Details

Autor(en) / Beteiligte

• Michalec-Wawiorka, Barbara
• Wawiorka, Leszek
• Derylo, Kamil
• Krokowski, Dawid
• Boguszewska, Aleksandra
• Molestak, Eliza
• Szajwaj, Monika
• Tchorzewski, Marek

Titel

Molecular behavior of human Mrt4 protein, MRTO4, in stress conditions is regulated by its C-terminal region

Ist Teil von

• The international journal of biochemistry & cell biology, 2015-12, Vol.69, p.233-240

Ort / Verlag

Netherlands: Elsevier Ltd

Erscheinungsjahr

2015

Quelle

MEDLINE

Beschreibungen/Notizen

• •Human Mrt4 protein is phosphorylated in vivo.•Three serines within C-termini of hMrt4/MRTO4 are phosphorylated by CK2 in vitro.•hMrt4/MRTO4 phosphorylation/dephosphorylation equilibrium determines its behavior during nucleolar stress induced by ActD treatment. Protein Mrt4 is one of trans-acting factors involved in ribosome biogenesis, which in higher eukaryotic cells contains a C-terminal extension similar to the C-terminal part of ribosomal P proteins. We show that human Mrt4 (hMrt4/MRTO4) undergoes phosphorylation in vivo and that serines S229, S233, and S235, placed within its acidic C-termini, have been phosphorylated by CK2 kinase in vitro. Such modification does not alter the subcellular distribution of hMrt4 in standard conditions but affects its molecular behavior during ActD induced nucleolar stress. Thus, we propose a new regulatory element important for the stress response pathway connecting ribosome biogenesis with cellular metabolism.