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Title: NAC1 is an actin-binding protein that is essential for effective cytokinesis in cancer cells
Authors: Kai Lee Yap
Stephanie I. Fraley
Michelle M. Thiaville
Natini Jinawath
Kentaro Nakayama
Jianlong Wang
Tian Li Wang
Denis Wirtz
Ie Ming Shih
Johns Hopkins University
Johns Hopkins Medical Institutions
Shimane University
The Mount Sinai Medical Center
Louisiana State University
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology;Medicine
Issue Date: 15-Aug-2012
Citation: Cancer Research. Vol.72, No.16 (2012), 4085-4096
Abstract: NAC1 is a transcriptional corepressor protein that is essential to sustain cancer cell proliferation and migration. However, the underlying molecular mechanisms of NAC1 function in cancer cells remain unknown. In this study, we show that NAC1 functions as an actin monomer-binding protein. The conserved BTB protein interaction domain in NAC1 is the minimal region for actin binding. Disrupting NAC1 complex function by dominant-negative or siRNA strategies reduced cell retraction and abscission during late-stage cytokinesis, causing multinucleation in cancer cells. In Nac1-deficient murine fibroblasts, restoring NAC1 expression was sufficient to partially avert multinucleation. We found that siRNA-mediated silencing of the actin-binding protein profilin-1 in cancer cells caused a similar multinucleation phenotype and that NAC1 modulated the binding of actin to profillin-1. Taken together, our results indicate that the NAC1/actin/profilin-1 complex is crucial for cancer cell cytokinesis, with a variety of important biologic and clinical implications. ©2012 AACR.
ISSN: 15387445
Appears in Collections:Scopus 2011-2015

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