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Published on: September 17, 2012

Cell cycle-dependent association of Gag-Mil and hsp90

J Lovrić1, O Bischof, K Moelling

  • 1Max-Planck-Institut für Molekulare Genetik, Abt. Schuster, Berlin (Dahlem), Germany.

FEBS Letters
|April 18, 1994
PubMed

Insights

Quail Gag-Mil protein kinase forms a complex with heat shock protein 90 (hsp90). During mitosis, Gag-Mil shifts to a form (p102Gag-Mil) that dissociates from hsp90.

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Protein Kinase Research

Background:

  • The Gag-Mil protein kinase is crucial in cellular processes.
  • Understanding protein interactions is key to deciphering kinase function.

Purpose of the Study:

  • To identify proteins associated with Gag-Mil kinase.
  • To investigate the interaction between Gag-Mil and its binding partners during mitosis.

Main Methods:

  • Immunoprecipitation of p100Gag-Mil from MH2-transformed quail embryo fibroblasts.
  • Electrophoretic analysis to detect protein mobility shifts.
  • Microsequencing to identify associated proteins.

Main Results:

  • p100Gag-Mil was found to be associated with an 89 kDa protein.
  • The 89 kDa protein was identified as the quail homologue of heat shock protein 90 (hsp90).
  • A high molar ratio (0.72) indicated significant Gag-Mil-hsp90 complex formation.
  • During mitosis, Gag-Mil shifts to p102Gag-Mil, which shows reduced association with hsp90.

Conclusions:

  • p100Gag-Mil forms a stoichiometric complex with hsp90.
  • Mitotic phosphorylation of Gag-Mil leads to its release from the hsp90 complex.

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