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  The guanine nucleotide exchange factor C3G is necessary for the formation of focal adhesions and vascular maturation

Voss, A. K., Gruss, P., & Thomas, T. (2003). The guanine nucleotide exchange factor C3G is necessary for the formation of focal adhesions and vascular maturation. Development, 130(2), 355-367. Retrieved from http://dev.biologists.org/content/130/2/355.full.pdf+html.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F1A7-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E40D-C
Genre: Journal Article

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 Creators:
Voss, A. K.1, Author              
Gruss, P.1, Author              
Thomas, T., Author
Affiliations:
1Department of Molecular Cell Biology, MPI for biophysical chemistry, Max Planck Society, ou_578585              

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Free keywords: C3G; Ras signalling; vascular development; focal adhesions; integrins; PDGF
 Abstract: The Ras signalling pathway has major roles in normal cell function and oncogenesis. C3G is a guanine nucleotide exchange factor for members of the Ras family of GTPases. We generated a mouse strain with a hypomorphic C3G allele. C3G(gt/gt) mutant embryos died of vascular defects around E11.5 due to haemorrhage and vascular integrity defects. Vascular supporting cells did not develop appropriately. C3G-deficient fibroblasts responded to PDGF-BB abnormally, exhibited cell adhesion defects and lacked paxillin and integrin-beta1-positive cell adhesions. In contrast, integrin-beta3-positive cell adhesions formed normally. These results show that C3G is required for (1) vascular myogenesis, (2) the formation of paxillin- and integrin beta1-positive, but not integrin beta3-positive, cell adhesions and (3) normal response to PDGF, necessary for vascular myogenesis.

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Language(s): eng - English
 Dates: 2003-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: Development
Source Genre: Journal
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Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 130 (2) Sequence Number: - Start / End Page: 355 - 367 Identifier: -