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Stability and function of mammalian lethal giant larvae-1 oncoprotein are regulated by the scaffolding protein RanBPM

Bharathi Suresh1, Suresh Ramakrishna, Yong-Soo Kim

  • 1Department of Biomedical Science, CHA University, CHA General Hospital, Seoul 135-081, Korea.

The Journal of Biological Chemistry
|September 11, 2010
PubMed

Insights

Ran-binding protein M (RanBPM) stabilizes the Mgl-1 protein, a mammalian homolog of the lethal giant larvae (Lgl) tumor suppressor. This interaction enhances Mgl-1

Area of Science:

  • Molecular biology
  • Cell biology
  • Cancer research

Background:

  • The lethal giant larvae (Lgl) tumor suppressor is crucial for cell polarity and tissue organization.
  • The exact molecular mechanisms of Lgl function are not fully understood.

Purpose of the Study:

  • To identify novel binding partners of Mgl-1, the mammalian Lgl homolog.
  • To elucidate the role of Ran-binding protein M (RanBPM) in regulating Mgl-1 function.

Main Methods:

  • Yeast two-hybrid screening to identify Mgl-1 interacting proteins.
  • Co-immunoprecipitation and GST pull-down assays to confirm protein association.
  • Cell migration and colony formation assays to assess Mgl-1 activity.

Main Results:

  • Ran-binding protein M (RanBPM) was identified as a novel binding partner of Mgl-1.
  • RanBPM acts as a scaffolding protein, enhancing Mgl-1 stability by inhibiting its degradation.
  • RanBPM significantly boosted Mgl-1's activity in cell migration and colony formation.

Conclusions:

  • RanBPM plays a novel role in modulating Mgl-1 stability and function.
  • RanBPM contributes to the tumor-suppressive activity of Mgl-1.

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