Literature DB >> 10571851

Cell-cycle modulation of CK2 activity in tobacco BY-2 cells.

M C Espunya1, B Combettes, J Dot, N Chaubet-Gigot, M C Martínez.   

Abstract

Protein kinase CK2 is an ubiquitous Ser/Thr kinase essential for cell growth. We have used the highly synchronizable tobacco BY-2 cell line to investigate whether CK2 activity and expression are regulated in a cell cycle phase-dependent manner in higher plants. Specific cDNA probes for tobacco CK2alpha and beta subunits, respectively, and polyclonal antibodies recognising alpha and beta subunits separately, were obtained to determine mRNA and protein levels of both subunits. Our results show that CK2 activity oscillates throughout the cell cycle, peaking at G1/S and M phases, due to a post-translational regulation of the tetrameric enzyme. Additional levels of control of CK2 expression operate in relation to the proliferative state of the cells, including differential accumulation of alpha and beta transcripts and post-transcriptional regulation of protein levels (beta subunit). Moreover, in vivo inhibition of CK2 activity corroborates the requirement of the functional CK2 to progress through the cell division cycle, and suggests that CK2 might play an important role at the G2/M checkpoint.

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Year:  1999        PMID: 10571851     DOI: 10.1046/j.1365-313x.1999.00563.x

Source DB:  PubMed          Journal:  Plant J        ISSN: 0960-7412            Impact factor:   6.417


  19 in total

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10.  Phosphorylation of maize eukaryotic translation initiation factor 5A (eIF5A) by casein kinase 2: identification of phosphorylated residue and influence on intracellular localization of eIF5A.

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