Activation of endogenous FAK via expression of its amino terminal domain in Xenopus embryos.

Bibliographic Details
Title: Activation of endogenous FAK via expression of its amino terminal domain in Xenopus embryos.
Authors: Nicoletta I Petridou, Panayiota Stylianou, Neophytos Christodoulou, Daniel Rhoads, Jun-Lin Guan, Paris A Skourides
Source: PLoS ONE, Vol 7, Iss 8, p e42577 (2012)
Publisher Information: Public Library of Science (PLoS), 2012.
Publication Year: 2012
Collection: LCC:Medicine
LCC:Science
Subject Terms: Medicine, Science
More Details: BACKGROUND: The Focal Adhesion Kinase is a well studied tyrosine kinase involved in a wide number of cellular processes including cell adhesion and migration. It has also been shown to play important roles during embryonic development and targeted disruption of the FAK gene in mice results in embryonic lethality by day 8.5. PRINCIPAL FINDINGS: Here we examined the pattern of phosphorylation of FAK during Xenopus development and found that FAK is phosphorylated on all major tyrosine residues examined from early blastula stages well before any morphogenetic movements take place. We go on to show that FRNK fails to act as a dominant negative in the context of the early embryo and that the FERM domain has a major role in determining FAK's localization at the plasma membrane. Finally, we show that autonomous expression of the FERM domain leads to the activation of endogenous FAK in a tyrosine 397 dependent fashion. CONCLUSIONS: Overall, our data suggest an important role for the FERM domain in the activation of FAK and indicate that integrin signalling plays a limited role in the in vivo activation of FAK at least during the early stages of development.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1932-6203
Relation: http://europepmc.org/articles/PMC3412797?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0042577
Access URL: https://doaj.org/article/3570a83bd1c8434e8a6b751b5e340eb4
Accession Number: edsdoj.3570a83bd1c8434e8a6b751b5e340eb4
Database: Directory of Open Access Journals
More Details
ISSN:19326203
DOI:10.1371/journal.pone.0042577
Published in:PLoS ONE
Language:English