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The MEK2-binding tumor suppressor hDlg is recruited by E-cadherin to the midbody ring

Suzanne Gaudet1, Marie-Josée Langlois, Robert A Lue

  • 1Department of Cancer Biology and Center for Cancer Systems Biology, Dana-Farber Cancer Institute, 450 Brookline Avenue, Boston, MA 02215, USA.

BMC Cell Biology
|December 22, 2011
PubMed

Insights

The human discs-large tumor suppressor protein (hDlg) interacts with MEK2 at the midbody during cell division. This interaction, crucial for cell signaling, involves phosphorylated MEK2 and E-cadherin, forming protein complexes.

Area of Science:

  • Cell biology
  • Molecular signaling
  • Cytoskeletal dynamics

Background:

  • The human discs-large tumor suppressor protein (hDlg) is a multi-domain protein found at intercellular junctions.
  • hDlg recruits signaling proteins into macromolecular complexes at synaptic and epithelial cell-cell junctions.
  • hDlg's function at the midbody during cytokinesis remains unclear.

Purpose of the Study:

  • To investigate the role of hDlg at the midbody during cytokinesis.
  • To identify proteins interacting with hDlg at the midbody.
  • To elucidate the mechanism of hDlg recruitment to the midbody.

Main Methods:

  • Co-immunoprecipitation to detect protein interactions.
  • Immunofluorescence microscopy to visualize protein localization.
  • Analysis of protein interactions and localization in the presence/absence of specific proteins.

Main Results:

  • hDlg interacts with the activated form of MEK2 (mitogen-activated protein kinase kinase 2) at the midbody ring.
  • The interaction between hDlg and MEK2 is dependent on MEK2 phosphorylation.
  • E-cadherin localizes to the midbody and is required for isoform-specific recruitment of hDlg.

Conclusions:

  • hDlg forms a macromolecular complex with structural and signaling proteins at the midbody.
  • This complex at the midbody may play a role in cell division regulation.
  • hDlg's function at the midbody is analogous to its role at other cell-cell junction sites.
Abstract

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