Alternative titles; symbols
HGNC Approved Gene Symbol: TRIP6
Cytogenetic location: 7q22.1 Genomic coordinates (GRCh38): 7:100,867,387-100,873,454 (from NCBI)
Thyroid hormone receptors (TRs) are hormone-dependent transcription factors that regulate expression of a variety of specific target genes. Lee et al. (1995) used a modified yeast 2-hybrid screen to identify proteins that interact with the ligand-binding domain of rat Tr-beta-1 (THRB; 190160). They recovered HeLa cell cDNAs encoding a number of different TR-interacting proteins, or TRIPs. One of the proteins, TRIP6, contains 2 LIM domains (see 601329) and is similar to zyxin (602002). Northern blot analysis detected a 1.8-kb TRIP6 mRNA in several tissues, with highest expression in kidney, liver, and lung.
Yi and Beckerle (1998) stated that the cDNA recovered by Lee et al. (1995) was incomplete. They reported that the predicted full-length protein contains 476 amino acids and has 3 tandemly arrayed C-terminal LIM domains and a proline-rich N-terminal region. The amino acid sequence of TRIP6 displays 35% and 50% identity to those of zyxin and LPP (600700), respectively.
Lee et al. (1995) found that TRIP6 interacted with TR-beta only in the presence of thyroid hormone.
Neisseria gonorrhoeae opacity-associated (Opa) proteins are a family of outer membrane proteins involved in gonococcal adherence to and invasion of human cells. In a yeast 2-hybrid screen to identify human epithelial cell proteins that interact with Opa proteins, Williams et al. (1998) isolated HeLa cell cDNAs encoding TRIP6, or OIP1 (Opa-interacting protein-1).
Salmonella typhimurium-infected phagocytes traverse the gastrointestinal epithelium and enter the bloodstream within minutes after ingestion, thereby spreading throughout the host. By yeast 2-hybrid analysis, Worley et al. (2006) found that S. typhimurium srfH, a secreted type III effector, interacted with the LIM domain of human TRIP6. Deconvolution microscopy demonstrated diffuse cytoplasmic colocalization of srfH and Trip6 in murine macrophages. Bacteria lacking SrfH were unable to stimulate TRIP6-dependent phagocyte migration in vitro or in vivo. Mice lacking Cd18 (ITGB2; 600065) and infected with Salmonella did not show phagocyte migration, in spite of diminished bactericidal function. Worley et al. (2006) concluded that TRIP6 functions in both inflammatory and cell motility pathways.
By analysis of a radiation hybrid panel, Yi and Beckerle (1998) mapped the TRIP6 gene to 7q22.
Lee, J. W., Choi, H.-S., Gyuris, J., Brent, R., Moore, D. D. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Molec. Endocr. 9: 243-254, 1995. [PubMed: 7776974] [Full Text: https://doi.org/10.1210/mend.9.2.7776974]
Williams, J. M., Chen, G.-C., Zhu, L., Rest, R. F. Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Molec. Microbiol. 27: 171-186, 1998. [PubMed: 9466265] [Full Text: https://doi.org/10.1046/j.1365-2958.1998.00670.x]
Worley, M. J., Nieman, G. S., Geddes, K., Heffron, F. Salmonella typhimurium disseminates within its host by manipulating the motility of infected cells. Proc. Nat. Acad. Sci. 103: 17915-17920, 2006. [PubMed: 17095609] [Full Text: https://doi.org/10.1073/pnas.0604054103]
Yi, J., Beckerle, M. C. The human TRIP6 gene encodes a LIM domain protein and maps to chromosome 7q22, a region associated with tumorigenesis. Genomics 49: 314-316, 1998. [PubMed: 9598321] [Full Text: https://doi.org/10.1006/geno.1998.5248]