Biology:Importin subunit alpha-4
Generic protein structure example |
Importin subunit alpha-4 also known as karyopherin subunit alpha-3 is a protein that in humans is encoded by the KPNA3 gene.[1][2]
The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60–100 proteins and is probably 120 million daltons in molecular size. Small molecules (up to 70 kD) can pass through the nuclear pore by nonselective diffusion; larger molecules are transported by an active process. Most nuclear proteins contain short basic amino acid sequences known as nuclear localization signals (NLSs). KPNA3, encodes a protein similar to certain nuclear transport proteins of Xenopus and human. The predicted amino acid sequence shows similarity to Xenopus importin, yeast SRP1, and human RCH1 (KPNA2), respectively. The similarities among these proteins suggests that karyopherin alpha-3 may be involved in the nuclear transport system.[3]
Interactions
KPNA3 has been shown to interact with KPNB1.[2][4]
References
- ↑ "Isolation and mapping of karyopherin alpha 3 (KPNA3), a human gene that is highly homologous to genes encoding Xenopus importin, yeast SRP1 and human RCH1". Cytogenet Cell Genet 76 (1–2): 87–93. Jun 1997. doi:10.1159/000134521. PMID 9154134.
- ↑ 2.0 2.1 "Cloning and characterization of hSRP1 gamma, a tissue-specific nuclear transport factor". Proc Natl Acad Sci U S A 95 (2): 582–7. Feb 1998. doi:10.1073/pnas.95.2.582. PMID 9435235. Bibcode: 1998PNAS...95..582N.
- ↑ "Entrez Gene: KPNA3 karyopherin alpha 3 (importin alpha 4)". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3839.
- ↑ Köhler, M; Speck C; Christiansen M; Bischoff F R; Prehn S; Haller H; Görlich D; Hartmann E (Nov 1999). "Evidence for distinct substrate specificities of importin alpha family members in nuclear protein import". Mol. Cell. Biol. (UNITED STATES) 19 (11): 7782–91. doi:10.1128/mcb.19.11.7782. ISSN 0270-7306. PMID 10523667. PMC 84838. http://pubman.mpdl.mpg.de/pubman/item/escidoc:1922685/component/escidoc:1922686/1922685.pdf.
Further reading
- "HIV-1 nuclear import: in search of a leader". Front. Biosci. 2 (4): d578–87. 2004. doi:10.2741/A213. PMID 9366553.
- "HIV-1 nuclear import: matrix protein is back on center stage, this time together with Vpr". Mol. Med. 4 (3): 138–43. 1998. doi:10.1007/BF03401911. PMID 9562972.
- "Active nuclear import of human immunodeficiency virus type 1 preintegration complexes". Proc. Natl. Acad. Sci. U.S.A. 89 (14): 6580–4. 1992. doi:10.1073/pnas.89.14.6580. PMID 1631159. Bibcode: 1992PNAS...89.6580B.
- "p17 and p17-containing gag precursors of input human immunodeficiency virus are transported into the nuclei of infected cells". AIDS Res. Hum. Retroviruses 7 (3): 303–6. 1991. doi:10.1089/aid.1991.7.303. PMID 2064827.
- "Mutational analysis of cell cycle arrest, nuclear localization and virion packaging of human immunodeficiency virus type 1 Vpr". J. Virol. 69 (12): 7909–16. 1996. doi:10.1128/JVI.69.12.7909-7916.1995. PMID 7494303.
- "HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase". Cell 83 (4): 569–76. 1995. doi:10.1016/0092-8674(95)90097-7. PMID 7585960.
- "Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection". J. Virol. 69 (6): 3949–54. 1995. doi:10.1128/JVI.69.6.3949-3954.1995. PMID 7745752.
- "HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is a key regulator". Cell 80 (3): 379–88. 1995. doi:10.1016/0092-8674(95)90488-3. PMID 7859280.
- "The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infection in macrophages and quiescent T lymphocytes". Proc. Natl. Acad. Sci. U.S.A. 91 (15): 6992–6. 1994. doi:10.1073/pnas.91.15.6992. PMID 8041734. Bibcode: 1994PNAS...91.6992V.
- "The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells". Proc. Natl. Acad. Sci. U.S.A. 91 (15): 7311–5. 1994. doi:10.1073/pnas.91.15.7311. PMID 8041786. Bibcode: 1994PNAS...91.7311H.
- "A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells". Nature 365 (6447): 666–9. 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. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Nuclear localization signal of HIV-1 as a novel target for therapeutic intervention". Mol. Med. 1 (2): 217–30. 1996. doi:10.1007/BF03401569. PMID 8529100.
- "Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import". J. Virol. 70 (2): 1027–32. 1996. doi:10.1128/JVI.70.2.1027-1032.1996. PMID 8551560.
- "Phosphorylation-dependent human immunodeficiency virus type 1 infection and nuclear targeting of viral DNA". Proc. Natl. Acad. Sci. U.S.A. 93 (1): 367–71. 1996. doi:10.1073/pnas.93.1.367. PMID 8552640. Bibcode: 1996PNAS...93..367B.
- "Evidence for direct association of Vpr and matrix protein p17 within the HIV-1 virion". Virology 220 (1): 208–12. 1996. doi:10.1006/viro.1996.0302. PMID 8659115.
- "Critical role of reverse transcriptase in the inhibitory mechanism of CNI-H0294 on HIV-1 nuclear translocation". Proc. Natl. Acad. Sci. U.S.A. 93 (21): 11859–64. 1996. doi:10.1073/pnas.93.21.11859. PMID 8876228. Bibcode: 1996PNAS...9311859P.
- "Phosphorylation of residue 131 of HIV-1 matrix is not required for macrophage infection". Cell 88 (2): 171–3; discussion 173–4. 1997. doi:10.1016/S0092-8674(00)81836-X. PMID 9008157.
- "HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway". Proc. Natl. Acad. Sci. U.S.A. 94 (18): 9825–30. 1997. doi:10.1073/pnas.94.18.9825. PMID 9275210. Bibcode: 1997PNAS...94.9825G.
