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  Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation

Sakai, T., Li, S. H., Docheva, D., Grashoff, C., Sakai, K., Kostka, G., et al. (2003). Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation. Genes & Development, 17(7), 926-940.

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Genre: Journal Article
Alternative Title : Genes Dev.

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 Creators:
Sakai, T.1, Author              
Li, S. H., Author
Docheva, D.1, Author              
Grashoff, C.1, 2, Author              
Sakai, K.1, Author              
Kostka, G.1, Author              
Braun, A.1, Author              
Pfeifer, A., Author
Yurchenco, P. D., Author
Fässler, R.1, Author              
Affiliations:
1Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
2Grashoff, Carsten / Molecular Mechanotransduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565150              

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Free keywords: integrin; integrin-linked kinase (ILK); epiblast; knockout
 Abstract: Integrin-mediated cell-matrix interactions are essential for development, tissue homeostasis, and repair. Upon ligand binding, integrins are recruited into focal adhesions (FAs). Integrin-linked kinase (ILK) is an FA component that interacts with the cytoplasmic domains of integrins, recruits adaptor proteins that link integrins to the actin cytoskeleton, and phosphorylates the serine/threonine kinases PKB/Akt and GSK-30. Here we show that mice lacking ILK expression die at the peri- implantation stage because they fail to polarize their epiblast and to cavitate. The impaired epiblast polarization is associated with abnormal F-actin accumulation at sites of integrin attachments to the basement membrane (BM) zone. Likewise, ILK-deficient fibroblasts showed abnormal F-actin aggregates associated with impaired cell spreading and delayed formation of stress fibers and FAs. Finally, ILK-deficient fibroblasts have diminished proliferation rates. However, insulin or PDGF treatment did not impair phosphorylation of PKB/Akt and GSK-3beta, indicating that the proliferation defect is not due to absent or reduced ILK-mediated phosphorylation of these substrates in vivo. Furthermore, expression of a mutant ILK lacking kinase activity and/or paxillin binding in ILK- deficient fibroblasts can rescue cell spreading, F-actin organization, FA formation, and proliferation. Altogether these data show that mammalian ILK modulates actin rearrangements at integrin-adhesion sites.

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Language(s): eng - English
 Dates: 2003-04-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41415
ISI: 000182044700012
 Degree: -

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Title: Genes & Development
  Alternative Title : Genes Dev.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 17 (7) Sequence Number: - Start / End Page: 926 - 940 Identifier: ISSN: 0890-9369