Biology:IPO5
 Generic protein structure example |
Importin-5 is a protein that in humans is encoded by the IPO5 gene.[1][2][3] The protein encoded by this gene is a member of the importin beta family. Structurally, the protein adopts the shape of a right hand solenoid and is composed of 24 HEAT repeats.[4]
Function
Nuclear transport, a signal- and energy-dependent process, takes place through nuclear pore complexes embedded in the nuclear envelope. The import of proteins containing a nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in the cytoplasm and importin beta docks the complex at the cytoplasmic side of the nuclear pore complex. In the presence of nucleoside triphosphates and the small GTP binding protein Ran, the complex moves into the nuclear pore complex and the importin subunits dissociate. Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex.[5]
IPO5 facilitates cytoplasmic polyadenylation element-binding protein (CPEB)3 translocation by binding to RRM1 motif of CPEB3 in neurons. NMDAR signaling increases RanBP1 expression and reduces the level of cytoplasmic GTP-bound Ran. These changes enhance CPEB3–IPO5 interaction, which consequently accelerates the nuclear import of CPEB3 and promotes its nuclear function.[6]
References
- ↑ "Cloning and characterization of human karyopherin beta3". Proceedings of the National Academy of Sciences of the United States of America 94 (9): 4451–6. April 1997. doi:10.1073/pnas.94.9.4451. PMID 9114010. Bibcode: 1997PNAS...94.4451Y.
- ↑ "Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts differently with RanBP1". Molecular and Cellular Biology 17 (9): 5087–96. September 1997. doi:10.1128/mcb.17.9.5087. PMID 9271386.
- ↑ "Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex". Journal of Virology 80 (24): 11911–9. December 2006. doi:10.1128/JVI.01565-06. PMID 17005651.
- ↑ "X-ray Structure of the Human Karyopherin RanBP5, an Essential Factor for Influenza Polymerase Nuclear Trafficking". Journal of Molecular Biology 432 (10): 3353–3359. May 2020. doi:10.1016/j.jmb.2020.03.021. PMID 32222384. https://hal.univ-grenoble-alpes.fr/hal-02555361/file/Swale%20et%20al.%20JMB.pdf.
- ↑ "Entrez Gene: RANBP5 RAN binding protein 5". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3843.
- ↑ "NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3". Nucleic Acids Research 40 (17): 8484–98. September 2012. doi:10.1093/nar/gks598. PMID 22730302.
Further reading
- "HIV-1 nuclear import: in search of a leader". Frontiers in Bioscience 2 (4): d578-87. December 1997. doi:10.2741/A213. PMID 9366553.
- "HIV-1 nuclear import: matrix protein is back on center stage, this time together with Vpr". Molecular Medicine 4 (3): 138–43. March 1998. doi:10.1007/BF03401911. PMID 9562972.
- "Nuclear targeting of proteins: how many different signals?". Cellular Signalling 12 (5): 337–41. May 2000. doi:10.1016/S0898-6568(00)00077-2. PMID 10822175.
- "Karyopherins and nuclear import". Current Opinion in Structural Biology 11 (6): 703–15. December 2001. doi:10.1016/S0959-440X(01)00264-0. PMID 11751052.
- "Active nuclear import of human immunodeficiency virus type 1 preintegration complexes". Proceedings of the National Academy of Sciences of the United States of America 89 (14): 6580–4. July 1992. doi:10.1073/pnas.89.14.6580. PMID 1631159. Bibcode: 1992PNAS...89.6580B.
- "A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells". Nature 365 (6447): 666–9. October 1993. doi:10.1038/365666a0. PMID 8105392. Bibcode: 1993Natur.365..666B.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. September 1996. doi:10.1101/gr.6.9.791. PMID 8889548.
- "HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway". Proceedings of the National Academy of Sciences of the United States of America 94 (18): 9825–30. September 1997. doi:10.1073/pnas.94.18.9825. PMID 9275210. Bibcode: 1997PNAS...94.9825G.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta". Journal of Molecular Biology 274 (5): 693–707. December 1997. doi:10.1006/jmbi.1997.1420. PMID 9405152.
- "The HIV-1 Tat nuclear localization sequence confers novel nuclear import properties". The Journal of Biological Chemistry 273 (3): 1623–8. January 1998. doi:10.1074/jbc.273.3.1623. PMID 9430704.
- "HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection". Genes & Development 12 (2): 175–85. January 1998. doi:10.1101/gad.12.2.175. PMID 9436978.
- "Viral protein R regulates nuclear import of the HIV-1 pre-integration complex". The EMBO Journal 17 (4): 909–17. February 1998. doi:10.1093/emboj/17.4.909. PMID 9463369.
- "Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex". The Journal of Biological Chemistry 273 (21): 13347–52. May 1998. doi:10.1074/jbc.273.21.13347. PMID 9582382.
- "Interaction of the human immunodeficiency virus type 1 Vpr protein with the nuclear pore complex". Journal of Virology 72 (7): 6004–13. July 1998. doi:10.1128/JVI.72.7.6004-6013.1998. PMID 9621063.
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