Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Adp-ribosylation factor 4 small gtpase mediates epidermal growth factor receptor-dependent phospholipase d2 activation

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Kim, S. W.
  • Hayashi, M.
  • Lo, J. F.
  • Yang, Y.
  • Yoo, J. S.
  • Lee, Jiing-Dwan

publication date

  • January 2003

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The epidermal growth factor receptor (EGFR) plays a critical role in the development, proliferation, and differentiation of cells of epithelial and mesenchymal origin. These EGFR-dependent cellular processes are mediated by a repertoire of intracellular signaling pathways triggered by the activation of the EGFR cytoplasmic domain, which originates from ligand binding of its extracellular domain. To understand the molecular mechanisms by which the intracellular domain of EGFR transmits mitogenic messages to the downstream signaling pathways, we used the cytoplasmic region of EGFR as bait in yeast two-hybrid screening. We found that ADP-ribosylation factor 4 (ARF4) interacts with the intracellular part of EGFR and mediates the EGF-dependent cellular activation of phospholipase D2 (PLD2) but does not mediate the activation of PLD1. In addition, ARF4-mediated PLD2 activation leads to dramatic activation of the transcription factor activator protein 1 (AP-1), and, importantly, ARF4 activity is required for EGF-induced activation of cellular AP-1. Our findings indicate that ARF4 is a critical molecule that directly regulates cellular PLD2 activity and that this ARF4-mediated PLD2 activation stimulates AP-1-dependent transcription in the EGF-induced cellular response.

subject areas

  • ADP-Ribosylation Factors
  • Cell Line
  • Cell Line, Transformed
  • Cell Membrane
  • Cytoplasm
  • DNA
  • DNA, Complementary
  • Digitonin
  • Enzyme Activation
  • Epidermal Growth Factor
  • GTP Phosphohydrolases
  • Gene Library
  • Genes, Reporter
  • Green Fluorescent Proteins
  • Growth Substances
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • Humans
  • Luminescent Proteins
  • Microscopy, Fluorescence
  • Phospholipase D
  • Precipitin Tests
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • Transcription Factor AP-1
  • Transcription, Genetic
  • Two-Hybrid System Techniques
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M205819200

PubMed ID

  • 12446727
scroll to property group menus

Additional Document Info

start page

  • 2661

end page

  • 2668

volume

  • 278

issue

  • 4

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support