Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1

92Citations
Citations of this article
32Readers
Mendeley users who have this article in their library.

Abstract

Pim-1, a protooncogene product, is a serine/threonine kinase and is thought to play a role in signal transduction in blood cells. Few phosphorylated target proteins for Pim-1, however, have been identified. In the present study, two-hybrid screening to clone cDNAs encoding proteins binding to Pim-1 was carried out, and a cDNA for heterochromatin protein 1γ (HP1γ) was obtained. Binding assays both in yeast and in vitro pull-down using the purified HP1γ and Pim-1 expressed in Escherichia coli showed that Pim-1 directly bound to the chromo shadow domain of HP1γ. HP1γ was also associated with Pim-1 in human HeLa cells and the serine clusters located at the center of HP1γ were phosphorylated by Pim-1 in vitro. Furthermore, a transcription repression activity of HP1γ was further stimulated by the deletion of the serine clusters targeted by Pim-1. These results suggest that Pim-1 affects the structure or silencing of chromatin by phosphorylating HP1. Copyright (C) 2000 Federation of European Biochemical Societies.

Cite

CITATION STYLE

APA

Koike, N., Maita, H., Taira, T., Ariga, H., & Iguchi-Ariga, S. M. M. (2000). Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1. FEBS Letters, 467(1), 17–21. https://doi.org/10.1016/S0014-5793(00)01105-4

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free