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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

RANBP3  -  RAN binding protein 3

Homo sapiens

Synonyms: Ran-binding protein 3, RanBP3
 
 
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Disease relevance of RANBP3

  • Selection of some of the most suitable mRNAs (TMEM69, RANBP3 and PRSS22) that were assayed in blood samples from normal subjects and patients with colon cancer as possible markers for the presence of epithelial cells in the blood, using reverse transcription-polymerase chain reaction (RT-PCR) [1].
  • Binding assays using recombinant importin-alpha1, -alpha3, -alpha4, -alpha5, and -alpha7 revealed a preferential interaction of the RanBP3 NLS with importin-alpha3 and -alpha4, in contrast to the simian virus 40 T-antigen NLS, which interacted to similar extents with all of the isoforms [2].
 

High impact information on RANBP3

  • We present evidence that a conformational change of the Ran binding loop accounts for the cooperativity of Ran- and substrate binding and for the selective enhancement of CRM1-mediated export by the cofactor RanBP3 [3].
  • However, several residues essential for import via the c-Myc NLS are unnecessary in the RanBP3 NLS [2].
  • Nuclear import of the RanBP3 NLS was most efficient in the presence of importin-alpha3 [2].
  • This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable [4].
  • Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor [4].
 

Biological context of RANBP3

 

Physical interactions of RANBP3

 

Regulatory relationships of RANBP3

  • RanBP3 stimulates export by enhancing the affinity of Crm1 for Ran.GTP and cargo [4].

References

  1. Microarray-based identification and RT-PCR test screening for epithelial-specific mRNAs in peripheral blood of patients with colon cancer. Solmi, R., Ugolini, G., Rosati, G., Zanotti, S., Lauriola, M., Montroni, I., del Governatore, M., Caira, A., Taffurelli, M., Santini, D., Coppola, D., Guidotti, L., Carinci, P., Strippoli, P. BMC Cancer (2006) [Pubmed]
  2. RanBP3 contains an unusual nuclear localization signal that is imported preferentially by importin-alpha3. Welch, K., Franke, J., Köhler, M., Macara, I.G. Mol. Cell. Biol. (1999) [Pubmed]
  3. Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. Petosa, C., Schoehn, G., Askjaer, P., Bauer, U., Moulin, M., Steuerwald, U., Soler-López, M., Baudin, F., Mattaj, I.W., Müller, C.W. Mol. Cell (2004) [Pubmed]
  4. Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor. Nemergut, M.E., Lindsay, M.E., Brownawell, A.M., Macara, I.G. J. Biol. Chem. (2002) [Pubmed]
  5. RanBP3 enhances nuclear export of active (beta)-catenin independently of CRM1. Hendriksen, J., Fagotto, F., van der Velde, H., van Schie, M., Noordermeer, J., Fornerod, M. J. Cell Biol. (2005) [Pubmed]
  6. RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. Englmeier, L., Fornerod, M., Bischoff, F.R., Petosa, C., Mattaj, I.W., Kutay, U. EMBO Rep. (2001) [Pubmed]
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