• Biomolecules & Therapeutics
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• v.29 no.2
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• pp.195-204
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• 2021

Cereblon (CRBN), a substrate receptor of cullin 4-RING E3 ligase (CRL4) regulates the ubiquitination and degradation of c-Jun, mediating the lipopolysaccharide-induced cellular response. However, the upstream signaling pathway that regulates this process is unknown. In this study, we describe how endoplasmic reticulum (ER) stress reversely regulates sequestosome-1 (p62)and c-Jun protein levels. Furthermore, our study reveals that expression of p62 attenuates c-Jun protein levels through the ubiquitinproteasome system. Conversely, siRNA knockdown of p62 elevates c-Jun protein levels. Immunoprecipitation and immunoblotting experiments demonstrate that p62 interacts with c-Jun and CRBN to form a ternary protein complex. Moreover, we find that CRBN knockdown completely abolishes the inhibitory effect of p62 on c-Jun. Using brefeldin A as an inducer of ER stress, we demonstrate that the p62/c-Jun axis participates in the regulation of ER stress-induced apoptosis, and that CRBN is required for this regulation. In summary, we have identified an upstream signaling pathway, which regulates p62-mediated c-Jun degradation. Our findings elucidate the underlying molecular mechanism by which p62/c-Jun axis regulates the ER stress-induced apoptosis, and provide a new molecular connection between ER stress and apoptosis.

• Corrosion Science and Technology
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• v.23 no.4
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• pp.283-288
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• 2024

Hot-dip Zn-Mg-Al coatings have a complex microstructure consisting of Zn, Al, and MgZn₂ phases. Its crystal structure depends on alloy content and cooling rates. Microstructure and corrosion resistance of these coatings might be affected by heat treatment. To investigate effect of heat treatment on microstructure and corrosion resistance of Zn-Mg-Al coatings, Zn-1.5%Mg-1.5%Al coated steel was heated up to 550 ℃ at a heating rate of 80 ℃/s and cooled down to room temperature. At above 500 ℃, the ternary phase of Zn-MgZn₂-Al was melted down. Only Zn and MgZn₂ phases remained in the coating. Heat- and non-heat-treated specimens showed similar corrosion resistance in Salt Spray Test (SST). When a Zn-3.0%Mg-2.5%Al coated steel was subjected to heat treatment at 100 ℃ or 300 ℃ for 200 h and compared with GA and GI coated steels, the microstructure of coatings was not significantly changed at 100 ℃. However, at 300 ℃, most Al in the coating reacted with Fe in the substrate, forming a Fe-Al compound layer in the lower part of the coating. MgZn₂ was preferentially formed in the upper part of the coating. As a result of SST, Zn-Mg-Al coated steels showed excellent corrosion resistance, better than GA and GI.

• Journal of Life Science
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• v.29 no.9
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• pp.949-954
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• 2019

Membrane topology is a key characteristic of membrane proteins. We previously reported the cloning of the chromosome 4 open-reading frame 32 (C4orf32) gene as a potential membrane protein; however, the cellular localization and membrane topology of C4orf32 was as yet unknown. In this study, we found that green fluorescent protein (GFP) fused to the C-terminus of C4orf32 (C4orf32-GFP) was localized to the endoplasmic reticulum (ER). We applied three tools to identify determinants of C4orf32 topology: protease protection, fluorescence protease protection (FPP), and an inducible system using the ternary complex between FK506 binding protein 12 (FKBP), rapamycin, and the rapamycin-binding domain of mTOR (FRB) (the FRB-rapamycin-FKBP system). Using protease protection and FPP assays, we found that the GFP tag in C4orf32-GFP was localized to the cytoplasmic surface of the ER membrane of HeLa cells. Protease protection and FPP assays are useful and complimentary tools for identifying the topology of GFP fusion membrane proteins. The FRB-rapamycin-FKBP system was also used to study the topology of C4orf32. In the absence of rapamycin, a monomeric red fluorescent protein-FKBP fusion (mRFP-FKBP) and C4orf32-GFP-FRB were localized to the cytoplasm and the ER membrane, respectively. However, in the presence of rapamycin, the mRFP-FKBP was shifted from the cytoplasm to the ER and colocalized with the C4orf32-GFP-FRB. These results indicate that the FRB moiety is facing the cytoplasmic surface of ER membrane. Overall, our results clearly suggest that C4orf32 belongs to the family of type I ER resident membrane proteins.

• Journal of the Institute of Electronics Engineers of Korea SD
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• v.40 no.5
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• pp.345-353
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• 2003

When designing network processors or implementing network equipments such as routers are implemented, IP lookup operations cause the major impact on their performance. As the organization of the IP address becomes simpler, the speed of the IP lookup operations can go faster. However, since the efficient management of IP address is inevitable due to the increasing number of network users, the address organization should become more complex. Therefore, for both IPv4(IP version 4) and IPv6(IP version 6), it is the essential fact that IP lookup operations are difficult and tedious. Lots of researcher for improving the performance of IP lookups have been presented, but the good solution has not been came out. Software approach alleviates the memory usage, but at the same time it si slow in terms of searching speed when performing an IP lookup. Hardware approach, on the other hand, is fast, however, it has disadvantages of producing hardware overheads and high memory usage. In this paper, conventional researches on IP lookups are shown and their advantages and disadvantages are explained. In addition, by mixing two representative structures, a new hybrid parallel architecture for fast IP lookups is proposed. The performance evaluation result shows that the proposed architecture provides better performance and lesser memory usage.

• Analytical Science and Technology
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• v.17 no.1
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• pp.1-7
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• 2004

The synergistic solvent extraction of Mn(II) by N-nitroso-N-phenylhydroxylamineammonium salt (cupferron) and tetrabutylammonium ion ($TBA^+$) has been studied. In the presence of $TBA^+$, over 95% Mn(II) was extracted from an aqueous solution into chloroform by the cupferron in the pH range of 4 to 10. But a part of Mn(II) was extracted with only cupferron. The ternary complex of Mn(II) was more efficiently extracted into $CH_2Cl_2$ and $CHCl_3$ than other nonpolar solvents. The extracted Mn(II) was determined in the back-extracted $HNO_3$ solution by GF-AAS. This fixed procedure was applied to the determination of trace Mn(II) in tap water samples of pH 5.0. The detection limit equivalent to 3 times standard deviation of the background absorption was 0.37 ng/mL and Mn(II) was determined with the range of 0.4 to 1.01 ng/mL in our laboratory's tap water. And the recovery was 94 to 107% in samples in which 2.0 ng/mL Mn(II) was spiked. The interferences of common concomitant elements such as Cu(II), Ca(II), Fe(III) and so on were not shown up to $10{\sim}20{\mu}g/mL$. From these results, this procedure could be concluded to be applied for the determination of trace Mn(II) in other environmental water samples.

• Journal of Life Science
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• v.25 no.1
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• pp.101-112
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• 2015

A type of cell junction that is formed between different parts within the same cell is called autotypic cell junction. Autotypic junction proteins form tight junctions found between membrane lamellae of a cell, especially in myelinating glial cells. Some of them have postsynaptic density-95/disks large/zonula occludens-1 (PDZ) domains, which interact with the carboxyl (C)-terminal PDZ-binding motif of other proteins. PDZ domains are protein-protein interaction modules that play a role in protein complex assembly. The PDZ domain, which is widespread in bacteria, plants, yeast, metazoans, and Drosophila, allows the assembly of large multi-protein complexes. The multi-protein complexes act in intracellular signal transduction, protein targeting, and membrane polarization. The identified PDZ domain-containing proteins located at autotypic junctions include zonula occludens-1 (ZO-1), ZO-2, pals-1-associated tight junction protein (PATJ), multi-PDZ domain proteins (MUPPs), membrane-associated guanylate kinase inverted 2 (MAGI2), and protease-activated receptor (PAR)-3. PAR-3 interacts with atypical protein kinase C and PAR-6, forming a ternary complex, which plays an important role in the regulation of cell polarity. MAGI2 interacts with ${\alpha}$-amino-3-hydroxyl-5-methyl-4-isoxazole propionate (AMPA) receptor at excitatory synapses. PATJ is detected in paranodal loops associated with claudin-1. On the other hand, MUPP1 is found in mesaxons and Schmidt-Lanterman incisures with claudin-5. ZO-1, ZO-2, and PAR-3 are found at all three sites. Different distributions of PDZ domain-containing proteins affect the development of autotypic junctions. In this review, we will describe PDZ domain-containing proteins at autotypic tight junctions in myelinating Schwann cells and their roles.