Interaction of TACC proteins with the FHL family: implications for ERK signaling.

The Transforming acidic coiled coil (TACC) proteins play a conserved role in normal development and tumorigenesis through interactions with multiple complexes involved in transcription, translation, and centrosomal dynamics. However, despite significant work on the function of TACC3 in the control of centrosomal mechanics, relatively little functional data is known about the family's founding member, TACC1. From a continued analysis of clones isolated by an unbiased yeast two-hybrid assay, we now show direct physical interactions between the TACC1 and the FHL (Four and a Half LIM-only) family of proteins.

Temporal and spatial expression of TACC1 in the mouse and human.

TACC1 is the founding member of the evolutionarily conserved transforming acidic coiled coil genes. These genes play a role in normal development and tumorigenesis through interactions with multiple complexes involved in transcription, translation, and centrosomal dynamics. Despite its importance, detailed examination of the expression of TACC1 and splice variants has not previously been performed.

Aberrations of TACC1 and TACC3 are associated with ovarian cancer.

Background: Dysregulation of the human Transforming Acidic Coiled Coil (TACC) genes is thought to be important in the development and progression of multiple myeloma, breast and gastric cancer. Recent, large-scale genomic analysis and Serial Analysis of Gene Expression data suggest that TACC1 and TACC3 may also be involved in the etiology of ovarian tumors from both familial and sporadic cases. Therefore, the aim of this study was to determine the occurrence of alterations of these TACCs in ovarian cancer.

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

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.

Molecular cloning, genomic structure and interactions of the putative breast tumor suppressor TACC2.

The human transforming acidic coiled-coil 2 (TACC2) gene has been suggested recently to be a putative breast tumor suppressor. Now we can report the cloning of full length TACC2 cDNAs corresponding to the major isoforms expressed during development. The TACC2 gene is encoded by 23 exons, and spans 255 kb of chromosome 10q26.

Interaction of the transforming acidic coiled-coil 1 (TACC1) protein with ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein complexes in human cells.

Dysregulation of the human transforming acidic coiled-coil (TACC) proteins is thought to be important in the evolution of breast cancer and multiple myeloma. However, the exact role of these proteins in the oncogenic process is currently unknown. Using the full-length TACC1 protein as bait to screen a human mammary epithelial cDNA library, we have identified two genes that are also amplified and overexpressed in tumours derived from different cellular origins.