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The actin cytoskeleton and the actin...

Posey Morley, Sharon Celeste.

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The actin cytoskeleton and the actin-binding protein gelsolin in T cell signal transduction.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	The actin cytoskeleton and the actin-binding protein gelsolin in T cell signal transduction./
Author:	Posey Morley, Sharon Celeste.
Description:	403 p.
Notes:	Adviser: Barbara E. Bierer.
Contained By:	Dissertation Abstracts International63-04B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3051263
ISBN:	0493658378

The actin cytoskeleton and the actin-binding protein gelsolin in T cell signal transduction.
Posey Morley, Sharon Celeste.

The actin cytoskeleton and the actin-binding protein gelsolin in T cell signal transduction. - 403 p.

Adviser: Barbara E. Bierer.

Thesis (Ph.D.)--Harvard University, 2002.

Understanding the spatial organization of signaling molecules is critical to understanding the outcome of signaling events. During T cell signal transduction, TCR engagement by a ligand of sufficient affinity stimulates the formation of a highly ordered array of signaling elements, termed a supramolecular activation complex (SMAC). TCR engagement by altered peptide ligands with reduced affinity for the TCR result in the formation of a disordered SMAC and a failure to transduce an activating signal. The mechanisms that drive the formation of signaling complexes, and the mechanisms by which the organization of such complexes is maintained, are not yet well understood. Critical to these processes is the reorganization of the actin cytoskeleton.

ISBN: 0493658378Subjects--Topical Terms:

1017686
Biology, Cell.

The actin cytoskeleton and the actin-binding protein gelsolin in T cell signal transduction.
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005 20110425
008 110425s2002 eng d
020 $a 0493658378
035 $a (UnM)AAI3051263
035 $a AAI3051263
040 $a UnM $c UnM
100 1 $a Posey Morley, Sharon Celeste. $3 1251329
245 1 0 $a The actin cytoskeleton and the actin-binding protein gelsolin in T cell signal transduction.
300 $a 403 p.
500 $a Adviser: Barbara E. Bierer.
500 $a Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1777.
502 $a Thesis (Ph.D.)--Harvard University, 2002.
520 $a Understanding the spatial organization of signaling molecules is critical to understanding the outcome of signaling events. During T cell signal transduction, TCR engagement by a ligand of sufficient affinity stimulates the formation of a highly ordered array of signaling elements, termed a supramolecular activation complex (SMAC). TCR engagement by altered peptide ligands with reduced affinity for the TCR result in the formation of a disordered SMAC and a failure to transduce an activating signal. The mechanisms that drive the formation of signaling complexes, and the mechanisms by which the organization of such complexes is maintained, are not yet well understood. Critical to these processes is the reorganization of the actin cytoskeleton.
520 $a I have investigated the role of the actin cytoskeleton in T cell signal transduction leading to both T cell activation and apoptosis. I have demonstrated that perturbation of actin cytoskeletal dynamics by treatment with the actin modifying compounds jasplakinolide or cytochalasin D enhanced commitment to apoptosis in a model system of lymphocyte apoptosis induced by cytokine deprivation. By overexpression of gelsolin, an actin-binding protein, I have addressed the role of gelsolin in signaling to apoptosis in model systems of lymphocyte apoptosis induced by cytokine deprivation, ceramide treatment, and Fas ligation. I have further investigated the participation of gelsolin and the regulation of actin dynamics in TCR-mediated signal transduction, and demonstrate that overexpression of gelsolin altered tyrosine phosphorylation patterns of substrates associated with lipid raft membrane microdomains, and this alteration of phosphorylation patterns correlated with inhibition of NF-AT transcriptional activation and IL-2 production. Finally, I have begun to characterize the possible dependence of T cell signaling on gelsolin in model systems of lymphocyte development and function utilizing lymphocytes isolated from gelsolin null mice. I thus provide clear evidence that the actin cytoskeleton participates in T cell signal transduction, and have begun to define the mechanisms by which it does so.
590 $a School code: 0084.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Health Sciences, Immunology. $3 1017716
690 $a 0379
690 $a 0982
710 2 0 $a Harvard University. $3 528741
773 0 $t Dissertation Abstracts International $g 63-04B.
790 $a 0084
790 1 0 $a Bierer, Barbara E., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3051263