Ack-1 Tyrosine Kinase Regulates Integrin Signaling Leading to Breast Cell Migration
Abstract
Appropriate interactions between breast cells and the ECM via alpha2beta 1 integrin help to establish normal cellular structure and differentiation. During transformation to a carcinoma, these normal interactions with the ECM are profoundly altered, resulting in cells that lose their specialization and lose control of their growth. Ultimately, these cells become invasive, and then migrate through the connective tissue environment to form distant metastases. We have previously found that Ack 1 tyrosine kinase enhances alpha2beta 1 integrin-induced cell migration and regulates signaling components downstream of the integrin. In the course of the research I have determined that Ack-1 is phosphorylated upon collagen stimulation and that this phosphorylation is dependent on Src and FAK kinases. Furthermore, I found that FAK is not required for Ack-l association with p130Cas or Src and that Src is not necessary for p130Cas and FAK association with Ack-1. I also determined that Ack-1 associates with the SH3 domains of p130Cas, Src and Spectrin, which suggest direct binding between these molecules.
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 01, 2003
- Accession Number
- ADA415773
Entities
People
- Katarzyna Modzelewska
- Patricia J. Keely
Organizations
- University of Wisconsin–Madison