Inositol polyphosphate multikinase is a coactivator for serum response factor-dependent induction of immediate early genes

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Inositol polyphosphate multikinase (IPMK) is a notably pleiotropic protein. It displays both inositol phosphate kinase and phosphatidylinositol kinase catalytic activities. Noncatalytically, IPMK stabilizes the mammalian target of rapamycin complex 1 and acts as a transcriptional coactivator for CREB-binding protein/E1A binding protein p300 and tumor suppressor protein p53. Serum response factor (SRF) is a major transcription factor for a wide range of immediate early genes. We report that IPMK, in a noncatalytic role, is a transcriptional coactivator for SRF mediating the transcription of immediate early genes. Stimulation by serum of many immediate early genes is greatly reduced by IPMK deletion. IPMK stimulates expression of these genes, an influence also displayed by catalytically inactive IPMK. IPMK acts by binding directly to SRF and thereby enhancing interactions of SRF with the serum response element of diverse genes.
Publisher
NATL ACAD SCIENCES
Issue Date
2013-12
Language
English
Article Type
Article
Keywords

ELEMENT-BINDING PROTEIN; C-FOS; TERNARY COMPLEX; DNA-BINDING; SACCHAROMYCES-CEREVISIAE; TRANSCRIPTION FACTORS; ARGININE METABOLISM; CREB PHOSPHORYLATION; MOUSE EMBRYOGENESIS; NERVOUS-SYSTEM

Citation

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.110, no.49, pp.19938 - 19943

ISSN
0027-8424
DOI
10.1073/pnas.1320171110
URI
http://hdl.handle.net/10203/187016
Appears in Collection
BS-Journal Papers(저널논문)
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