Inositol polyphosphate multikinase (IPMK) in transcriptional regulation and nuclear inositide metabolism

Biochem Soc Trans. 2016 Feb;44(1):279-85. doi: 10.1042/BST20150225.

M Merced Malabanan ¹, Raymond D Blind ²

Affiliations

1 Department of Biochemistry; Vanderbilt Center for Structural Biology and Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
2 Department of Biochemistry; Vanderbilt Center for Structural Biology and Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA Department of Medicine, Vanderbilt Diabetes Research and Training Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA ray.blind@vanderbilt.edu).

PMID: 26862216 DOI: 10.1042/BST20150225

Abstract

Inositol polyphosphate multikinase (IPMK, ipk2, Arg(82), ArgRIII) is an inositide kinase with unusually flexible substrate specificity and the capacity to partake in many functional protein-protein interactions (PPIs). By merging these two activities, IPMK is able to execute gene regulatory functions that are very unique and only now beginning to be recognized. In this short review, we present a brief history of IPMK, describe the structural biology of the Enzyme and highlight a few recent discoveries that have shed more light on the role IPMK plays in inositide metabolism, nuclear signalling and transcriptional regulation.

Keywords

ArgR; IPMK; gene expression; inositide; ipk2; multikinase; transcription.

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