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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
41

Characterization of the Interaction of Alpha4 Phosphoprotein with Novel Binding Partners: EDD E3 Ubiquitin Ligase and Poly(A)-Binding Protein

McDonald, William 22 March 2011 (has links)
?4 phosphoprotein (also known as IGBP1) is a component of the mammalian target-of-rapamycin (mTOR) pathway that controls the initiation of translation and cell-cycle progression in response to nutrients and growth factors. Aberrant signaling of the mTOR pathway has been reported in many cancers. ?4 interacts with the catalytic subunit of protein phosphtase 2A (PP2Ac) to mediate the dephosphorylation of eukaryotic initiation factor 4E-binding protein1 (4E-BP1) and p70S6 kinase (p70S6K). Our laboratory has reported that EDD E3 ubiquitin ligase (EDD/UBR5) and poly(A)-binding protein (PABP) are novel binding partners of ?4 phosphoprotein. In the present study, the interaction of EDD and PABP with ?4 was confirmed in human MCF-7 breast cancer and African green monkey COS-1 kidney cell lines, using immunoprecipitation and immunoblotting (IP/IB) analysis. However, co-IP of total MCF-7 cell lysates with anti-EDD antibodies revealed that EDD does not physically interact with PP2Ac. Several ?4 deletion constructs, that contained either the N-terminal or C-terminal regions of ?4, were transfected into MCF-7 and COS-1 cells. Co-IP studies with anti-EDD and PABP antibodies revealed that EDD interacts with the C-terminal region of ?4 whereas PABP, like PP2Ac, binds to the N-terminal region. EDD and PABP were found to interact with ?4 in both quiescent and actively growing cells. EDD is known to ubiquitinate poly(A)-binding protein-interacting protein 2 (Paip2), targeting it for proteosomal degradation. Paip2 is an antagonist of PABP activity. When ?4 levels in MCF-7 cells were knocked down using small interfering RNA (siRNA), there was no effect on EDD protein levels. There was also no effect on Paip2 levels, indicating that ?4 is not involved in the EDD- mediated ubiquitination of Paip2. Knockdown of EDD gene expression by siRNA did not alter mono-ubiquitination of ?4, indicating that ?4 is not a substrate of EDD. However, knockdown of EDD gene expression decreased poly-ubiquitination of PP2Ac and increased the overall cellular levels of PP2Ac, suggesting PP2Ac as a novel substrate of EDD. The present study suggests a potential role for ?4 in PABP-mediated initiation of mRNA translation. Furthermore, this study suggests a role for EDD in regulating PP2Ac levels through its interaction with ?4. In summary, the ?4 partners EDD, PABP and PP2Ac interact at specific regions of ?4. PP2Ac, but not ?4, is a substrate of EDD. The interaction of PABP with ?4 suggests a potential role for ?4 in PABP-mediated initiation of mRNA translation.
42

Analysis of timekeeper implicates antagonism between CK2 and PP2A during Drosophila neurogenesis

Kunttas, Ezgi. January 1900 (has links)
Thesis (M.S.)--West Virginia University, 2008. / Title from document title page. Document formatted into pages; contains ix, 128 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 118-127).
43

Polymer-modified plates for enrichment of phosphopeptides prior to analysis by matrix-assisted laser desorption/ionization mass spectrometry

Dunn, Jamie D. January 2007 (has links)
Thesis (Ph. D.)--Michigan State University. Dept. of Chemistry, 2007. / Title from PDF t.p. (viewed on Apr. 16, 2009) Includes bibliographical references. Also issued in print.
44

Regulation of mitotic exit in S. pombe through activation of a Cdc14 family phosphate

Wolfe, Benjamin A. January 2005 (has links)
Thesis (Ph. D. in Cell and Developmental Biology)--Vanderbilt University, May 2005. / Title from title screen. Includes bibliographical references.
45

Regulation of nerve growth factor signaling by protein phosphatase 2A

Van Kanegan, Michael J.. Strack, Stefan. January 2008 (has links)
Thesis supervisor: Stefan Strack. Includes bibliographic references (p. 87-100).
46

Regulation of the neuromuscular junction by protein tyrosine phosphatases /

Tanowitz, Michael Brian. January 2000 (has links)
Thesis (Ph. D.)--University of Virginia, 2000. / Spine title: Synaptic role of TYR-phosphatases. Includes bibliographical references (p. 135-172). Also available online through Digital Dissertations.
47

Genetic and biochemical analysis of the interaction between unc-44 AO13 ankyrin and protein phosphatase 2A

Gong, Ping. Otsuka, Anthony John, January 2005 (has links)
Thesis (Ph. D.)--Illinois State University, 2005. / Title from title page screen, viewed September 26, 2006. Dissertation Committee: Anthony J. Otsuka (chair), Radheshyam Jayaswal, Kevin A. Edwards, David L. Williams, Hou Tak Cheung. Includes bibliographical references (leaves 110-124) and abstract. Also available in print.
48

Dopamine depletion alters the balance between Ca²⁺/calmodulin-dependent protein kinase II and protein phosphatase I

Brown, Abigail Maureen. January 2007 (has links)
Thesis (Ph. D. in Molecular Physiology and Biophysics)--Vanderbilt University, Aug. 2007. / Title from title screen. Includes bibliographical references.
49

Observations On Phosvitin-Protein Interactions : Implications Of Their Biological Significance

Lakhey, Hitendra V 09 1900 (has links) (PDF)
No description available.
50

Actions of Secreted Phosphoprotein 1 in the Bovine Corpus Luteum and the Role of Resident T Lymphocytes during Luteolysis

Poole, Daniel Heath 25 September 2009 (has links)
No description available.

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