A period-timeless (per-tim) based feedback loop is considered to be essential in generating circadian rhythms in Drosophila melanogaster. In addition to transcriptional regulation, the post-transcriptional modification is essential to the circadian oscillation of core clock proteins in the circadian system. Here we present expression profiles of the catalytic subunit of casein kinase 2alpha (ck2alpha) and casein kinase 2beta (ck2beta) in Bombyx mori. Southern blot analyses showed that ck2alpha and ck2beta of B. mori were single copy genes. Northern blot analyses demonstrated that both subunits were expressed in eggs, larval heads, adult heads, testes and ovaries. In situ hybridization analyses indicated that subunits were expressed in brain neurons expressing PER-like protein. Surprisingly, antisense RNAs of ck2alpha and ck2beta were also detected in the putative clock neurons. Temporal expressions of ck2alpha and ck2beta mRNAs were constant in adult heads under LD12:12. The core clock genes per and tim showed daily fluctuations of mRNA abundance in the embryonic stage that is photoperiod sensitive period to determine egg diapause in the next generation whereas the expression of ck2alpha and ck2beta was constant. No evidence supports that ck2alpha and ck2beta of B. mori were transcriptionally regulated by circadian oscillation, but histological data show a close association of ck2alpha and ck2beta with circadian system in B. mori.
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http://dx.doi.org/10.1016/j.cbpb.2007.08.004 | DOI Listing |
ChemMedChem
January 2025
Université Claude Bernard Lyon 1: Universite Claude Bernard Lyon 1, Centre de Recherche en Cancérologie de Lyon, FRANCE.
The serine/threonine protein kinase CK2, a tetramer composed of a regulatory dimer (CK2β2) bound to two catalytic subunits CK2α, is a well-established therapeutic target for various pathologies, including cancer and viral infections. Several types of CK2 inhibitors have been developed, including inhibitors that bind to the catalytic ATP-site, bivalent inhibitors that occupy both the CK2α ATP-site and the αD pocket, and inhibitors that target the CK2α/CK2β interface. Interestingly, the bivalent inhibitor AB668 shares a similar chemical structure with the interface inhibitor CCH507.
View Article and Find Full Text PDFMolecules
December 2024
Institut für Pharmazeutische und Medizinische Chemie, Universität Münster, Corrensstraße 48, D-48149 Münster, Germany.
The serine/threonine kinase CK2 (formerly known as casein kinase II) plays a crucial role in various CNS disorders and is highly expressed in various types of cancer. Therefore, inhibiting this key kinase could be promising for the treatment of these diseases. The CK2 holoenzyme is formed by the recruitment of two catalytically active CK2α and/or CK2α' subunits by a regulatory CK2β dimer.
View Article and Find Full Text PDFACS Chem Neurosci
August 2024
Department of Neuroscience, School of Medicine, University of Minnesota, Minneapolis, Minnesota 55414, United States.
Protein kinase CK2 is a holoenzyme composed of two regulatory subunits (CK2β) and two catalytic subunits (CK2α and CK2α'). CK2 controls several cellular processes, including proliferation, inflammation, and cell death. However, CK2α and CK2α' possess different expression patterns and substrates and therefore impact each of these processes differently.
View Article and Find Full Text PDFFront Immunol
May 2024
Hematology Unit, Department of Medicine (DIMED), University of Padova, Padova, Italy.
Introduction: In classical Hodgkin lymphoma (cHL), the survival of neoplastic cells is mediated by the activation of NF-κB, JAK/STAT and PI3K/Akt signaling pathways. CK2 is a highly conserved serine/threonine kinase, consisting of two catalytic (α) and two regulatory (β) subunits, which is involved in several cellular processes and both subunits were found overexpressed in solid tumors and hematologic malignancies.
Methods And Results: Biochemical analyses and assays showed an impaired expression of CK2 subunits in cHL, with CK2α being overexpressed and a decreased expression of CK2β compared to normal B lymphocytes.
bioRxiv
January 2024
Department of Neuroscience, University of Minnesota, School of Medicine, Minneapolis, Minnesota 55414, United States.
Protein Kinase CK2 is a holoenzyme composed of two regulatory subunits (CK2β) and two catalytic subunits (CK2α and CK2α'). CK2 controls several cellular processes including proliferation, inflammation, and cell death. However, CK2α and CK2α' possess different expression patterns and substrates and therefore impact each of these processes differently.
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