Disease relevance of TARP

• TARP: a nuclear protein expressed in prostate and breast cancer cells derived from an alternate reading frame of the T cell receptor gamma chain locus [1].
• These results suggest that TARP has a role in regulating growth and gene expression in prostate cancer cells [2].
• A novel TARP-promoter-based adenovirus against hormone-dependent and hormone-refractory prostate cancer [3].
• Tarp and Arp: How Chlamydia induces its own entry [4].
• The chlamydial protein (Tarp) appears to be translocated into the host cell by type III secretion because it is exported in a Yersinia heterologous expression assay [5].

High impact information on TARP

• Domain analysis of TARP identified an actin-binding domain that bears structural and primary amino acid sequence similarity to WH2 domain family proteins [6].
• In addition, a proline-rich domain was found to promote TARP oligomerization and was required for TARP-dependent nucleation of new actin filaments [6].
• We have named this protein TCRgamma alternate reading frame protein (TARP) [1].
• The TARP-binding sites in the ckm enhancer and the ckb promoter were found to be functionally interchangeable [7].
• We have previously reported that the rat brain creatine kinase (ckb) gene promoter contains an AT-rich sequence that is a binding site for a protein called TARP (TA-rich recognition protein) [7].

Chemical compound and disease context of TARP

• TARP is expressed in the androgen-sensitive LNCaP prostate cancer cell line but not in the androgen-independent PC3 prostate cancer cell line, indicating that TARP may play a role in prostate cancer progression [2].
• Recently, a Chlamydia trachomatis type III secreted effector protein, Tarp, was found to be translocated and tyrosine phosphorylated at the site of entry and associated with the recruitment of actin that coincides with endocytosis [8].

Biological context of TARP

• We also transfected a plasmid encoding TARP fused to green fluorescent protein into LNCaP, MDA-Pca-2b, and PC-3 cells and confirmed its specific mitochondrial localization in living cells [9].
• We further demonstrate that the promoter specifically initiates reporter gene expression in TARP-positive prostate cancer cell lines [10].
• Here we demonstrate that TARP expression is regulated by testosterone at the transcriptional level through specific binding of androgen receptor to an androgen response element in the proximal TARP promoter [10].
• We propose that TARP is active in both muscle and nonmuscle cells and that it is one of many potential activators that may interact with muscle-specific regulators to determine the myogenic phenotype [7].
• We propose that binding of TARP to the upstream consensus TATA box may block formation of the upstream initiating complex [11].

Anatomical context of TARP

• To elucidate the function of TARP, we generated a stable PC3 cell line that expresses TARP in a constitutive manner [2].
• Fractionation of mitochondria shows that TARP is located in the outer mitochondrial membrane [9].
• TARP (T cell receptor gamma-chain alternate reading frame protein) is uniquely expressed in males in prostate epithelial cells and prostate cancer cells [10].
• TARP was found in both muscle cells (C2 and L6 myotubes) and nonmuscle (HeLa) cells and appeared to be indistinguishable from both sources, as judged by gel retardation and footprinting assays [7].
• We have shown previously that brain and HeLa cell nuclear extracts contain an abundant factor, TARP, which binds to the upstream consensus TATA box and have proposed that this factor is distinct from the classical TATA box binding factor TFIID [11].

Associations of TARP with chemical compounds

• We also demonstrated that TARP expression is up-regulated by testosterone in LNCaP cells that express a functional androgen receptor [2].
• These data demonstrate that TARP is the first prostate-specific protein localizing in mitochondria and indicate that TARP, an androgen-regulated protein, may act on mitochondria to carry out its biological functions [9].
• Neuronal AMPA receptors comprise pore forming glutamate receptor (GluR) proteins and auxiliary transmembrane AMPA receptor regulatory (TARP) subunits [12].
• Tyrosine phosphorylation of the chlamydial effector protein Tarp is species specific and not required for recruitment of actin [8].
• Combined application of a thiourea RSB and plastic tarps had a synergetic effect in emission control and could eliminate the relatively high fumigant flux that occurs upon tarp disruption [13].

Other interactions of TARP

• To develop a regulatory sequence for prostate-specific gene expression, we constructed a chimeric sequence consisting of the TARP promoter and the prostate-specific antigen (PSA) enhancer [10].
• The aim of the present study was to use immunohistochemistry and semi-quantitative histomorphometric analysis to compare the distribution and relative abundance of AQP1 on NCI TARP human multiple tumor tissue microarrays (TMAs) with normal tissues represented on the CHTN TMAs [14].
• Here, we employ site-directed mutagenesis to determine functional interactions between GluR1 and the prototypical TARP, stargazin [12].

Analytical, diagnostic and therapeutic context of TARP

• We used TP1 to determine the subcellular localization of TARP by Western blotting following subcellular fractionation and immunocytochemistry [9].
• We have done experiments aimed at identifying helper T lymphocyte (HTL) epitopes for TARP for the design of T cell-based immunotherapy for prostate cancer [15].
• Here, we present a three-dimensional (3D) density map of the hetero-tetrameric AMPA-R without associated stargazin/TARP proteins as determined by cryo-negative stain single-particle electron microscopy [16].
• Weather information, field size, application date, application rate, application type, soil incorporation depth, pesticide degradation rates in air, tarp presence, field retreatment, and other sensitive parameters are varied stochastically using Monte Carlo techniques to mimic region and crop specific agronomic practices [17].

References