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As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website.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

The growth-promoting activity of the bad protein in chicken embryo fibroblasts requires binding to protein 14-3-3

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

Overview

authors

  • Maslyar, D. J.
  • Aoki, M.
  • Vogt, Peter K.

publication date

  • August 2001

journal

  • Oncogene  Journal

abstract

  • Phosphorylation of the Bad protein is a key regulatory event in the prevention of apoptosis by survival factors. Phosphorylated Bad binds to the cytosolic 14-3-3 protein and is sequestered from the apoptotic machinery of the mitochondrial membrane. To examine the role of Bad in cell growth and apoptosis in primary cultures, we produced stable Bad transfectants of chicken embryo fibroblasts (CEF). As expected, serum starvation of Bad transfectants promoted apoptosis. However, Bad-transfected CEF maintained in media with a high serum concentration were capable of anchorage-independent growth and grew to a higher saturation density than control CEF transfected with the empty vector. High dilutions of the infectious retroviral vector RCAS expressing Bad led to the formation of multilayered cell foci. The growth-promoting effects of Bad were dependent on the serine 136 phosphorylation site and correlated directly with binding of Bad to 14-3-3. These results suggest that phosphorylated Bad promotes cell growth and in oncogenic transformation may contribute to the neoplastic phenotype of the cell.

subject areas

  • 14-3-3 Proteins
  • Animals
  • Apoptosis
  • Binding Sites
  • Blotting, Western
  • Carrier Proteins
  • Cell Division
  • Chick Embryo
  • Culture Media, Serum-Free
  • Cytosol
  • Fibroblasts
  • In Situ Nick-End Labeling
  • Mitochondria
  • Phenotype
  • Phosphatidylinositol 3-Kinases
  • Phosphorylation
  • Plasmids
  • Precipitin Tests
  • Protein Binding
  • Proto-Oncogene Proteins c-raf
  • Retroviridae
  • Time Factors
  • Transfection
  • Tyrosine 3-Monooxygenase
  • bcl-Associated Death Protein
scroll to property group menus

Research

keywords

  • 14-3-3
  • BH3 proteins
  • anchorage-independent growth
  • apoptosis
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0950-9232

Digital Object Identifier (DOI)

  • 10.1038/sj.onc.1204662

PubMed ID

  • 11526496
scroll to property group menus

Additional Document Info

start page

  • 5087

end page

  • 5092

volume

  • 20

issue

  • 37

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

  • About
  • Contact Us
  • Support