Disease relevance of Nup210

• We conclude that the bovine coronavirus is comprised of four major structural proteins, gp190 (normally present as 120- and 100-kilodalton subunits), gp140, pp52, and gp26 [1].
• The mouse hepatitis coronavirus A59 has an antigenically homologous counterpart to only three of these proteins: gp190, pp52 and gp26 [1].

High impact information on Nup210

• POM121 and gp210 were, until this point, the only known membrane-integral nucleoporins (Nups) of vertebrates and, thus, the only candidate anchors for nuclear pore complexes (NPCs) within the nuclear membrane [2].
• Using immunofluorescence staining and confocal microscopy, we compared the localization of two inner nuclear membrane proteins (laminaassociated polypeptides 1 and 2 [LAP1 and LAP2]) and a nuclear pore membrane protein (gp210) to the distribution of bulk ER membranes, which was determined with lipid dyes (DiOC6 and R6) and polyclonal antibodies [3].
• The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope [4].
• A mouse monoclonal IgG directed against an epitope in the lumenal domain of rat gp210 was expressed in cultured rat cells by microinjection of mRNA prepared from a hybridoma cell line [5].
• To locate determinants for sorting of gp210 to the pore membrane, we constructed various cDNAs coding for wild-type, mutant, and chimeric gp210, and monitored localization of the expressed protein in 3T3 cells by immunofluorescence microscopy using appropriate antibodies [4].

Biological context of Nup210

• However, here we demonstrate cell-type specific expression of the gp210 protein during mouse organogenesis [6].
• The deduced 1886 amino acid sequence shows a 95% identity to the sequence of rat gp210 [7].
• The specific receptor for LIF, gp190, binds this cytokine with low affinity and is also required for signal transduction [8].
• Recombinant S protein was synthesized as an endo-beta-N-acetylglucosaminidase H (Endo H)-sensitive glycoprotein with high mannose simple oligosaccharides (gp 190) that underwent post-translational modification to an Endo H-resistant glycoprotein with complex oligosaccharides (gp210) [9].

Anatomical context of Nup210

• The nuclear pore membrane glycoprotein 210 (POM210/gp210) is considered to be important for the assembly and structure of pore complexes in metazoan cells [6].
• In four cultured mouse cell lines, gp210 mRNA and protein were below detection levels, in contrast to some other nucleoporins tested [6].
• To test this hypothesis, we have investigated dynamic properties of the NPC and distribution of NPC proteins in NIH/3T3 cells lacking gp210 [10].
• In this study, we initially showed that transport of LIF is mediated by its specific receptor LIFRalpha (gp190), using both adult mice and monolayers of mouse brain microvessel endothelial cells [11].

Associations of Nup210 with chemical compounds

• Polyproline type II conformation in the C-terminal domain of the nuclear pore complex protein gp210 [12].
• We have developed an ELISA which detects, with high specificity, antibodies against a major surface protein of P. falciparum merozoites which is a processing product of the precursor glycoprotein gp190 [13].
• In vitro, BCH-1868 inhibited the proliferation of several murine and human cancer cell lines with IC50s in the microM range independently of the tissue type or the presence of multidrug resistance protein MRP/gp190 [14].

Analytical, diagnostic and therapeutic context of Nup210

• Because gp190 comprises two hematopoietin binding domains, crude epitope mapping was possible using the same reagents [15].

References