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HIRIP3 is a nuclear phosphoprotein interacting with and phosphorylated by the serine-threonine kinase CK2.

Abstract : The HIRIP3 protein had been identified from its interaction with the HIRA histone chaperone. Experiments using anti-peptide antisera indicated that this 556-aa protein is nuclear throughout the cell cycle and excluded from condensed chromatin during mitosis. Based on its electrophoretic migration and sensitivity to phosphatase treatment, endogenous HIRIP3 was found to be heavily phosphorylated. HIRIP3 can be phosphorylated in vitro by a recombinant form of the serine-threonine kinase CK2. Moreover, HIRIP3 protein was found to co-purify with a CK2 activity. Together, these data prompt us to propose HIRIP3 as a new member of the growing list of CK2 substrates with a possible role in chromatin metabolism.
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https://www.hal.inserm.fr/inserm-00170840
Contributor : Marie-Annie Dambo <>
Submitted on : Monday, September 10, 2007 - 4:42:23 PM
Last modification on : Tuesday, October 27, 2020 - 3:31:10 AM

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Nadine Assrir, Odile Filhol, Frédéric Galisson, Marc Lipinski. HIRIP3 is a nuclear phosphoprotein interacting with and phosphorylated by the serine-threonine kinase CK2.. Biological Chemistry, De Gruyter, 2007, 388 (4), pp.391-8. ⟨10.1515/BC.2007.045⟩. ⟨inserm-00170840⟩

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