Disease relevance of TACC2

• Studies of human breast cancer samples and cell lines suggest a putative role of TACC2 as a tumor suppressor protein [1].

High impact information on TACC2

• Finally, in TACC2-deficient embryonic fibroblasts, proliferation and cell cycle progression as well as centrosome numbers are comparable to those in wild-type cells [1].
• Therefore, TACC2 is not required, nonredundantly, for mouse development and normal cell proliferation and is not a tumor suppressor protein [1].
• In addition, reexpression of AZU-1 in T4-2 cells, using viral vectors, was sufficient to reduce their malignant phenotype substantially, both in culture and in vivo [2].
• These results indicate that AZU-1 is a candidate breast tumor suppressor that may exert its effects by promoting correct tissue morphogenesis [2].
• The AZU-1 gene encodes an acidic 571-amino-acid protein containing at least two structurally distinct domains with potential protein-binding functions: an N-terminal serine and proline-rich domain with a predicted immunoglobulin-like fold and a C-terminal coiled-coil domain [2].

Biological context of TACC2

• The nucleotide sequence of the cDNA is nearly identical to that of transforming acidic coiled coil-containing (TACC2) and anti-zuai-1 (AZU-1) cDNA clones except at the 5'- and 3'-ends [3].
• In these centrosomal TACC2-liberated cells, chromosomes were lagging and mis-aligned [4].
• Here, we show that a centrosomal protein TACC2 is phosphorylated in mitosis by TTK signaling pathway [4].
• The TACC2 gene is encoded by 23 exons, and spans 255 kb of chromosome 10q26 [5].
• Significantly, we demonstrate that TACC2 interacts with GAS41 and the SWI/SNF chromatin remodeling complex [5].

Anatomical context of TACC2

• In addition, the distance between two centrosomes was markedly reduced, suggesting that centrosomal TACC2 is required for mitotic spindle maintenance [4].
• Cloning and structural characterization of ECTACC, a new member of the transforming acidic coiled coil (TACC) gene family: cDNA sequence and expression analysis in human microvascular endothelial cells [3].

Other interactions of TACC2

• In contrast, TACC1 and TACC2 mRNA levels are more widespread [6].
• TACC2 was pulled down by wild type TTK but not kinase death mutant, suggesting the potential phosphorylation-mediated interaction between these two proteins [4].
• Using the yeast two-hybrid assay, we have now identified the histone acetyltransferase (HAT) hGCN5L2 as a TACC2-binding protein [7].

Analytical, diagnostic and therapeutic context of TACC2

• Using real-time PCR, we quantitated the mRNA levels of TACC3 compared to TACC1 and TACC2 in various human adult tissues [6].
• Our immunofluorescence studies revealed that both TTK and TACC2 are located to the centrosome [4].
• Molecular cloning, genomic structure and interactions of the putative breast tumor suppressor TACC2 [5].

References