Compartmentalization of the mitogen-activated protein kinase (MAPK) in hepatic endosomes: association with the internalized epidermal growth factor (EGF) receptor

Mol Cell Biol Res Commun. 1999 May;1(2):132-9. doi: 10.1006/mcbr.1999.0120.

Abstract

A pool of MAPK was found in hepatic plasma membrane (PM) and endosomes (ENs). After injection of a single dose of EGF (10 microg/100 g body weight), MAPK was detected in EGF receptor (EGFR) immunoprecipitates prepared from ENs. MAPK was detected in a time-dependent manner in EGFR immunoprecipitates that was coincident with the progressive concentration of the EGFR. The EGFR-associated MAPK was also detected by using an anti-phospho-MAPK suggesting that it was active. MAPK was present in wheat-germ agglutinin (WGA) eluates prepared from ENs and was maximally tyrosine-phosphorylated at the time peak of EGFR internalization. MAPK therefore is compartmentalized in PM and ENs of rat liver. A fraction of the endosomal MAPK was found to be associated with the internalized EGFR complexes, suggesting that it plays a role in the control of the EGFR activity at this locus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Compartmentation
  • Cell Membrane / metabolism
  • Endosomes / enzymology
  • Endosomes / metabolism*
  • ErbB Receptors / metabolism*
  • Female
  • Immunoblotting
  • Liver / enzymology
  • Liver / metabolism*
  • Liver / ultrastructure
  • Mitogen-Activated Protein Kinases / metabolism*
  • Phosphorylation
  • Precipitin Tests
  • Rats
  • Rats, Sprague-Dawley
  • Tyrosine / metabolism
  • Wheat Germ Agglutinins

Substances

  • Wheat Germ Agglutinins
  • Tyrosine
  • ErbB Receptors
  • Mitogen-Activated Protein Kinases