Heregulin β1 induces the down regulation and the ubiquitin-proteasome degradation pathway of p185(HER2) oncoprotein

A. Magnifico, E. Tagliabue, E. Ardini, P. Casalini, M. I. Colnaghi, S. Ménard

Research output: Contribution to journalArticlepeer-review

Abstract

Analysis of the fate of the p185(HER2) oncoprotein following activation by heregulin β1 revealed the induction of the tyrosine-phosphorylation, down-modulation, and polyubiquitination of p185(HER2). Receptor ubiquitination was suppressed in cells treated with heregulin β1 in the presence of sodium azide, an inhibitor of ATP-dependent reactions, or genistein, a tyrosine kinase protein inhibitor, indicating the requirement for kinase activity and ATP in p185(HER2) polyubiquitination. Ubiquitinated p185(HER2) was degradated by the 26S proteasome proteolytic pathway. Kinetics and inhibition experiments indicated that endocytosis of the receptor occurs downstream of the initiation of the degradation process.

Original languageEnglish
Pages (from-to)129-131
Number of pages3
JournalFEBS Letters
Volume422
Issue number2
DOIs
Publication statusPublished - Jan 30 1998

Keywords

  • Down-modulation
  • p185(HER2) oncoprotein
  • Proteasome enzyme
  • Ubiquitination

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint

Dive into the research topics of 'Heregulin β1 induces the down regulation and the ubiquitin-proteasome degradation pathway of p185(HER2) oncoprotein'. Together they form a unique fingerprint.

Cite this