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Focal adhesion kinase and Grb7 in in...

Shen, Tang-Long.

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Focal adhesion kinase and Grb7 in integrin signaling in cell migration.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Focal adhesion kinase and Grb7 in integrin signaling in cell migration./
Author:	Shen, Tang-Long.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2003,
Description:	230 p.
Notes:	Source: Dissertation Abstracts International, Volume: 63-12, Section: B, page: 5628.
Contained By:	Dissertation Abstracts International63-12B.
Subject:	Cellular biology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3075890
ISBN:	9780493961835

Focal adhesion kinase and Grb7 in integrin signaling in cell migration.
Shen, Tang-Long.

Focal adhesion kinase and Grb7 in integrin signaling in cell migration. - Ann Arbor : ProQuest Dissertations & Theses, 2003 - 230 p.

Source: Dissertation Abstracts International, Volume: 63-12, Section: B, page: 5628.

Thesis (Ph.D.)--Cornell University, 2003.

The transmembrane adhesion receptors, integrins, binding to extracellular matrix (ECM) proteins, are essential for cell migration. Not only can integrins link ECM molecules to the cytoskeleton, they also transmit signals that regulate cell migration. Focal adhesion kinase (FAK) plays a central role in integrin-mediated signaling pathways. The activation, localization, and cellular functions of FAK are intimately regulated by integrins. Nevertheless, the mechanism of FAK-mediated cell migration is not fully understood. This dissertation attempts to understand the molecular mechanism of FAK- and Grb7-mediated cell migration in integrin signaling.

ISBN: 9780493961835Subjects--Topical Terms:

3172791
Cellular biology.

Focal adhesion kinase and Grb7 in integrin signaling in cell migration.
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100 1 $a Shen, Tang-Long. $3 3283780
245 1 0 $a Focal adhesion kinase and Grb7 in integrin signaling in cell migration.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2003
300 $a 230 p.
500 $a Source: Dissertation Abstracts International, Volume: 63-12, Section: B, page: 5628.
500 $a Adviser: Jun-Lin Guan.
502 $a Thesis (Ph.D.)--Cornell University, 2003.
520 $a The transmembrane adhesion receptors, integrins, binding to extracellular matrix (ECM) proteins, are essential for cell migration. Not only can integrins link ECM molecules to the cytoskeleton, they also transmit signals that regulate cell migration. Focal adhesion kinase (FAK) plays a central role in integrin-mediated signaling pathways. The activation, localization, and cellular functions of FAK are intimately regulated by integrins. Nevertheless, the mechanism of FAK-mediated cell migration is not fully understood. This dissertation attempts to understand the molecular mechanism of FAK- and Grb7-mediated cell migration in integrin signaling.
520 $a In addition to functioning as a tyrosine kinase, FAK may act as a docking protein that recruits other signaling molecules to focal adhesions to mediate downstream signaling. To investigate this possibility, several FAK interacting proteins fused with FAT were constructed and they exhibited focal adhesion localization as expected. Overexpression of Src-FAT, p85-FAT and Grb7-FAT chimeras stimulated cell migration. However, Grb2-FAT, but not other chimeras, enhanced cell proliferation. These data provided further support for the scaffold mechanism of FAK in mediating integrin signaling (Chapter 2).
520 $a Grb7 is capable of interacting with FAK to mediate cell migration. Grb7's GM domain is responsible for downstream signaling in cell migration. Yet, it is unknown how this region regulates cell migration. In speculation of the Grb7's PH domain (within the GM domain) binding to phospholipids, a Grb7 mutant (R239L) incapable of binding to phospholipids abolished Grb7-stimulated cell migration (Chapter 3). Further investigation has indicated that Grb7 binding to D3-phosphoinositides is required for FAK phosphorylating Grb7 and for Grb7-mediated cell migration. These data suggest that Grb7 can be modulated by PI3K and FAK in mediating cell migration (Chapter 3).
520 $a EphB1 receptor associates with Grb7 in a phosphorylation dependent manner and phosphorylates Grb7. The tyrosine phosphorylation of Grb7 by EphB1 is necessary for Grb7-stimulated cell migration (Chapter 4). Together, these data highlight that tyrosine phosphorylation of Grb7 is necessary in integrin-mediated cell migration.
520 $a To date, the physiological role of FAK remains to be elucidated. The appendix describes a Cre/loxP system for the conditional knockout in FAK alleles to overcome the early embryonic lethality that occurs using a conventional knockout approach.
590 $a School code: 0058.
650 4 $a Cellular biology. $3 3172791
650 4 $a Biochemistry. $3 518028
690 $a 0379
690 $a 0487
710 2 $a Cornell University. $3 530586
773 0 $t Dissertation Abstracts International $g 63-12B.
790 $a 0058
791 $a Ph.D.
792 $a 2003
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3075890