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

BMC Cell Biology

Research Article

Nathalie Rivard¹  Marie-Josée Langlois¹  Suzanne Gaudet²  Robert A Lue³  Alain Viel³ 

[1] Department of Anatomy and Cell Biology, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 12th North avenue, Sherbrooke, Canada;Department of Cancer Biology and Center for Cancer Systems Biology, Dana-Farber Cancer Institute, 450 Brookline Avenue, 02215, Boston, MA, USA;Department of Genetics, Harvard Medical School, 02115, Boston, MA, USA;Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, 02138, Cambridge, MA, USA;

关键词: Insect Cell;    Recombinant Baculoviruses;    Cytoplasmic Bridge;    Central Spindle;    Late Anaphase;   

DOI  :  10.1186/1471-2121-12-55

 received in 2011-09-07, accepted in 2011-12-20,  发布年份 2011

来源: Springer

【 摘 要 】

BackgroundThe human homologue of the Drosophila Discs-large tumor suppressor protein, hDlg, is a multi-domain cytoplasmic protein that localizes to the membrane at intercellular junction sites. At both synaptic junctions and epithelia cell-cell junctions, hDlg is known to recruit several signaling proteins into macromolecular complexes. hDlg is also found at the midbody, a small microtubule-rich structure bridging the two daughter cells during cytokinesis, but its function at this site is not clear.ResultsHere we describe the interaction of hDlg with the activated form of MEK2 of the canonical RAF/MEK/ERK pathway, a protein that is found at the midbody during cytokinesis. We show that both proteins localize to a sub-structure of the midbody, the midbody ring, and that the interaction between the PDZ domains of hDlg and the C-terminal portion of MEK2 is dependent on the phosphorylation of MEK2. Finally, we found that E-cadherin also localizes to the midbody and that its expression is required for the isoform-specific recruitment of hDlg, but not activated MEK2, to that structure.ConclusionOur results suggest that like at other cell-cell junction sites, hDlg is part of a macromolecular complex of structural and signaling proteins at the midbody.

【 授权许可】

Unknown   
© Gaudet et al; licensee BioMed Central Ltd. 2011. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.