• Biomedical Science Letters
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• v.9 no.2
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• pp.105-110
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• 2003

Ankyrins are a ubiquitously expressed family of intracellular adaptor proteins involved in targeting diverse proteins to specialized membrane domains in both the plasma membrane and the endoplasmic reticulum. Canonical ankyrins are 190-220 kDa proteins expressed in most tissues and cell types and comprise a membrane-binding domain (MBD) of 24 ANK repeats, a spectrin-binding domain, a death domain and a C-terminal domain. Rescue studies with ankyrin-B/G chimeras have identified the C-terminal domain of ankyrin-B as the defining domain in specifying ankyrin-B activity, but the function of C-terminal domain of ankyrin-B is, however, not known. We report here that the C-terminal domain of ankyrin-B is capable of interacting with the C-terminal Region of Hsp40. The Hsps are induced not only by heat shock but also by various other environmental stresses. Hsps are also expressed constitutively at normal growth temperatures and have basic and indispensable functions in the life cycle of proteins as molecular chaperones, as well as playing a role in protecting cells from the deleterious stresses. The binding sites required in the interaction between C-terminal domain of ankyrin-B and C-terminal region of Hsp40 were characterized using the yeast two-hybrid system and GST-pull down assay. The interaction between ankyrin-B and Hsp40 represents the first direct evidence of ankyrin's role as chaperones.

• Biomedical Science Letters
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• v.12 no.4
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• pp.303-310
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• 2006

Ankyrins are a ubiquitously expressed family of intracellular adaptor proteins involved in targeting diverse proteins to specialized membrane domains in both the plasma membrane and the endoplasmic reticulum. We described here that the C-terminal domain of ankyrin-B interact specifically with Z-line portion of titin in yeast two-hybrid analysis, in vitro pull-down assays and localization experiments in COS-7 cells. In this study we provide the first experimental evidence that Z-line portion of titin is necessary for the localization of ankyrin-B and ankyrin-B links between the sarcolemma and the myofibril in costameres.

• Biomedical Science Letters
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• v.9 no.3
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• pp.159-165
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• 2003

Ankyrins are a ubiquitously expressed family of intracellular adaptor proteins involved in targeting diverse proteins to specialized membrane domains in both the plasma membrane and the endoplasmic reticulum. Recently, the studies with C-terminus of ankyrins have identified that ankyrin-B is capable of interacting with Hsp40 and sAnkl is capable of interacting with obscurin and titin, but the function of C-terminal domain of ankyrin-G remains unknown. To identify proteins interacting C-terminus of ankyrin-G, we used the C-terminus of ankyrin-G as a bait for a yeast two-hybrid screen of brain cDNA library. Approximately 1.33$\times$l0$^6$ transformants were screened, of which 13 positive clones were obtained as determined by activation of HIS3, ADE2 and MELl reporter genes. Sequence analyses of these 13 plasmids revealed that cDNA inserts of 13 colonies showed highly homologous to 11 genes, including 5 known (i.e., Na$^+$/K$^+$ ATPase $\beta$1, SERBPl, UTF2, cytochrome C oxidase and collagen IV $\alpha$2) and 6 unknown genes. The evaluation of the proteins that emerge from these experiments provides a rational approach to investigate the those proteins significant in interaction with ankyrin-G.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2003.06a
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• pp.201-201
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• 2003

• Genomics & Informatics
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• v.21 no.2
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• pp.22.1-22.15
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• 2023

Kidney renal clear cell carcinoma (KIRC) is one of the most aggressive cancer type of the urinary system. Metastatic KIRC patients have poor prognosis and limited therapeutic options. Ankyrin 3 (ANK3) is a scaffold protein that plays important roles in maintaining physiological function of the kidney and its alteration is implicated in many cancers. In this study, we investigated differential expression of ANK3 in KIRC using GEPIA2, UALCAN, and HPA databases. Survival analysis was performed by GEPIA2, Kaplan-Meier plotter, and OS-kirc databases. Genetic alterations of ANK3 in KIRC were assessed using cBioPortal database. Interaction network and functional enrichment analyses of ANK3-correlated genes in KIRC were performed using GeneMANIA and Shiny GO, respectively. Finally, the TIMER2.0 database was used to assess correlation between ANK3 expression and immune infiltration in KIRC. We found that ANK3 expression was significantly decreased in KIRC compared to normal tissues. The KIRC patients with low ANK3 expression had poorer survival outcomes than those with high ANK3 expression. ANK3 mutations were found in 2.4% of KIRC patients and were frequently co-mutated with several genes with a prognostic significance. ANK3-correlated genes were significantly enriched in various biological processes, mainly involved in peroxisome proliferator-activated receptor (PPAR) signaling pathway, in which positive correlations of ANK3 with PPARA and PPARG expressions were confirmed. Expression of ANK3 in KIRC was significantly correlated with infiltration level of B cell, CD8+ T cell, macrophage, and neutrophil. These findings suggested that ANK3 could serve as a prognostic biomarker and promising therapeutic target for KIRC.

• Korean journal of applied entomology
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• v.45 no.1 s.142
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• pp.15-24
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• 2006

Inhibitor kB (IkB)-like gene has been found in the genome of Cotesia plutellae bracovirus (CpBV), which is the obligatory symbiont of an endoparsitoid wasp, C. plutellae. The open reading frame of CpBV-IkB was 417 bp and encoded 138 amino acids. Four ankyrin repeat domains were found in CpBV-IkB, which shared high homology with other known polydnavirus IkBs. Considering a presumptive cellular IkB based on Drosophila Cactus, CpBV-IkB exhibited a truncated structure with deletion of signal-receiving domains, which suggested its irreversible inhibitory role in NFkB signal transduction pathway of the parasitized host in response to the wasp parasitization. CpBV-IkB was expressed only in the parasitized diamondback moth, Plutella flostella. Its expression was estimated by quantitative RT-PCR during parasitization period, showing a constitutive expression pattern from the first day of parasitization. An indirect functional analysis of CpBV-IkB was conducted and suggested a hypothesis of host antivirus inhibition.

• Korean journal of applied entomology
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• v.52 no.1
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• pp.35-43
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• 2013

All tested Korean populations of the diamondback moth, Plutella xylostella, are known to be resistant especially against pyrethroid insecticides by mutation in its molecular target, para-sodium channel. Moreover, P. xylostella is able to develop resistance against most commercial insecticides. This study was performed to develop an efficient control technique against P. xylostella by a combined treatment of an endoparasitoid wasp, Cotesia plutellae, and a microbial insecticide, Bacillus thuringiensis. To investigate any parasitism preference of C. plutellae against susceptible and resistant P. xylostella, five different populations of P. xylostella were compared in insecticide susceptibilities and parasitism by C. plutellae. These five P. xylostella populations showed a significant variation against three commercial insecticides including pyrethroid, organophosphate, neonicotinoid, and insect growth regulator. However, there were no significant differences among five P. xylostella populations in their parasitic rates by C. plutellae. Moreover, parasitized larvae of P. xylostella showed significantly higher susceptibility to B. thuringiensis. As an immunosuppressive agent, viral ankyrin genes (vankyrins) encoded in C. plutellae were transiently expressed in nonparasitized larvae. Expression of vankyrins significantly enhanced the efficacy of B. thuringiensis against the third instar larvae of P. xylostella. Thus an immunosuppression induced by C. plutellae enhanced the insecticidal efficacy of B. thuringiensis. These results suggest that a combined treatment of C. plutellae and B. thuringiensis may effectively control the insecticide-resistant populations of P. xylostella.

• BMB Reports
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• v.49 no.12
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• pp.651-652
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• 2016

EphA2 has been implicated in amplifying ErbB2 tumorigenic signaling. One protein that interacts with EphA2 is the Anks1a PTB adaptor. However, the precise role of Anks1a in EphA2-mediated tumorigenesis is unclear. We demonstrated that Anks1a localizes to the ER upon phosphorylation and that the Ankyrin repeats and PTB of Anks1a bind to EphA2 and Sec23, respectively. Thus, Anks1a facilitates the selective packaging of EphA2 into COPII vesicles. Additionally, Anks1a knockout mice, a phenocopy of EphA2 knockout mice, exhibited markedly reduced ErbB2-induced breast tumorigenesis. Strikingly, ErbB2 did not localize to the cell surface following Anks1a knockdown in primary mammary tumor cells over-expressing ErbB2. Importantly, EphA2 was critical for stabilizing ErbB2 through complex formation, but its interaction with Anks1a also facilitated ErbB2 loading into COPII carriers. These findings suggest a novel role for Anks1a in the molecular pathogenesis of breast tumors and possibly other human diseases.

• International Journal of Industrial Entomology and Biomaterials
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• v.37 no.2
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• pp.49-54
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• 2018

To artificially enhance antimicrobial peptide expression in Bombyx mori, we constructed genetically engineered silkworms overexpressing Rel family transcription factor. The truncated BmRelish1 (BmRelish1t) gene contained a Rel homolog domain (RHD), nuclear localization signal (NLS), acidic and hydrophobic amino acid (AHAA)-rich region, and death domain (DD), but no ankyrin-repeat (ANK) domain. The BmRelish1t gene was controlled by B. mori cytoplasmic actin 3 promoter in the PiggyBac transposon vector. Chromosome analysis of G1 generations of a transgenic silkworm with EGFP expression confirmed stable insertion of BmRelish1t. BmRelish1t gene overexpression in transgenic silkworms resulted in higher mRNA expression levels of B. mori antimicrobial peptides such as lebocin(~20.5-fold), moricin(~8.7-fold), and nuecin(~17.4-fold) than those in normal silkworms.

• Molecules and Cells
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• v.43 no.6
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• pp.572-580
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• 2020

Transient receptor potential ankyrin 1 from rattlesnakes (rsTRPA1) and boas (bTRPA1) was previously proposed to underlie thermo-sensitive infrared sensing based on transcript enrichment in infrared-sensing neurons and hyper-thermosensitivity expressed in Xenopus oocytes. It is unknown how these TRPA1s show thermosensitivities that overwhelm other thermoreceptors, and why rsTRPA1 is more thermosensitive than bTRPA1. Here, we show that snake TRPA1s differentially require Ca²⁺ for hyper-thermosensitivity and that predisposition to cytosolic Ca²⁺ potentiation correlates with superior thermosensitivity. Extracellularly applied Ca²⁺ upshifted the temperature coefficients (Q10s) of both TRPA1s, for which rsTRPA1, but not bTRPA1, requires cytosolic Ca²⁺. Intracellular Ca²⁺ chelation and substitutive mutations of the conserved cytosolic Ca²⁺-binding domain lowered rsTRPA1 thermosensitivity comparable to that of bTRPA1. Thapsigargin-evoked Ca²⁺ or calmodulin little affected rsTRPA1 activity or thermosensitivity, implying the importance of precise spatiotemporal action of Ca²⁺. Remarkably, a single rattlesnake-mimicking substitution in the conserved but presumably dormant cytosolic Ca²⁺-binding domain of bTRPA1 substantially enhanced thermosensitivity through cytosolic Ca²⁺ like rsTRPA1, indicating the capability of this single site in the determination of both cytosolic Ca²⁺ dependence and thermosensitivity. Collectively, these data suggest that Ca²⁺ is essential for the hyper-thermosensitivity of these TRPA1s, and cytosolic potentiation by permeating Ca²⁺ may contribute to the natural variation of infrared senses between rattlesnakes and boas.