scholarly journals CaMK IV phosphorylates prohibitin 2 and regulates prohibitin 2-mediated repression of MEF2 transcription

2011 ◽  
Vol 23 (10) ◽  
pp. 1686-1690 ◽  
Author(s):  
Luguo Sun ◽  
Xia Cao ◽  
Bin Liu ◽  
Honglan Huang ◽  
Xu Wang ◽  
...  
Keyword(s):  
Camk Iv

Compound K Induces Apoptosis via CAMK-IV/AMPK Pathways in HT-29 Colon Cancer Cells

2009 ◽  
Vol 57 (22) ◽  
pp. 10573-10578 ◽  
Author(s):  
Do Yeon Kim ◽  
Min Woo Park ◽  
Hai Dan Yuan ◽  
Hyo Jung Lee ◽  
Sung Hoon Kim ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cancer Cells ◽  
Colon Cancer Cells ◽  
Compound K ◽  
Camk Iv ◽  
Ht 29

A CaMK IV responsive RNA element mediates depolarization-induced alternative splicing of ion channels

Nature ◽  
2001 ◽  
Vol 410 (6831) ◽  
pp. 936-939 ◽  
Author(s):  
Jiuyong Xie ◽  
Douglas L. Black
Keyword(s):  
Alternative Splicing ◽  
Ion Channels ◽  
Camk Iv

scholarly journals Regulation of microtubule dynamics by Ca2+/calmodulin-dependent kinase IV/Gr-dependent phosphorylation of oncoprotein 18.

1997 ◽  
Vol 17 (6) ◽  
pp. 3459-3467 ◽  
Author(s):  
H Melander Gradin ◽  
U Marklund ◽  
N Larsson ◽  
T A Chatila ◽  
M Gullberg
Keyword(s):  
Cell Cycle ◽  
Genetic System ◽  
Mitogen Activated Protein Kinase ◽  
Cross Linking ◽  
Mitogen Activated Protein ◽  
Oncoprotein 18 ◽  
Partial Degradation ◽  
Camk Iv ◽  
External Signals ◽  
Chemical Cross Linking

Oncoprotein 18 (Op18; also termed p19, 19K, p18, prosolin, and stathmin) is a regulator of microtubule (MT) dynamics and is phosphorylated by multiple kinase systems on four Ser residues. In addition to cell cycle-regulated phosphorylation, external signals induce phosphorylation of Op18 on Ser-25 by the mitogen-activated protein kinase and on Ser-16 by the Ca2+/calmodulin-dependent kinase IV/Gr (CaMK IV/Gr). Here we show that induced expression of a constitutively active mutant of CaMK IV/Gr results in phosphorylation of Op18 on Ser-16. In parallel, we also observed partial degradation of Op18 and a rapid increase of total cellular MTs. These results suggest a link between CaMK IV/Gr, Op18, and MT dynamics. To explore such a putative link, we optimized a genetic system that allowed conditional coexpression of a series of CaMK IV/Gr and Op18 derivatives. The result shows that CaMK IV/Gr can suppress the MT-regulating activity of Op18 by phosphorylation on Ser-16. In line with these results, by employing a chemical cross-linking protocol, it was shown that phosphorylation of Ser-16 is involved in weakening of the interactions between Op18 and tubulin. Taken together, these data suggest that the mechanism of CaMK IV/Gr-mediated suppression of Op18 activity involves both partial degradation of Op18 and direct modulation of the MT-destabilizing activity of this protein. These results show that Op18 phosphorylation by CaMK IV/Gr may couple alterations of MT dynamics in response to external signals that involve Ca2+.

scholarly journals Subchronic Exposure to Arsenic Represses the TH/TRβ1-CaMK IV Signaling Pathway in Mouse Cerebellum

2016 ◽  
Vol 17 (2) ◽  
pp. 157 ◽  
Author(s):  
Huai Guan ◽  
Shuangyue Li ◽  
Yanjie Guo ◽  
Xiaofeng Liu ◽  
Yi Yang ◽  
...  
Keyword(s):  
Signaling Pathway ◽  
Subchronic Exposure ◽  
Mouse Cerebellum ◽  
Camk Iv

Exercise and CaMK activation both increase the binding of MEF2A to the Glut4 promoter in skeletal muscle in vivo

2007 ◽  
Vol 292 (2) ◽  
pp. E413-E420 ◽  
Author(s):  
James A. H. Smith ◽  
Malcolm Collins ◽  
Liesl A. Grobler ◽  
Carrie J. Magee ◽  
Edward O. Ojuka
Keyword(s):  
Dominant Negative ◽  
Binding Assays ◽  
Cis Element ◽  
Calcium Calmodulin Dependent ◽  
Dependent Protein ◽  
Autonomous Activity ◽  
Exercise Induced ◽  
Camk Iv

In vitro binding assays have indicated that the exercise-induced increase in muscle GLUT4 is preceded by increased binding of myocyte enhancer factor 2A (MEF2A) to its cis-element on the Glut4 promoter. Because in vivo binding conditions are often not adequately recreated in vitro, we measured the amount of MEF2A that was bound to the Glut4 promoter in rat triceps after an acute swimming exercise in vivo, using chromatin immunoprecipitation (ChIP) assays. Bound MEF2A was undetectable in nonexercised controls or at 24 h postexercise but was significantly elevated ∼6 h postexercise. Interestingly, the increase in bound MEF2A was preceded by an increase in autonomous activity of calcium/calmodulin-dependent protein kinase (CaMK) II in the same muscle. To determine if CaMK signaling mediates MEF2A/DNA associations in vivo, we performed ChIP assays on C2C12 myotubes expressing constitutively active (CA) or dominant negative (DN) CaMK IV proteins. We found that ∼75% more MEF2A was bound to the Glut4 promoter in CA compared with DN CaMK IV-expressing cells. GLUT4 protein increased ∼70% 24 h after exercise but was unchanged by overexpression of CA CaMK IV in myotubes. These results confirm that exercise increases the binding of MEF2A to the Glut4 promoter in vivo and provides evidence that CaMK signaling is involved in this interaction.

scholarly journals Molecular Docking Performance of Selective Organic Compounds with Target Protein

2021 ◽  
Vol 11 (4) ◽  
pp. 12414-12424
Keyword(s):  
Hydrogen Bonding Interaction ◽  
Target Species ◽  
Dependent Protein Kinase ◽  
Docking Analysis ◽  
Penicillin Binding Proteins ◽  
Calcium Calmodulin Dependent ◽  
Bonding Interaction ◽  
Donor Acceptor ◽  
Dependent Protein ◽  
Camk Iv

In this article, the docking analysis has been carried out to know some selective compounds' interaction to bind with a targeted protein. There are three approaches have been analyzed here with three different kinds of protein as the target species. They are 2-aminobenzimidazole (2ABZ) with Acetylcholinesterase receptor (AChE), Phenoxazine (POZ) with Penicillin-binding proteins (PBPs) receptor, and Phenothiazines with Calcium/calmodulin-dependent protein kinase IV (CAMK IV) receptor. All three studies showed that the binding is perfect at the binding site and explained with hydrogen bonding interaction via donor-acceptor interactions.

CaMK IV Controls Splicing

2001 ◽  
Vol 2001 (79) ◽  
pp. tw2-tw2
Keyword(s):  
Camk Iv
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