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January 24, 2010 | History

Role of Sp1 phosphorylation in mechanotranscriptional activation of filamin A 1 edition

Role of Sp1 phosphorylation in mechanotranscriptional activation of fi ...
Mario D'Addario

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Role of Sp1 phosphorylation in mechanotranscriptional activation of filamin A.

Published 2005 .
Written in English.

About the Book

Connective tissue cells survive mechanical forces by inducing the expression of filamin A, an actin cross-linking protein that inhibits force-induced cell death. Filamin A expression is dependent on p38 activation and Sp-1 binding to the filamin promoter. Force application through integrins increased filamin promoter activity by >5-fold but was blocked by mutations to Sp1 binding sites in the filamin promoter. In Sp deficient SL2 cells, transfection with wild-type but not mutant Sp1 caused phosphorylation of Sp1 at both Thr453 and Thr739 and enhanced binding of nuclear extracts to a filamin promoter. Sp1 phosphorylated at Thr453 and Thr739 by p38 bound to filamin promoter more than unphosphorylated Sp1. Recombinant active p38 phosphorylated wild-type Sp1 but not the Sp1T453A-T739A double mutant protein in vitro. We conclude that filamin A expression is increased by p38-induced phosphorylation of Sp1 at specific threonine residues that in turn enhances binding to the filamin promoter.

Edition Notes

Source: Masters Abstracts International, Volume: 44-02, page: 0806.

Thesis (M.Sc.)--University of Toronto, 2005.

Electronic version licensed for access by U. of T. users.

GERSTEIN MICROTEXT copy on microfiche (1 microfiche).

The Physical Object

Pagination
82 leaves.
Number of pages
82

ID Numbers

Open Library
OL19216671M
ISBN 10
049407227X

History Created December 11, 2009 · 2 revisions Download catalog record: RDF / JSON

January 24, 2010 Edited by WorkBot add more information to works
December 11, 2009 Created by WorkBot add works page