Advanced

Focal Adhesion-associated Proteins p125FAK and Paxillin Are Substrates for Bradykinin-stimulated Tyrosine Phosphorylation in Swiss 3T3 Cells

Leeb-Lundberg, L. M Fredrik LU ; Song, Xin Hua and Mathis, Sandra A. (1994) In Journal of Biological Chemistry 269(39). p.24328-24334
Abstract

In this study we examined the involvement of the focal adhesion-associated proteins p125FAK and paxillin as substrates for bradykinin (BK)-stimulated tyrosine phosphorylation in Swiss 3T3 cells and the potential role of protein kinase C and Ca2+ in these events. BK (1 UM) stimulated tyrosine phosphorylation of p125FAK and paxillin. In addition, BK also increased the phosphotyrosine content of the src transformation-associated protein p130. The responses were rapid and transient and peaked at ∼1 min after BK addition. Furthermore, the responses were dose-dependent with half-maximal effects occurring at 1-10 nM BK. The phosphotyrosine content of p125FAK, paxillin, and p130 was also increased... (More)

In this study we examined the involvement of the focal adhesion-associated proteins p125FAK and paxillin as substrates for bradykinin (BK)-stimulated tyrosine phosphorylation in Swiss 3T3 cells and the potential role of protein kinase C and Ca2+ in these events. BK (1 UM) stimulated tyrosine phosphorylation of p125FAK and paxillin. In addition, BK also increased the phosphotyrosine content of the src transformation-associated protein p130. The responses were rapid and transient and peaked at ∼1 min after BK addition. Furthermore, the responses were dose-dependent with half-maximal effects occurring at 1-10 nM BK. The phosphotyrosine content of p125FAK, paxillin, and p130 was also increased following stimulation with phorbol 12-myristate 13-acetate (PMA) (0.1 μM). In contrast, PMA had no effect on the phosphotyrosine content of p125, a Ras-GAP-associated tyrosine phosphoprotein that we recently identified. Long term pretreatment (18 h) of cells with 0.3 μM PMA partially attenuated BK-stimulated phosphorylation of p125FAK but was without effect on phosphorylation of paxillin and Ras-GAP-associated p125. Furthermore, only a small inhibition of BK- and PMA-stimulated phosphorylation of p125FAK was observed following pretreatment with 25 μM BAPTA/AM. In all, these results show that multiple mechanisms are involved in BK-stimulated tyrosine phosphorylation of p125FAK, paxillin, RasGAP-associated p125, and src transformation-associated p130.

(Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
269
issue
39
pages
24328 - 24334
publisher
ASBMB
external identifiers
  • pmid:7929090
  • scopus:0028071784
ISSN
0021-9258
language
English
LU publication?
no
id
67e8e285-8096-4064-8f4d-da59c9630333
alternative location
http://www.jbc.org/content/269/39/24328.abstract
date added to LUP
2019-06-12 11:42:06
date last changed
2019-11-25 09:31:23
@article{67e8e285-8096-4064-8f4d-da59c9630333,
  abstract     = {<p>In this study we examined the involvement of the focal adhesion-associated proteins p125<sup>FAK</sup> and paxillin as substrates for bradykinin (BK)-stimulated tyrosine phosphorylation in Swiss 3T3 cells and the potential role of protein kinase C and Ca<sup>2+</sup> in these events. BK (1 UM) stimulated tyrosine phosphorylation of p125<sup>FAK</sup> and paxillin. In addition, BK also increased the phosphotyrosine content of the src transformation-associated protein p130. The responses were rapid and transient and peaked at ∼1 min after BK addition. Furthermore, the responses were dose-dependent with half-maximal effects occurring at 1-10 nM BK. The phosphotyrosine content of p125<sup>FAK</sup>, paxillin, and p130 was also increased following stimulation with phorbol 12-myristate 13-acetate (PMA) (0.1 μM). In contrast, PMA had no effect on the phosphotyrosine content of p125, a Ras-GAP-associated tyrosine phosphoprotein that we recently identified. Long term pretreatment (18 h) of cells with 0.3 μM PMA partially attenuated BK-stimulated phosphorylation of p125<sup>FAK</sup> but was without effect on phosphorylation of paxillin and Ras-GAP-associated p125. Furthermore, only a small inhibition of BK- and PMA-stimulated phosphorylation of p125<sup>FAK</sup> was observed following pretreatment with 25 μM BAPTA/AM. In all, these results show that multiple mechanisms are involved in BK-stimulated tyrosine phosphorylation of p125<sup>FAK</sup>, paxillin, RasGAP-associated p125, and src transformation-associated p130.</p>},
  author       = {Leeb-Lundberg, L. M Fredrik and Song, Xin Hua and Mathis, Sandra A.},
  issn         = {0021-9258},
  language     = {eng},
  month        = {09},
  number       = {39},
  pages        = {24328--24334},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Focal Adhesion-associated Proteins p125FAK and Paxillin Are Substrates for Bradykinin-stimulated Tyrosine Phosphorylation in Swiss 3T3 Cells},
  url          = {http://www.jbc.org/content/269/39/24328.abstract},
  volume       = {269},
  year         = {1994},
}