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Literature DB >> 8598217

Impairment of mobility in endodermal cells by FAK deficiency.

D Ilić¹, S Kanazawa, Y Furuta, T Yamamoto, S Aizawa.

Abstract

Focal adhesion kinase (FAK) is a novel nonreceptor protein tyrosine kinase that localizes in focal adhesions. It is expressed in a variety of cell types, and we reported earlier that is deficiency causes a decrease of mobility in mesodermal cells with enhanced formation of focal adhesions. With embryoid bodies generated from embryonic stem cells, we also observed a decrease of mobility in FAK-deficient endodermal cells with enhanced focal adhesion formation.

Entities: Disease Gene

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Year: 1996 PMID： 8598217 DOI： 10.1006/excr.1996.0038

Source DB: PubMed Journal: Exp Cell Res ISSN： 0014-4827 Impact factor: 3.905

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Cited

15 in total

Review 1. Focal adhesion kinases: interest in immunoendocrinology, developmental biology, and cancer.

Authors: H J Martens; V Geenen
Journal: Endocrine Date: 2000-12 Impact factor: 3.633

2. Autosomal mutations affecting adhesion between wing surfaces in Drosophila melanogaster.

Authors: M Prout; Z Damania; J Soong; D Fristrom; J W Fristrom
Journal: Genetics Date: 1997-05 Impact factor: 4.562

Review 3. Central role of paxillin phosphorylation in regulation of LFA-1 integrins activity and lymphocyte migration.

Authors: Larisa Y Romanova; J Frederic Mushinski
Journal: Cell Adh Migr Date: 2011 Nov-Dec Impact factor: 3.405

4. Plasma membrane-associated pY397FAK is a marker of cytotrophoblast invasion in vivo and in vitro.

Authors: D Ilić; O Genbacev; F Jin; E Caceres; E A Almeida; V Bellingard-Dubouchaud; E M Schaefer; C H Damsky; S J Fisher
Journal: Am J Pathol Date: 2001-07 Impact factor: 4.307

5. SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading.

Authors: Leslie A Cary; Richard A Klinghoffer; Christoph Sachsenmaier; Jonathan A Cooper
Journal: Mol Cell Biol Date: 2002-04 Impact factor: 4.272

6. Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: a role for paxillin tyrosine phosphorylation.

Authors: A Richardson; R K Malik; J D Hildebrand; J T Parsons
Journal: Mol Cell Biol Date: 1997-12 Impact factor: 4.272

Impairment of mobility in endodermal cells by FAK deficiency.

Review 1. Focal adhesion kinases: interest in immunoendocrinology, developmental biology, and cancer.

2. Autosomal mutations affecting adhesion between wing surfaces in Drosophila melanogaster.

Review 3. Central role of paxillin phosphorylation in regulation of LFA-1 integrins activity and lymphocyte migration.

4. Plasma membrane-associated pY397FAK is a marker of cytotrophoblast invasion in vivo and in vitro.

5. SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading.

6. Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: a role for paxillin tyrosine phosphorylation.

7. Focal adhesion kinase is involved in mechanosensing during fibroblast migration.

8. A novel strategy to inhibit FAK and IGF-1R decreases growth of pancreatic cancer xenografts.

9. A novel small molecule inhibitor of FAK decreases growth of human pancreatic cancer.

10. Requirement of focal adhesion kinase in branching tubulogenesis.