The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases.

Article Details

Citation

Gangisetty O, Lauffart B, Sondarva GV, Chelsea DM, Still IH

The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases.

Oncogene. 2004 Apr 1;23(14):2559-63.

PubMed ID
14767476 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Histone acetyltransferase KAT2BQ92831Details
Histone acetyltransferase KAT2AQ92830Details