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Grb7 and Filamin‐a associate and are colocalized to cell membrane ruffles upon EGF stimulation
Authors:Prakash Paudyal  Sanjay Shrestha  Thushara Madanayake  Charles B Shuster  Larry R Rohrschneider  Aaron Rowland  Barbara A Lyons
Institution:1. Department of Chemistry and Biochemistry, New Mexico State University, , Las Cruces, NM, 88003 USA;2. Department of Biology, New Mexico State University, , Las Cruces, NM, 88003 USA;3. Basic Sciences Division, Fred Hutchinson Cancer Research Center, , Seattle, WA, 98109 USA
Abstract:Grb7 is an adaptor molecule mediating signal transduction from multiple cell surface receptors to diverse downstream pathways. Grb7, along with Grb10 and Grb14, make up the Grb7 protein family. This protein family has been shown to be overexpressed in certain cancers and cancer cell lines. Grb7 and a receptor tyrosine kinase, ErbB2, are overexpressed in 20–30% of breast cancers. Grb7 overexpression has been linked to enhanced cell migration and metastasis, although the participants in these pathways have not been fully determined. In this study, we report the Grb7 protein interacts with Filamin‐a, an actin‐crosslinking component of the cell cytoskeleton. Additionally, we have demonstrated the interaction between Grb7 and Flna is specific to the RA‐PH domains of Grb7, and the immunoglobulin‐like repeat 16–19 domains of Flna. We demonstrate that full‐length Grb7 and Flna interact in the mammalian cellular environment, as well as in vitro. Immunofluorescent microscopy shows potential co‐localization of Grb7 and Flna in membrane ruffles upon epidermal growth factor stimulation. These studies are amongst the first to establish a clear connection between Grb7 signaling and cytoskeletal remodeling. Copyright © 2013 John Wiley & Sons, Ltd.
Keywords:Grb7  ErbB2  HER2  neu  cell migration  cytoskeleton  actin binding  Filamin‐a
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