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

Eunha Kim, Richa Tyagi, Joo Young Lee, Jina Park, Young Ran Kim, Jiyoon Beon, Po Yu Chen, Jiyoung Y. Cha, Solomon H. Snyder, Seyun Kim

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)19938-19943
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume110
Issue number49
DOIs
StatePublished - Dec 3 2013

ASJC Scopus subject areas

  • General

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