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dc.contributor.authorMålen, Hiwaeng
dc.contributor.authorLillehaug, Johaneng
dc.contributor.authorArnesen, Thomaseng
dc.description.abstractBackground: The hNaa10p (hArd1) protein is the catalytic subunit of the human NatA Nα- terminal acetyltransferase complex. The NatA complex is associated with ribosomes and cotranslationally acetylates human proteins with Ser-, Ala-, Thr-, Val-, and Gly- N-termini after the initial Met- has been removed. In the flexible C-terminal tail of hNaa10p, there are several potential phosphorylation sites that might serve as points of regulation. Findings: Using 2D-gel electrophoresis and hNaa10p specific antibodies, we have investigated whether hNaa10p is phosphorylated in HEK293 cells. Several differently charged forms of hNaa10p are present in HEK293 cells and treatment with Calf Intestine Alkaline Phophatase (CIAP) strongly suggests that hNaa10p is phosphorylated at multiple sites under various cell culture conditions. A direct or indirect role of GSK-3 kinase in regulating hNaa10p phosphorylation is supported by the observed effects of Wortmannin and LiCl, a GSK-3 activator and inhibitor, respectively. Conclusion: We demonstrate that hNaa10p protein is phosphorylated in cell culture potentially pointing at phosphorylation as a means of regulating the function of one of the major Nα-terminal acetyltransferases in human cells.en_US
dc.publisherBioMed Centralen_US
dc.rightsAttribution CC BYeng
dc.titleThe protein N-alpha-terminal acetyltransferase hNaa10p (hArd1) is phosphorylated in HEK293 cellsen_US
dc.typePeer reviewed
dc.typeJournal article
dc.description.versionPeer Reviewed
dc.rights.holderHiwa Målen et al.; licensee BioMed Central Ltd.en_US
dc.rights.holderCopyright 2008 Arnesen et al; licensee BioMed Central Ltden_US
dc.source.journalBMC Research Notes

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