positions [2].
• Utilizing phosphoserine-mimicking Ser-to-Glu point mutations, the effects of phosphorylation on hnRNP-C function were investigated by quantitative equilibrium fluorescence RNA binding analyses [2].

Biological context of Hnrpc

• hnRNP C is required for postimplantation mouse development but Is dispensable for cell viability [1].
• Wild-type hnRNP-C1 and hnRNP-C1 modified at the basal sites of phosphorylation (S247E and S286E) both avidly bound RNA with similar binding constants [2].
• By using nuclear yellow fluorescent protein (YFP) fusion, we determined that the C-terminal 40-amino-acid region of hnRNP C1/C2 is a novel nuclear export signal responsive to ROCK-activation [3].

Anatomical context of Hnrpc

• Short interfering RNA-mediated gene-specific knockdown of CUGBP2, GRY-RBP, and hnRNP-C1 resulted in increased editing in Caco-2 cells, consistent with their known inhibitory function [4].

Associations of Hnrpc with chemical compounds

• In primary human endothelial cells, low concentrations of H(2)O(2) stimulated the rapid phosphorylation of the acidic C-terminal domain (ACD) of heterogeneous nuclear ribonucleoprotein C (hnRNP-C), a nuclear restricted pre-mRNA-binding protein, at Ser(240) and at Ser(225)-Ser(228) [2].
• Intron sequences and the length of the downstream second exon affect the binding of hnRNP C proteins in an in vitro splicing reaction [5].

Other interactions of Hnrpc

• The C-terminal region is more divergent between hnRNP C and Raly [6].
• Following the variable region, a basic region and a leucine zipper are conserved in all hnRNP C-related proteins including mouse and human Raly [6].

Analytical, diagnostic and therapeutic context of Hnrpc

• Immunoprecipitation suggested that these proteins may be the heteronuclear proteins hnRNPC1/C2 [7].

References