Cited by 394Fungal and yeast genetics researchProtein Kinase Regulation and GTPase SignalingGenomics and Chromatin Dynamics

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A Role for Nuclear Inositol 1,4,5-Trisphosphate Kinase in Transcriptional Control

Odom, Audrey R., Stahlberg, Alke, Wente, Susan R., York, John D.·2000·Science

DOI 10.1126/science.287.5460.2026

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Abstract

Phospholipase C and two inositol polyphosphate (IP) kinases constitute a signaling pathway that regulates nuclear messenger RNA export through production of inositol hexakisphosphate (IP 6 ). The inositol 1,4,5-trisphosphate kinase of this pathway in Saccharomyces cerevisiae , designated Ipk2, was found to be identical to Arg82, a regulator of the transcriptional complex ArgR-Mcm1. Synthesis of inositol 1,4,5,6-tetrakisphosphate, but not IP 6 , was required for gene regulation through ArgR-Mcm1. Thus, the phospholipase C pathway produces multiple IP messengers that modulate distinct nuclear processes. The results reveal a direct mechanism by which activation of IP signaling may control gene expression.

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Inositol trisphosphate and calcium signalling
Berridge, M. J. (1993) · Nature · doi:10.1038/361315a0 · Cited by 6,545
The MADS-Box Family of Transcription Factors
Shore, P., & Sharrocks, A. D. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0001l.x · Cited by 921
The MADS-Box Family of Transcription Factors
Shore, P., & Sharrocks, A. D. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20430.x · Cited by 702
A Phospholipase C-Dependent Inositol Polyphosphate Kinase Pathway Required for Efficient Messenger RNA Export
York, J. D., John, A. R. O., Murphy, R., Ives, E. B., & Wente, S. R. (1999) · Science · doi:10.1126/science.285.5424.96 · Cited by 547
Self-citation
Synthesis of Diphosphoinositol Pentakisphosphate by a Newly Identified Family of Higher Inositol Polyphosphate Kinases
Saiardi, A., Erdjument-Bromage, H., Snowman, A. M., Tempst, P., & Snyder, S. H. (1999) · Current Biology · doi:10.1016/s0960-9822(00)80055-x · Cited by 414
INOSITOL PHOSPHATE BIOCHEMISTRY
Majerus, P. W. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.001301 · Cited by 397
Phosphoinositide Signaling Pathways in Nuclei Are Associated with Nuclear Speckles Containing Pre-mRNA Processing Factors
Boronenkov, I. V., Loijens, J. C., Umeda, M., & Anderson, R. A. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.12.3547 · Cited by 337
Nuclear localization and signalling activity of phosphoinositidase Cβ in Swiss 3T3 cells
Martelli, A. M., Gilmour, R., Bertagnolo, V., Neri, L. M., Manzoli, L., & Cocco, L. (1992) · Nature · doi:10.1038/358242a0 · Cited by 322
The yeast cell-type-specific repressor α2 acts cooperatively with a non-cell-type-specific protein
Keleher, C. A., Goutte, C., & Johnson, A. D. (1988) · Cell · doi:10.1016/s0092-8674(88)90449-7 · Cited by 314
Significance of PIP2 hydrolysis and regulation of phospholipase C isozymes
Lee, S. B., & Rhee, S. G. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80026-3 · Cited by 284

Flagged first, then by citations

Show all 39 references

Research works printed but not linked: 6

Messenguy F., Dubois E., Mol. Cell. Biol. 13, 2586 (1993).
Flick J., Thorner J., Mol. Cell. Biol. 13, 5861 (1993);
Payne W. E., Fitzgerald-Hayes M., Mol. Cell Biol. 13, 4351 (1993).
Dubois E., Messenguy F., Mol. Cell. Biol. 11, 2162 (1991).
Seneca S., Punyammalee B., Glansdorff N., Crabeel M., Mol. Cell. Biol. 12, 68 (1992).
Supplementary material is available to Science Online subscribers at www.sciencemag.org/feature/data/1045815.shl.

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Authors: Odom, A. R., Stahlberg, A., Wente, S. R., & York, J. D.
Affiliations: Departments of Pharmacology and Cancer Biology and of Biochemistry, Duke University Medical Center, DUMC 3813, Durham, NC 27710, USA.
Department of Cell Biology and Physiology, Washington University School of Medicine, 660 South Euclid, St. Louis, MO 63110, USA.
Washington University in St. Louis (US)
Duke University (US)
Corresponding author: York, John D.
ORCID: Wente, Susan R.
York, John D.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2000-03-17
Volume: 287
Issue: 5460
Pages: 2026-2029
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.287.5460.2026
OpenAlex: W2087358641
Cited by: 394
References: 39
Citations by year: 2026: 5 · 2025: 8 · 2024: 8 · 2023: 7 · 2022: 5 · 2021: 5 · 2020: 10 · 2019: 11 · 2018: 6 · 2017: 13 · 2016: 13 · 2015: 17 · 2014: 6 · 2013: 11 · 2012: 21
FWCI: 10.49
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: phytic acid, mRNA export, transcriptional regulation, Saccharomyces cerevisiae, gene expression regulation
MeSH terms: Amino Acid Sequence, Arginine, Cell Nucleus, DNA-Binding Proteins, Inositol Phosphates, Molecular Sequence Data, Type C Phospholipases, Phosphoric Monoester Hydrolases, Phosphorylation, Phytic Acid, Saccharomyces cerevisiae, Transcription Factors, Transcription, Genetic, Signal Transduction, Inositol 1,4,5-Trisphosphate, Gene Expression Regulation, Fungal, Phosphotransferases (Alcohol Group Acceptor), Minichromosome Maintenance 1 Protein

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A Role for Nuclear Inositol 1,4,5-Trisphosphate Kinase in Transcriptional Control

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