Nuclear transport and transcription

Current Opinion in Cell Biology

Volumn 12, Issue 3, 2000, Pages 355-360

  Komeili, Arash ^a   O'Shea, Erin K ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN P53; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR;

EUKARYOTE; INTRACELLULAR TRANSPORT; NONHUMAN; PRIORITY JOURNAL; REVIEW; TRANSCRIPTION REGULATION;

EID: 0034061186     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00100-9     Document Type: Review

References (24)

1. Ohno M., Fornerod M., Mattaj I.W. Nucleocytoplasmic transport: the last 200 nanometers. Cell. 92:1998;327-336. A very well written and comprehensive review of nuclear transport. This review describes the role of karyopherins and Ran in nuclear transport and contains many references to the original work and other reviews.
2. Turpin P., Ossareh-Nazari B., Dargemont C. Nuclear transport and transcriptional regulation. FEBS Lett. 452:1999;82-86.
3. Fornerod M., Ohno M., Yoshida M., Mattaj I.W. Crm1 is an export receptor for leucine-rich nuclear export signals. Cell. 90:1997;1051-1060.
4. Pemberton L.F., Rosenblum J.S., Blobel G. Nuclear import of the TATA binding protein: mediation by karyopherin Kap114 and a possible mechanism for intranuclear targeting. J Cell Biol. 145:1999;1407-1417. Kap114 is identified as the import receptor for TBP. The authors show that the RanGTP-mediated dissociation of TBP from Kap114 is stimulated by TATA DNA and TFIIA. They conclude that TBP import might be terminated at promoters.
5. Morehouse H., Buratowski R.M., Silver P.A., Buratowski S. The importin/karyopherin Kap114 mediates the nuclear import of TATA-binding protein. Proc Natl Acad Sci USA. 96:1999;12542-12547.
6. Titov A.A., Blobel G. The karyopherin Kap122p/Pdr6p imports both subunits of the transcription factor IIA into the nucleus. J Cell Biol. 147:1999;235-245.
7. Middeler G., Zerf K., Jenovai S., Thulig A., Tschodrich-Rotter M., Kubitscheck U., Peters R. The tumor suppressor p53 is subject to both nuclear import and export and both are fast, energy-dependent and lectin-inhibited. Oncogene. 14:1997;1407-1417.
8. Stommel J.M., Marchenko N.D., Jimenez G.S., Moll U.M., Hope T.J., Wahl G.M. A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking. EMBO J. 18:1999;1660-1672. This is a very interesting paper that identifies NES-masking as a mode of regulating the localization of p53. The p53 NES is also its tetramerization domain. The transcriptionally active form of p53 is a tetramer. Thus, tetramerization masks the p53 NES and traps the active form of p53 in the nucleus.
9. Lee W., Harvey T.S., Yin Y., Yau P., Litchfield D., Arrowsmith C.H. Solution structure of the tetrameric minimum transforming domain of p53. Nature Struct Biol. 1:1994;877-890.
10. Schlamp C.L., Poulsen G.L., Nork T.M., Nickells R.W. Nuclear exclusion of wild-type p53 in immortalized human retinoblastoma cells. J Natl Cancer Inst. 89:1997;1530-1536.
11. Moll U.M., LaQuaglia M., Bernard J., Riou G. Wild-type p53 protein undergoes cytoplasmic sequestration in undifferentiated neuroblastomas but not in differentiated tumors. Proc Natl Acad Sci USA. 92:1995;4407-4411.
12. Roth J., Dobbelstein M., Freedman D.A., Shenk T., Levine A.J. Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J. 17:1998;554-564.
13. Zhu J., McKeon F. NF-AT activation requires suppression of Crm1 dependent export by calcineurin. Nature. 398:1999;256-260. This study reveals NES masking as a mode of regulating the localization of a protein. The authors show that the NES of NF-AT coincides with its calcineurin-binding site. Thus, when calcineurin is bound to NF-AT it prevents Crm1 from binding to NF-AT and exporting it from the nucleus. NF-AT is also regulated by masking of its NLS. When the NLS-masking domain is removed NF-AT is nuclear but not active transcriptionally. However, when both the NLS-masking domain and the NESs are removed, NF-AT is nuclear and active. Thus, nuclear localization is not sufficient to regulate the activity of NF-AT.
14. Hogan P.G., Rao A. Transcriptional regulation. Modification by nuclear export? Nature. 398:1999;200-201.
15. Zhu J., Shibasaki F., Price R., Guillemot J., Yano T., Dötsch V., Wagner G., Ferrara P., McKeon F. Intramolecular masking of nuclear import signal on NF-AT4 by casein kinase I and MEKKI. Cell. 93:1998;851-861.
16. Oshima Y. The phosphatase system in Saccharomyces cerevisiae. Genes Genet Syst. 72:1997;323-334.
17. O'Neill E.M., Kaffman A., Jolly E.R., O'Shea E.K. Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex. Science. 271:1996;209-212.
18. Kaffman A., Herskowitz I., Tjian R., O'Shea E.K. Phosphorylation of the transcription factor PHO4 by a cyclin-CDK complex, PHO80-PHO85. Science. 263:1994;1153-1156.
19. Kaffman A., Rank N.M., O'Shea E.K. Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121. Genes Dev. 12:1998;2673-2683.
20. Kaffman A., Rank N.M., O'Neill E.M., Huang L.S., O'Shea E.K. The receptor Msn5p exports the phosphorylated transcription factor Pho4 out of the nucleus. Nature. 396:1998;482-486.
21. Komeili A., O'Shea E.K. Roles of phosphorylation sites in regulating activity of the transcription factor Pho4. Science. 284:1999;977-980. This study dissects the role of phosphorylation in regulating the activity of Pho4. Pho4 is inactivated by phosphorylation by the Pho80-Pho85 cyclin-CDK complex. The phosphorylation sites on Pho4 have unique and separable roles in regulating its activity. Two sites promote the export of Pho4 and a third site inhibits its import. Nuclear localization is not sufficient to regulate Pho4 activity as phosphorylation of a fourth site regulates Pho4 interaction with the transcription factor Pho2.
22. Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T. HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J. 18:1999;5099-5107.
23. Khokhlatchev A.V., Canagarajah B., Wilsbacher J., Robinson M., Atkinson M., Goldsmith E., Cobb M.H. Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation. Cell. 93:1998;605-615.
24. Barbaric S., Fascher K.D., Hörz W. Activation of the weakly regulated PHO8 promoter in S. cerevisiae: chromatin transition and binding sites for the positive regulator protein Pho4. Nucleic Acids Res. 5:1992;2689-2696.