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The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases

Abstract

Dysregulation of the human transforming acidic coiled coil (TACC) genes is thought to be important in the development of multiple myeloma, breast and gastric cancer. However, even though these proteins have been implicated in the control of cell growth and differentiation, the mechanism by which they function still remains to be clarified. Using the yeast two-hybrid assay, we have now identified the histone acetyltransferase (HAT) hGCN5L2 as a TACC2-binding protein. GST pull-down analysis subsequently confirmed that all human TACC family members can bind in vitro to hGCN5L2. The authenticity of these interactions was validated by coimmunoprecipitation assays within the human embryonic kidney cell line HEK293, which identified the TACC2s isoform as a component consistently bound to several different members of HAT family. This raises the possibility that aberrant expression of one or more TACC proteins may affect gene regulation through their interaction with components of chromatin remodeling complexes, thus contributing to tumorigenesis.

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Acknowledgements

We thank Dr Jennifer Black, Director of the Roswell Park Cell Analysis Core Facility, and Dr Sei-ichi Matsui for their assistance and input in the preparation of this manuscript. This work was supported in part by US Army Medical Research Grant DAMD17-01-1-0208, developmental funds support from the Roswell Park Cancer Institute and Core grant CA16056 from the National Cancer Institute. The latter maintains the Biopolymer and Tissue Culture media core facilities at the Roswell Park Cancer Institute.

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Correspondence to Ivan H Still.

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Gangisetty, O., Lauffart, B., Sondarva, G. et al. The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases. Oncogene 23, 2559–2563 (2004). https://doi.org/10.1038/sj.onc.1207424

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