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NUP88  -  nucleoporin 88kDa

Homo sapiens

Synonyms: 88 kDa nucleoporin, MGC8530, Nuclear pore complex protein Nup88, Nucleoporin Nup88
 
 
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Disease relevance of NUP88

  • Nup88 mRNA overexpression is associated with high aggressiveness of breast cancer [1].
  • Alterations of cellular proliferation proteins, such as p73, Nup88, Id1 and p27 have been considered to play critical roles in melanoma development [2].
  • Clinicopathological significance of Nup88 expression in patients with colorectal cancer [3].
  • RESULTS: The results showed that the intensity of Nup88 expression increased from the normal mucosa to the primary tumors (p < 0.0001) and tended to increase from the primary tumors to the metastases (p = 0.15) [3].
  • CONCLUSION: Based on our immunohistochemical data, HBV and HCV are unlikely to influence the expression of Nup88 in cirrhotic and neoplastic liver tissue, but point to an interaction of HBV with the nuclear pore in chronic hepatitis [4].
 

High impact information on NUP88

 

Biological context of NUP88

  • When cleavage is blocked by a point mutation, a minimal eight amino acids downstream of the cleavage site is sufficient to prevent most binding to either Nup96 or Nup88 [9].
  • The present results indicate that the role of Nup88 in cell differentiation and organ development could be fruitfully investigated using the developing chick embryo as an experimental model [10].
  • UVA enhanced protein expression concerning cell growth (p73 and Nup88) and UVB might over-express proteins concerning cellular proliferation (Id1 and p27) [2].
  • Nup88 expression was positively related to distal tumor location (p = 0.01), infiltrative growth pattern (p = 0.04) and higher proliferative activity (p = 0.04) and reversely to the grade of differentiation (p = 0.02) and apoptosis (p = 0.049) [3].
 

Anatomical context of NUP88

 

Associations of NUP88 with chemical compounds

 

Physical interactions of NUP88

  • Interestingly, the same site within Nup98 is involved in binding to both Nup88 and Nup96 [9].
 

Regulatory relationships of NUP88

 

Other interactions of NUP88

  • Here we show that Nup88 localizes midway between Nup358 and Nup214 and physically interacts with them [14].
  • AIM: To investigate the anticancer effects and the molecular mechanisms of deguelin on human U937 leukemia cells, and to explore the underlying mechanism regulating nucleoporin 98 (Nup98) and nucleoporin 88 (Nup88) in vitro [11].
 

Analytical, diagnostic and therapeutic context of NUP88

References

  1. Nup88 mRNA overexpression is associated with high aggressiveness of breast cancer. Agudo, D., Gómez-Esquer, F., Martínez-Arribas, F., Núñez-Villar, M.J., Pollán, M., Schneider, J. Int. J. Cancer (2004) [Pubmed]
  2. Ultraviolet A and B differently induce intracellular protein expression in human skin melanocytes--a speculation of separate pathways in initiation of melanoma. Zhang, H., Rosdahl, I. Carcinogenesis (2003) [Pubmed]
  3. Clinicopathological significance of Nup88 expression in patients with colorectal cancer. Emterling, A., Skoglund, J., Arbman, G., Schneider, J., Evertsson, S., Carstensen, J., Zhang, H., Sun, X.F. Oncology (2003) [Pubmed]
  4. Nucleoporin 88 expression in hepatitis B and C virus-related liver diseases. Knoess, M., Kurz, A.K., Goreva, O., Bektas, N., Breuhahn, K., Odenthal, M., Schirmacher, P., Dienes, H.P., Bock, C.T., Zentgraf, H., Zur Hausen, A. World J. Gastroenterol. (2006) [Pubmed]
  5. The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. Fornerod, M., van Deursen, J., van Baal, S., Reynolds, A., Davis, D., Murti, K.G., Fransen, J., Grosveld, G. EMBO J. (1997) [Pubmed]
  6. Nup214 is required for CRM1-dependent nuclear protein export in vivo. Hutten, S., Kehlenbach, R.H. Mol. Cell. Biol. (2006) [Pubmed]
  7. Overexpression of the nucleoporin CAN/NUP214 induces growth arrest, nucleocytoplasmic transport defects, and apoptosis. Boer, J., Bonten-Surtel, J., Grosveld, G. Mol. Cell. Biol. (1998) [Pubmed]
  8. The nuclear pore complex protein Nup88 is overexpressed in tumor cells. Martínez, N., Alonso, A., Moragues, M.D., Pontón, J., Schneider, J. Cancer Res. (1999) [Pubmed]
  9. Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes. Griffis, E.R., Xu, S., Powers, M.A. Mol. Biol. Cell (2003) [Pubmed]
  10. Developing chick embryos express a protein which shares homology with the nuclear pore complex protein Nup88 present in human tumors. Schneider, J., Linares, R., Martínez-Arribas, F., Moragues, M.D., Nuñez-Villar, M.J., Palomar, M.A., Pontón, J. Int. J. Dev. Biol. (2004) [Pubmed]
  11. Deguelin regulates nuclear pore complex proteins Nup98 and Nup88 in U937 cells in vitro. Liu, H.L., Chen, Y., Cui, G.H., Wu, Q.L., He, J., Chen, W.H., Zhou, J.F. Acta Pharmacol. Sin. (2005) [Pubmed]
  12. The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-kB/Rel/dorsal family transcription factor. Takano, H., Gusella, J.F. BMC neuroscience [electronic resource]. (2002) [Pubmed]
  13. Expression of p16, p27, p53, p73 and Nup88 proteins in matched primary and metastatic melanoma cells. Zhang, H., Schneider, J., Rosdahl, I. Int. J. Oncol. (2002) [Pubmed]
  14. Nup358/RanBP2 attaches to the nuclear pore complex via association with Nup88 and Nup214/CAN and plays a supporting role in CRM1-mediated nuclear protein export. Bernad, R., van der Velde, H., Fornerod, M., Pickersgill, H. Mol. Cell. Biol. (2004) [Pubmed]
 
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