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From G proteins to mitosis: Identify...

Kaplan, Daniel David.

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From G proteins to mitosis: Identifying new roles of the beta-catenin oncoprotein.

Record Type:	Electronic resources : Monograph/item
Title/Author:	From G proteins to mitosis: Identifying new roles of the beta-catenin oncoprotein./
Author:	Kaplan, Daniel David.
Description:	137 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2736.
Contained By:	Dissertation Abstracts International65-06B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3136822
ISBN:	0496840185

From G proteins to mitosis: Identifying new roles of the beta-catenin oncoprotein.
Kaplan, Daniel David.

From G proteins to mitosis: Identifying new roles of the beta-catenin oncoprotein. - 137 p.

Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2736.

Thesis (Ph.D.)--Duke University, 2004.

beta-Catenin is a multifunctional protein that is known to participate in two well-defined cellular processes, cell-cell adhesion and Wnt-stimulated transcriptional activation. In this thesis, I explored mechanisms by which cellular signals regulate these functions of beta-catenin. During this process, a novel function for beta-catenin in the establishment of a bipolar mitotic spindle was uncovered.

ISBN: 0496840185Subjects--Topical Terms:

1017686
Biology, Cell.

From G proteins to mitosis: Identifying new roles of the beta-catenin oncoprotein.
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245 1 0 $a From G proteins to mitosis: Identifying new roles of the beta-catenin oncoprotein.
300 $a 137 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2736.
500 $a Supervisor: Patrick J. Casey.
502 $a Thesis (Ph.D.)--Duke University, 2004.
520 $a beta-Catenin is a multifunctional protein that is known to participate in two well-defined cellular processes, cell-cell adhesion and Wnt-stimulated transcriptional activation. In this thesis, I explored mechanisms by which cellular signals regulate these functions of beta-catenin. During this process, a novel function for beta-catenin in the establishment of a bipolar mitotic spindle was uncovered.
520 $a Our laboratory recently demonstrated that heterotrimeric G proteins of the G12 subfamily specifically interact with the cadherin family of cell adhesion molecules, causing beta-catenin release from cadherin. In a follow-up to this study, I found that two distinct regions of the cadherin tail are required for interaction with beta-catenin and Galpha12, respectively. These findings indicate that Galpha12 and beta-catenin do not compete for the same binding site on cadherin, and allowed us to selectively disrupt the interaction of these proteins with cadherin. In doing so, we demonstrated that a cadherin mutant unable to interact with Galpha12 could still mediate cell adhesion, while a cadherin mutant unable to interact with beta-catenin could not. Furthermore, I found that expression of constitutively-active Galpha12 disrupted cadherin-mediated cell adhesion and that this response required the Galpha12-binding region of cadherin.
520 $a During mitosis, beta-catenin was found to re-localize to mitotic spindle poles and to the midbody. Importantly, this centrosomal translocation of beta-catenin was independent of the adenomatous polyposis coli protein and Wnt signaling. The proper localization of beta-catenin to centrosomes appeared to involve dynein, a microtubule motor critical for mitotic spindle formation. Reduction of cellular beta-catenin by RNA interference led to numerous mitotic defects, including a prometaphase block, mitotic cell death, and aberrant cytokinesis. The prometaphase block appeared to result from the failure of centrosomes to fully separate, as I observed a marked increase in the frequency of monoastral mitotic spindles in beta-catenin siRNA-treated cells. Analysis of time-lapse phase-contrast images, together with three-dimensional reconstructions of monoastral spindles resulting from beta-catenin siRNA treatment, revealed that these monoastral spindles likely result from the collapse of partially-formed spindles. My results define a new and important function for beta-catenin in mitosis and demonstrate that beta-catenin is involved in vital biological processes beyond cell adhesion and Wnt signaling.
590 $a School code: 0066.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Health Sciences, Pharmacology. $3 1017717
650 4 $a Chemistry, Biochemistry. $3 1017722
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710 2 0 $a Duke University. $3 569686
773 0 $t Dissertation Abstracts International $g 65-06B.
790 1 0 $a Casey, Patrick J., $e advisor
790 $a 0066
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3136822