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The GTP-binding nuclear protein Ran (RAN) plays a crucial role in nuclear transport processes. Ran is a small GTPase that cycles between GTP-bound and GDP-bound states, regulating the directionality of nuclear transport [1]. In the GTP-bound state, Ran interacts with various effectors to facilitate nuclear import and export of proteins [2]. Ran-binding proteins such as NUP358/RanBP2 and RanBP1 are key regulators of Ran-dependent nuclear import and export, acting as docking sites for Ran in the GTP-bound state [3][4][5]. These proteins modulate the GTPase cycle of Ran, influencing its interactions with nuclear transport factors [6].
The asymmetric distribution of Ran in its GTP and GDP-bound states is essential for the proper functioning of nuclear transport. Proteins like RCC1, RanGAP1, and NTF2 work in concert with Ran to maintain this distribution, ensuring efficient nuclear protein import and export [7]. Ran also interacts with other factors like p97/β-karyopherin to facilitate the translocation steps of nuclear import [8]. Furthermore, Ran's nucleotide binding specificity is critical for its role in nuclear protein import, with mutations affecting its function in cell cycle progression [9][10].
References:
[1] M. Ren, A. Villamarin, A. Shih, E. Coutavas, M. Moore, M. Locurcioet al., "Separate domains of the ran gtpase interact with different factors to regulate nuclear protein import and rna processing", Molecular and Cellular Biology, vol. 15, no. 4, p. 2117-2124, 1995. https://doi.org/10.1128/mcb.15.4.2117
[2] S. Boor, P. Knyphausen, N. Kuhlmann, S. Wroblowski, J. Brenig, L. Scislowskiet al., "Small gtp-binding protein ran is regulated by posttranslational lysine acetylation", Proceedings of the National Academy of Sciences, vol. 112, no. 28, 2015. https://doi.org/10.1073/pnas.1505995112
[3] K. Carey, S. Richards, K. Lounsbury, & I. Macara, "Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the ran/tc4 gtpase mediates an essential function independent of nuclear protein import", The Journal of Cell Biology, vol. 133, no. 5, p. 985-996, 1996. https://doi.org/10.1083/jcb.133.5.985
[4] G. Murphy, M. Moore, G. Drivas, P. Ossa, A. Villamarin, P. D'Eustachioet al., "A t42a ran mutation: differential interactions with effectors and regulators, and defect in nuclear protein import", Molecular Biology of the Cell, vol. 8, no. 12, p. 2591-2604, 1997. https://doi.org/10.1091/mbc.8.12.2591
[5] K. Lounsbury and I. Macara, "Ran-binding protein 1 (ranbp1) forms a ternary complex with ran and karyopherin β and reduces ran gtpase-activating protein (rangap) inhibition by karyopherin β", Journal of Biological Chemistry, vol. 272, no. 1, p. 551-555, 1997. https://doi.org/10.1074/jbc.272.1.551
[6] B. Black, L. Levesque, J. Holaska, T. Wood, & B. Paschal, "Identification of an ntf2-related factor that binds ran-gtp and regulates nuclear protein export", Molecular and Cellular Biology, vol. 19, no. 12, p. 8616-8624, 1999. https://doi.org/10.1128/mcb.19.12.8616
[7] R. Baker, M. Harreman, J. Eccleston, A. Corbett, & M. Stewart, "Interaction between ran and mog1 is required for efficient nuclear protein import", Journal of Biological Chemistry, vol. 276, no. 44, p. 41255-41262, 2001. https://doi.org/10.1074/jbc.m106060200
[8] K. Lounsbury, S. Richards, R. Perlungher, & I. Macara, "Ran binding domains promote the interaction of ran with p97/β-karyopherin, linking the docking and translocation steps of nuclear import", Journal of Biological Chemistry, vol. 271, no. 5, p. 2357-2360, 1996. https://doi.org/10.1074/jbc.271.5.2357
[9] M. Ren, E. Coutavas, P. D'Eustachio, & M. Rush, "Effects of mutant ran/tc4 proteins on cell cycle progression.", Molecular and Cellular Biology, vol. 14, no. 6, p. 4216-4224, 1994. https://doi.org/10.1128/mcb.14.6.4216
[10] K. Weis, C. Dingwall, & A. Lamond, "Characterization of the nuclear protein import mechanism using ran mutants with altered nucleotide binding specificities.", The Embo Journal, vol. 15, no. 24, p. 7120-7128, 1996. https://doi.org/10.1002/j.1460-2075.1996.tb01103.x
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