Disease relevance of Nolc1

• Anisoosmotic regulation of the Nopp140 mRNA in H4IIE rat hepatoma cells and primary hepatocytes [1].

High impact information on Nolc1

• Nopp140 is a nucleolar phosphoprotein of 140 kd that we originally identified and purified as a nuclear localization signal (NLS)-binding protein [2].
• Indeed, Nopp140 is one of the most phosphorylated proteins in the cell, and NLS binding was dependent on phosphorylation [2].
• Immunofluorescence and immunogold electron microscopy with NAP57 specific antibodies show colocalization with Nopp140 to the dense fibrillar component of the nucleolus, to coiled bodies, and to the nucleoplasm [3].
• Immunogold staining in the nucleoplasm is occasionally seen in the form of curvilinear tracks between the nucleolus and the nuclear envelope, similar to those previously reported for Nopp140 [3].
• Using coimmunoprecipitation experiments, we show that the nucleolar and coiled-body protein Nopp140 interacts with both classes of snoRNPs [4].

Biological context of Nolc1

• Based on its subcellular location, its nuclear localization signal binding capacity, and its shuttling between the nucleolus and the cytoplasm, Nopp140 was proposed to function as a chaperone in ribosome biogenesis [5].
• Nopp140 is a nuclear localisation signal binding protein that shuttles on curvilinear tracks between the nucleolus and the cytoplasm [6].
• Because Nopp140 is involved in the regulation of transcriptional activity it could play a role in the osmosignalling pathway towards gene expression in H4IIE cells and hepatocytes [1].

Anatomical context of Nolc1

• Hyperosmotic incubation increased Nopp140 mRNA levels in H4IIE cells but not in hepatocytes [1].

Analytical, diagnostic and therapeutic context of Nolc1

• Using the differential display polymerase chain reaction osmosensitive regulation of mRNA levels of the nucleolar phosphoprotein of 140 kDa (Nopp140) was found in H4IIE rat hepatoma cells [1].

References