subject:(eEF 2K) – OATD

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You searched for subject:(eEF 2K). Showing records 1 – 4 of 4 total matches.

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University of Texas – Austin

1. -8962-3030. Regulation of elongation factor 2 kinase (eEF-2K) by acidity.

Degree: PhD, Cell and Molecular Biology, 2019, University of Texas – Austin

URL: http://hdl.handle.net/2152/72809

► Eukaryotic elongation factor 2 kinase (eEF-2K) is a calmodulin (CaM)/calcium regulated kinase whose activity disrupts translation elongation resulting in the global decrease of protein synthesis¹.… (more)

Subjects/Keywords: eEF-2K; Acidity; Elongation factor 2 kinase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

-8962-3030. (2019). Regulation of elongation factor 2 kinase (eEF-2K) by acidity. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/72809

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

Chicago Manual of Style (16^th Edition):

-8962-3030. “Regulation of elongation factor 2 kinase (eEF-2K) by acidity.” 2019. Doctoral Dissertation, University of Texas – Austin. Accessed March 03, 2021. http://hdl.handle.net/2152/72809.

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

MLA Handbook (7^th Edition):

-8962-3030. “Regulation of elongation factor 2 kinase (eEF-2K) by acidity.” 2019. Web. 03 Mar 2021.

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

Vancouver:

-8962-3030. Regulation of elongation factor 2 kinase (eEF-2K) by acidity. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2019. [cited 2021 Mar 03]. Available from: http://hdl.handle.net/2152/72809.

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

Council of Science Editors:

-8962-3030. Regulation of elongation factor 2 kinase (eEF-2K) by acidity. [Doctoral Dissertation]. University of Texas – Austin; 2019. Available from: http://hdl.handle.net/2152/72809

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

University of Texas – Austin

2. Devkota, Ashwini Kumar. Mechanistic studies and drug discovery for eEF-2 kinase.

Degree: PhD, Cell and Molecular Biology, 2011, University of Texas – Austin

URL: http://hdl.handle.net/2152/22246

► eEF-2K, also known as CaM kinase-III, is an atypical protein kinase which negatively regulates the global rate of protein synthesis through the phosphorylation and inactivation… (more)

Subjects/Keywords: eEF-2 kinase; eEF-2K; Cancer; High-throughput screen; Drug discovery

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Devkota, A. K. (2011). Mechanistic studies and drug discovery for eEF-2 kinase. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/22246

Chicago Manual of Style (16^th Edition):

Devkota, Ashwini Kumar. “Mechanistic studies and drug discovery for eEF-2 kinase.” 2011. Doctoral Dissertation, University of Texas – Austin. Accessed March 03, 2021. http://hdl.handle.net/2152/22246.

MLA Handbook (7^th Edition):

Devkota, Ashwini Kumar. “Mechanistic studies and drug discovery for eEF-2 kinase.” 2011. Web. 03 Mar 2021.

Vancouver:

Devkota AK. Mechanistic studies and drug discovery for eEF-2 kinase. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2011. [cited 2021 Mar 03]. Available from: http://hdl.handle.net/2152/22246.

Council of Science Editors:

Devkota AK. Mechanistic studies and drug discovery for eEF-2 kinase. [Doctoral Dissertation]. University of Texas – Austin; 2011. Available from: http://hdl.handle.net/2152/22246

University of Texas – Austin

3. Tavares, Clint Damian Jaxon. Regulation of elongation factor 2 kinase (eEF-2K) by phosphorylation.

Degree: PhD, Cell and Molecular Biology, 2014, University of Texas – Austin

URL: http://hdl.handle.net/2152/47184

► Eukaryotic elongation factor 2 kinase (eEF-2K) is an atypical calcium/calmodulin-dependent protein kinase (CaMK-III). The kinase provides a mechanism by which cells can globally control the… (more)

▼ Eukaryotic elongation factor 2 kinase (eEF-2K) is an atypical calcium/calmodulin-dependent protein kinase (CaMK-III). The kinase provides a mechanism by which cells can globally control the rate of the elongation phase of protein synthesis, through inhibition of its only known substrate, elongation factor 2 (eEF-2). eEF-2K has been reported to promote proliferation, migration and survival of cancer cells, and has also been implicated in depression. Understanding the regulation of kinase activity is important for development of inhibitors to treat these disease states. However, the mechanisms through which upstream kinases regulate eEF-2K activity via multisite phosphorylation, and how calcium and calmodulin contribute to this, are still unclear. This deficiency may result from the difficulty of obtaining the recombinant kinase in a form suitable for biochemical analysis. This work reports the purification (a three-step protocol using a calmodulin-affinity column) and characterization of recombinant human eEF-2K expressed in E. coli. Mass spectrometry identified Thr-348 and Ser-500 as major calcium/calmodulin-stimulated autophosphorylation sites. Rapid quench analysis indicates that the rate of Thr-348 autophosphorylation is extremely fast (k = 2.6 s⁻¹, t [subscript ½] ~ 279 ms), and requires calmodulin. Mutagenesis studies suggest that phosphorylation at Thr-348 is required for eEF-2 phosphorylation both in vitro and in cells. However, while T348A has an overall lower activity than the WT kinase, the extent of stimulation of eEF-2K activity by 2-deoxy-D-glucose, hydrogen peroxide, ionomycin or cellular starvation is the same for both forms of the kinase. Thus, to control the amplitude of eEF-2K activity in cells following a stimulus that promotes calmodulin binding, phosphorylation at Thr-348 could act as an additional allosteric switch. This could potentially occur though interaction with a putative phosphate-binding pocket comprised of Lys-205, Arg-252 and Thr-254. Additionally, we observed that Ser-500 phosphorylation promotes an increase in affinity for calmodulin, and we provide evidence that Ser-500 phosphorylation on the eEF-2K•calmodulin complex significantly enhances the already rapid rate of Thr-348 autophosphorylation. Here we propose a two-step model involving calcium/calmodulin binding and Thr-348 autophosphorylation to modulate eEF-2K activity. Phosphorylation at Ser-500 is able to alter the kinetics at both these levels of regulation. Advisors/Committee Members: Dalby, Kevin N. (advisor), Digiovanni, John (committee member), Brodbelt, Jennifer S (committee member), Fast, Walter L (committee member), Bratton, Shawn B (committee member).

Subjects/Keywords: Elongation factor 2 kinase (eEF-2K); Calmodulin; Kinase; Protein synthesis; Calcium; eEF-2, Autophosphorylation; Thr-348; Ser-500

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Tavares, C. D. J. (2014). Regulation of elongation factor 2 kinase (eEF-2K) by phosphorylation. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/47184

Chicago Manual of Style (16^th Edition):

Tavares, Clint Damian Jaxon. “Regulation of elongation factor 2 kinase (eEF-2K) by phosphorylation.” 2014. Doctoral Dissertation, University of Texas – Austin. Accessed March 03, 2021. http://hdl.handle.net/2152/47184.

MLA Handbook (7^th Edition):

Tavares, Clint Damian Jaxon. “Regulation of elongation factor 2 kinase (eEF-2K) by phosphorylation.” 2014. Web. 03 Mar 2021.

Vancouver:

Tavares CDJ. Regulation of elongation factor 2 kinase (eEF-2K) by phosphorylation. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2014. [cited 2021 Mar 03]. Available from: http://hdl.handle.net/2152/47184.

Council of Science Editors:

Tavares CDJ. Regulation of elongation factor 2 kinase (eEF-2K) by phosphorylation. [Doctoral Dissertation]. University of Texas – Austin; 2014. Available from: http://hdl.handle.net/2152/47184

Penn State University

4. Huber-keener, Kathryn Joyce. Alterations In Gene Expression As A Response of Tumor Cells To Stresses .

Degree: 2013, Penn State University

URL: https://submit-etda.libraries.psu.edu/catalog/15352

► Cancer cells are constantly under stress, a factor which needs to be taken into consideration during the treatment of cancers. Both intrinsic and extrinsic stresses… (more)

▼ Cancer cells are constantly under stress, a factor which needs to be taken into consideration during the treatment of cancers. Both intrinsic and extrinsic stresses impact the development and progression of neoplasms, down to the level of individual proteins and genes. Stresses like nutrient deficiency, hypoxia, and the immune response are present during normal tumor growth and throughout treatment. Tumor cells that survive these stresses are more adept at surviving hostile conditions and are more resistant to current therapies. Stress, therefore, shapes the tumor cell population. Gene expression alterations are the driving feature behind the adaptive ability of cancer cells to these stresses, and therefore, careful examination of these gene expression changes must be undertaken in order to develop effective therapies. In the present investigations, we first explore the global alterations of gene expression in tamoxifen resistance. Resistance to tamoxifen (Tam), a widely used antagonist of the estrogen receptor (ER), occurs in one third of patients treated with Tam within 5 years of therapy. A better understanding of gene expression alterations associated with Tam resistance will facilitate circumventing this problem. Using a next generation sequencing approach and a new bioinformatics model, we compared the transcriptomes of Tam-sensitive and Tam-resistant breast cancer cells for identification of genes involved in the development of Tam resistance. We identified differential expression of 1215 mRNA and 513 small RNA transcripts clustered into ERα functions, cell cycle regulation, gen expression, and mitochondrial modification. The extent of alterations found at multiple levels of gene regulation highlights the ability of the Tam-resistant cells to modulate global gene expression. Alterations of small nucleolar RNA, oxidative phosphorylation, and a protein called SIRT3 in Tam-resistant cells present areas for diagnostic and therapeutic tool development for combating resistance to this anti-estrogen agent. After such a global exploration of cancer cell responses to stress, we next investigated a mechanism of cancer cell survival by exploring the alterations in protein synthesis inhibitor eEF-2K. Studies show that eEF-2K plays a role in cell survival through this inhibition of protein synthesis and that its protein levels are increased in cancer. Post-translational modification of translation machinery is important for its regulation and could be critical for survival of cancer cells encountering stress. Thus, the purpose of our study is to examine the regulation of eEF-2K during stress with a focus on the phosphorylation status and stability of EF-2K protein in cancer cells. Using two human glioma cell lines (T98G and LN229), under stress conditions, we found a paradoxical increase in eEF-2K protein expression with a decrease in eEF-2K protein stability. Phosphorylation may play a role in this altered protein stability as EF-2K has multiple phosphorylation sites that are phosphorylated by the… Advisors/Committee Members: Jin Ming Yang, Dissertation Advisor/Co-Advisor, Robert G Levenson, Committee Member, Rongling Wu, Committee Member, Willard Freeman, Committee Member, Andrea Manni, Committee Member.

Subjects/Keywords: eEF-2K; tamoxifen; glioma; breast cancer; protein synthesis; next generation-sequencing; protein stability

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Huber-keener, K. J. (2013). Alterations In Gene Expression As A Response of Tumor Cells To Stresses . (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/15352

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Huber-keener, Kathryn Joyce. “Alterations In Gene Expression As A Response of Tumor Cells To Stresses .” 2013. Thesis, Penn State University. Accessed March 03, 2021. https://submit-etda.libraries.psu.edu/catalog/15352.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Huber-keener, Kathryn Joyce. “Alterations In Gene Expression As A Response of Tumor Cells To Stresses .” 2013. Web. 03 Mar 2021.

Vancouver:

Huber-keener KJ. Alterations In Gene Expression As A Response of Tumor Cells To Stresses . [Internet] [Thesis]. Penn State University; 2013. [cited 2021 Mar 03]. Available from: https://submit-etda.libraries.psu.edu/catalog/15352.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Huber-keener KJ. Alterations In Gene Expression As A Response of Tumor Cells To Stresses . [Thesis]. Penn State University; 2013. Available from: https://submit-etda.libraries.psu.edu/catalog/15352

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation