scholarly journals Protein kinase CK2 phosphorylates Hsp105alpha at Ser509 and modulates its function

2003 ◽  
Vol 371 (3) ◽  
pp. 917-925 ◽  
Author(s):  
Keiichi ISHIHARA ◽  
Nobuyuki YAMAGISHI ◽  
Takumi HATAYAMA
Keyword(s):  
Heat Shock ◽  
Protein Kinase ◽  
Mammalian Cells ◽  
Protein Kinase Ck2 ◽  
Peptide Mapping ◽  
Stress Protein ◽  
Cellular Events ◽  
Kinase Ck2

The 105 kDa heat-shock protein (Hsp) Hsp105α is a mammalian stress protein that belongs to the HSP105/HSP110 family. We have shown previously that Hsp105α exists as non-phosphorylated and phosphorylated forms in vivo, and is phosphorylated by protein kinase CK2 (CK2) in vitro. In this study, to elucidate the role of phosphorylation of Hsp105α, we first analysed the site of phosphorylation of Hsp105α by CK2. Peptide mapping analysis of Hsp105α phosphorylated by CK2 and in vitro phosphorylation experiments using various deletion and substitution mutants of Hsp105α revealed that Hsp105α is phosphorylated at Ser509 in the β-sheet domain. Furthermore, Ser509 in Hsp105α was also phosphorylated in mammalian COS-7 cells, although other sites were phosphorylated as well. Next, we examined the effects of phosphorylation of Hsp105α on its functions using CK2-phosphorylated Hsp105α. Interestingly, Hsp105α suppressed 70 kDa heat-shock cognate protein (Hsc70)-mediated protein folding, whereas the phosphorylation of Hsp105α at Ser509 abolished the inhibitory activity of Hsp105α in vitro. In accordance with these findings, wild-type Hsp105α, which was thought to be phosphorylated in vivo, had no effect on Hsp70-mediated refolding of heat-denatured luciferase, whereas a non-phosphorylatable mutant of Hsp105α suppressed the Hsp70-mediated refolding of heat-denatured luciferase in mammalian cells. Thus it was suggested that CK2 phosphorylates Hsp105α at Ser509 and modulates the function of Hsp105α. The regulation of Hsp105α function by phosphorylation may play an important role in a variety of cellular events.

scholarly journals Phosphorylation of Serine 239 of Groucho/TLE1 by Protein Kinase CK2 Is Important for Inhibition of Neuronal Differentiation

2004 ◽  
Vol 24 (19) ◽  
pp. 8395-8407 ◽  
Author(s):  
Hugh N. Nuthall ◽  
Kerline Joachim ◽  
Stefano Stifani
Keyword(s):  
Protein Kinase ◽  
Neuronal Differentiation ◽  
Mammalian Cells ◽  
Protein Kinase Ck2 ◽  
Molecular Mechanisms ◽  
Transcription Repression ◽  
Transcriptional Corepressors ◽  
Kinase Ck2 ◽  
Nuclear Association

ABSTRACT Transcriptional corepressors of the Groucho (Gro)/TLE family play important roles during a variety of developmental pathways, including neuronal differentiation. In particular, they act as negative regulators of neurogenesis, together with Hairy/Enhancer of split (Hes) DNA-binding proteins. The interaction with Hes1 leads to Gro/TLE hyperphosphorylation and increased transcription repression activity in mammalian cells, but the underlying molecular mechanisms are poorly characterized. We now show that Gro/TLE1 is phosphorylated in vivo by protein kinase CK2. This phosphorylation occurs at serine 239 within the conserved CcN domain present in all Gro/TLE family members. Mutation of serine 239 into alanine decreases Hes1-induced hyperphosphorylation of Gro/TLE1 and also reduces its nuclear association and transcription repression activity. We demonstrate further that Gro/TLE1 inhibits the transition of cortical neural progenitors into neurons and that its antineurogenic activity is inhibited by a serine-239-alanine mutation but not by a serine-239-glutamate mutation. These results suggest that CK2 phosphorylation of serine 239 of Gro/TLE1 is important for its function during neuronal differentiation.

Protein Kinase CK2 Regulates Leukocyte-Endothelial Cell Interactions during Ischemia and Reperfusion in Striated Skin Muscle

2016 ◽  
Vol 57 (1-2) ◽  
pp. 111-124 ◽  
Author(s):  
Emmanuel Ampofo ◽  
Daniela Widmaier ◽  
Mathias Montenarh ◽  
Michael D. Menger ◽  
Matthias W. Laschke
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Tissue Injury ◽  
Cell Interactions ◽  
Ischemia And Reperfusion ◽  
Kinase Ck2

Background: Ischemia and reperfusion (I/R) causes tissue injury by inflammatory processes. This involves the upregulation of endothelial surface proteins by phospho-regulated signaling pathways, resulting in enhanced interactions of leukocytes with endothelial cells. Recently, we found that protein kinase CK2 is a crucial regulator of leukocyte-mediated inflammation. Therefore, in this study we investigated the involvement of CK2 in leukocyte-endothelial cell interactions during I/R injury. Methods: We first analyzed the inhibitory action of (E)-3-(2,3,4,5-tetrabromophenyl)acrylic acid (TBCA) and CX-4945 on CK2 kinase activity and the viability of human dermal microvascular endothelial cells (HDMEC). To mimic I/R conditions in vitro, HDMEC were exposed to hypoxia and reoxygenation and the expression of adhesion molecules was analyzed by flow cytometry. Moreover, we analyzed in vivo the effect of CK2 inhibition on leukocyte-endothelial cell interactions in the dorsal skinfold chamber model of I/R injury by means of repetitive intravital fluorescence microscopy and immunohistochemistry. Results: We found that TBCA and CX-4945 suppressed the activity of CK2 in HDMEC without affecting cell viability. This was associated with a significant downregulation of E-selectin and intercellular adhesion molecule (ICAM)-1 after in vitro hypoxia and reoxygenation. In vivo, CX-4945 treatment significantly decreased the numbers of adherent and transmigrated leukocytes in striated muscle tissue exposed to I/R. Conclusion: Our findings indicate that CK2 is involved in the regulation of leukocyte-endothelial cell interactions during I/R by mediating the expression of E-selectin and ICAM-1.

scholarly journals Effect of etimizole structural analogues on protein kinase CK2, protein phosphorylation and transcription of chromatin in rat brain cortex and hippocampus

2020 ◽  
Vol 66 (2) ◽  
pp. 130-137
Author(s):  
B.A. Reikhardt ◽  
P.D. Shabanov
Keyword(s):  
Protein Kinase ◽  
Rat Brain ◽  
Protein Kinase Ck2 ◽  
Long Term Memory ◽  
Term Memory ◽  
Structural Analogues ◽  
Kinase Ck2

Protein kinase CK2 is an important enzyme in the nervous system. The nuclear forms of CK2 regulate chromatin structure and gene expression, the key processes for long-term memory formation. Memory modulators, the Structural Analogues of Etimizole (SAE), were able to increase or decrease the activity of chromatin-associated CK in the cortex and hippocampus of rat brain in vitro. In vivo memory enhancers from SAE-group (3 mg/kg) stimulated CK2 activity and the transcriptional ability of chromatin in the cortex and hippocampus, starting from 30 min with a peak for 60 min and a duration up to 180 min. At these periods the memory inhibitor from the SAE-group reduced CK2 activity and chromatin transcription. It is assumed that the modulating effect of SAE on CK2 activity and transcription underlies the effects of these compounds on long-term memory.

scholarly journals Phosphorylation by Protein Kinase CK2 Changes the DNA Binding Properties of the Human Chromatin Protein DEK

2004 ◽  
Vol 24 (13) ◽  
pp. 6011-6020 ◽  
Author(s):  
Ferdinand Kappes ◽  
Catalina Damoc ◽  
Rolf Knippers ◽  
Michael Przybylski ◽  
Lorenzo A. Pinna ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Ion Trap ◽  
Quadrupole Ion Trap ◽  
Chromatin Protein ◽  
Binding Assays ◽  
Kinase Ck2

ABSTRACT We have examined the posttranslational modification of the human chromatin protein DEK and found that DEK is phosphorylated by the protein kinase CK2 in vitro and in vivo. Phosphorylation sites were mapped by quadrupole ion trap mass spectrometry and found to be clustered in the C-terminal region of the DEK protein. Phosphorylation fluctuates during the cell cycle with a moderate peak during G1 phase. Filter binding assays, as well as Southwestern analysis, demonstrate that phosphorylation weakens the binding of DEK to DNA. In vivo, however, phosphorylated DEK remains on chromatin. We present evidence that phosphorylated DEK is tethered to chromatin throughout the cell cycle by the un- or underphosphorylated form of DEK.

In Vitro and In Vivo Assays of Protein Kinase CK2 Activity

2010 ◽  
pp. 597-610 ◽  
Author(s):  
Renaud Prudent ◽  
Céline F. Sautel ◽  
Virginie Moucadel ◽  
Béatrice Laudet ◽  
Odile Filhol ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
In Vivo Assays ◽  
Kinase Ck2

scholarly journals Inhibition of Protein Kinase CK2 by Condensed Polyphenolic Derivatives. An in Vitro and in Vivo Study†

Biochemistry ◽  
2004 ◽  
Vol 43 (40) ◽  
pp. 12931-12936 ◽  
Author(s):  
Flavio Meggio ◽  
Mario A. Pagano ◽  
Stefano Moro ◽  
Giuseppe Zagotto ◽  
Maria Ruzzene ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
In Vivo Study ◽  
Kinase Ck2

scholarly journals The catalytic subunit of protein kinase CK2 phosphorylates in vitro the movement protein of Tomato mosaic virus

2003 ◽  
Vol 84 (2) ◽  
pp. 497-505 ◽  
Author(s):  
Yasuhiko Matsushita ◽  
Mayumi Ohshima ◽  
Kuniaki Yoshioka ◽  
Masamichi Nishiguchi ◽  
Hiroshi Nyunoya
Keyword(s):  
Protein Kinase ◽  
Mosaic Virus ◽  
Protein Kinase Ck2 ◽  
Movement Protein ◽  
Catalytic Subunit ◽  
Tomato Mosaic Virus ◽  
Kinase Ck2

Yeast surviving factor Svf1 as a new interacting partner, regulator and in vitro substrate of protein kinase CK2

2008 ◽  
Vol 312 (1-2) ◽  
pp. 61-69 ◽  
Author(s):  
Maciej Masłyk ◽  
Elżbieta Kochanowicz ◽  
Rafał Zieliński ◽  
Konrad Kubiński ◽  
Ulf Hellman ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Kinase Ck2

Interaction of tubulin and protein kinase CK2 in Trypanosoma equiperdum

2017 ◽  
Vol 72 (11-12) ◽  
pp. 459-465 ◽  
Author(s):  
Beatriz E. Boscán ◽  
Graciela L. Uzcanga ◽  
Maritza Calabokis ◽  
Rocío Camargo ◽  
Frank Aponte ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Polyacrylamide Gel Electrophoresis ◽  
Direct Interaction ◽  
Exchange Chromatography ◽  
Parasite Protein ◽  
Α Subunit ◽  
Trypanosoma Equiperdum ◽  
Kinase Ck2

AbstractA polypeptide band with an apparent molecular weight of 55,000 was phosphorylated in vitro in whole-cell lysates ofTrypanosoma equiperdum. This band corresponds to tubulin as demonstrated by immunoprecipitation of the phosphorylated polypeptide fromT. equiperdumextracts when anti-α and anti-β tubulin monoclonal antibodies were employed. A parasite protein kinase CK2 was in charge of modifying tubulin given that common mammalian CK2 inhibitors such as emodin and GTP, hindered the phosphorylation of tubulin and exogenously added casein. Interestingly, a divalent cation-dependent translocation of theT. equiperdumtubulin and the CK2 responsible for its phosphorylation was noticed, suggesting a direct interaction between these two proteins. Additionally, this fraction of tubulin and its kinase coeluted using separations based on parameters as different as charge (DEAE-Sepharose anion-exchange chromatography) and size (Sephacryl S-300 gel filtration chromatography). Analyses by non-denaturing polyacrylamide gel electrophoresis and immunoblot of the purified and radioactively labeled fraction containing both tubulin and the CK2 enzyme, established the phosphorylation of a single band that was recognized by anti-CK2 α-subunit and anti-tubulin antibodies. All these findings revealed a physical association between a pool of tubulin and a CK2 inT. equiperdum.

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