FAK regulates tyrosine phosphorylation of CAS, paxillin, and PYK2 in cells expressing v-Src, but is not a critical determinant of v-Src transformation
✍ Scribed by Shyamali Roy; Paul J. Ruest; Steven K. Hanks
- Book ID
- 102299508
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- English
- Weight
- 337 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
Abstract
FAK (focal adhesion kinase) is a nonreceptor protein‐tyrosine kinase activated by tyrosine phosphorylation following integrin‐mediated cell adhesion. Oncogenic Src promotes enhanced and deregulated FAK tyrosine phosphorylation which has been proposed to contribute to altered cell growth and/or morphological properties associated with transformation. In this study, an inducible FAK expression system was used to study the potential role of FAK in v‐Src transformation. Our results portray FAK as a major v‐Src substrate that also plays a role in recruiting v‐Src to phosphorylate substrates CAS (Crk‐associated substrate) and paxillin. The FAK Tyr‐397 autophosphorylation site was necessary for this scaffolding function, but was not required for v‐Src to stably interact with and phosphorylate FAK. FAK was also shown to negatively regulate v‐Src mediated phosphorylation of the FAK‐related kinase PYK2. Despite these effects, FAK does not play an essential role in targeting v‐Src to major cellular substrates including CAS and paxillin. Nor is FAK strictly required to achieve the altered morphological and growth characteristics of v‐Src transformed cells. J. Cell. Biochem. 84: 377–388, 2002. © 2001 Wiley‐Liss, Inc.