{{Short description|Protein-coding gene in the species Homo sapiens}} {{Infobox gene}}
'''Nuclear pore glycoprotein-210''' (gp210) is an essential trafficking regulator in the eukaryotic nuclear pore complex. Gp-210 anchors the pore complex to the nuclear membrane.<ref name="pmid2184032">{{cite journal |vauthors=Greber UF, Senior A, Gerace L | title = A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail | journal = EMBO J. | volume = 9 | issue = 5 | pages = 1495–502 | year = 1990 | pmid = 2184032 | doi = 10.1002/j.1460-2075.1990.tb08267.x| pmc = 551841 }}</ref> and protein tagging reveals its primarily located on the luminal side of double layer membrane at the pore. A single polypeptide motif of gp210 is responsible for sorting to nuclear membrane,<ref name="pmid1281815">{{cite journal |vauthors=Wozniak RW, Blobel G | title = The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope | journal = J. Cell Biol. | volume = 119 | issue = 6 | pages = 1441–9 | year = 1992 | pmid = 1281815 | doi =10.1083/jcb.119.6.1441 | pmc = 2289754 }}</ref> and indicate the carboxyl tail of the protein is oriented toward the cytoplasmic side of the membrane.
==Disassembly and Assembly== During eukaryotic mitosis the nuclear envelope disintegrates into vesicles dispersing nuclear lamina proteins and nuclear pore complexes. Nup210 is specifically phosphorylated on the C-terminal (cytoplasmic) domain in mitosis at Ser1880<ref name="pmid8672508">{{cite journal |vauthors=Favreau C, Worman HJ, Wozniak RW, Frappier T, Courvalin JC | title = Cell cycle-dependent phosphorylation of nucleoporins and nuclear pore membrane protein Gp210 | journal = Biochemistry | volume = 35 | issue = 24 | pages = 8035–44 | year = 1996 | pmid = 8672508 | doi = 10.1021/bi9600660}}</ref> and is dispersed throughout the endoplasmic reticulum during mitosis as homodimers.<ref name="pmid11453980">{{cite journal |vauthors=Favreau C, Bastos R, Cartaud J, Courvalin JC, Mustonen P | title = Biochemical characterization of nuclear pore complex protein gp210 oligomers | journal = Eur. J. Biochem. | volume = 268 | issue = 14 | pages = 3883–9 | year = 2001 | pmid = 11453980 | doi =10.1046/j.1432-1327.2001.02290.x | doi-access = free }}</ref> Nuclear lamins begin to reassemble around chromosomes at the end of mitosis.<ref name="pmid9182656">{{cite journal |vauthors=Yang L, Guan T, Gerace L | title = Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis | journal = J. Cell Biol. | volume = 137 | issue = 6 | pages = 1199–210 | year = 1997 | pmid = 9182656 | doi =10.1083/jcb.137.6.1199 | pmc = 2132536 }}</ref> Nup210 lags the reassembly process relative to other Nups.<ref name="pmid10362555">{{cite journal |vauthors=Bodoor K, Shaikh S, Salina D, etal | title = Sequential recruitment of NPC proteins to the nuclear periphery at the end of mitosis | journal = J. Cell Sci. | volume = 112 | issue = 13| pages = 2253–64 | year = 1999 | doi = 10.1242/jcs.112.13.2253 | pmid = 10362555 }}</ref> and while much of the assembly process can occur without it, the final assembly and dilation of the complexes require Nup210.<ref name="pmid14517331">{{cite journal |vauthors=Cohen M, Feinstein N, Wilson KL, Gruenbaum Y | title = Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans | journal = Mol. Biol. Cell | volume = 14 | issue = 10 | pages = 4230–7 | year = 2003 | pmid = 14517331 | doi = 10.1091/mbc.E03-04-0260 | pmc = 207014}}</ref> The replacement of serine at position 1880 with a phosphorylated 'looking' glutamate results in Nup210 complexes that fail to reassemble indicating that dephosphorylation of Nup210 within the final phases of proper assembly is required.<ref name="pmid17559836">{{cite journal |vauthors=Onischenko EA, Crafoord E, Hallberg E | title = Phosphomimetic mutation of the mitotically phosphorylated serine 1880 compromises the interaction of the transmembrane nucleoporin gp210 with the nuclear pore complex | journal = Exp. Cell Res. | volume = 313 | issue = 12 | pages = 2744–51 | year = 2007 | pmid = 17559836 | doi = 10.1016/j.yexcr.2007.05.011| hdl = 10616/41278 | hdl-access = free }}</ref>
==Pathology== Recognized by anti-nuclear antibodies found in primary biliary cirrhosis (PBC) anti-Nup210 antibodies correlate with progression toward end stage liver disease. Nup210 is possibly a destructive autoimmune target of the disease. One idea for the loss of tolerance is the increased or abnormal expression of Nup210 in patients with PBC.<ref name="pmid16337775">{{cite journal |vauthors=Nakamura M, Takii Y, Ito M, etal | title = Increased expression of nuclear envelope gp210 antigen in small bile ducts in primary biliary cirrhosis | journal = J. Autoimmun. | volume = 26 | issue = 2 | pages = 138–45 | year = 2006 | pmid = 16337775 | doi = 10.1016/j.jaut.2005.10.007}}</ref>
Anti-mitochondrial, anti-centromere and anti-nup62 are also found in PBC.
==References== {{reflist}}
{{Autoantigens}}
{{DEFAULTSORT:Nucleoporin 210kda}} Category:Autoantigens Category:Glycoproteins Category:Membrane proteins Category:Nuclear pore complex