• Title/Summary/Keyword: AP2 domain

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CDK2AP1, a Cyclin-Dependent Kinase 2-Associated Protein, Interacts with Kinesin-1 through Kinesin Superfamily Protein 5A (KIF5A) (Cyclin-dependent kinase 1 결합 단백질 CDK2AP1은 kinesin superfamily protein 5A (KIF5A)을 매개로 Kinesin-1와 결합)

  • Myoung Hun Kim;Se Young Pyo;Young Joo Jeong;Sung Woo Park;Mi Kyoung Seo;Won Hee Lee;Sang-Hwa Urm;Mooseong Kim;Jung Goo Lee;Dae-Hyun Seog
    • Journal of Life Science
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    • v.33 no.7
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    • pp.531-537
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    • 2023
  • Intracellular and axonal transport is mediated by microtubule-dependent motor proteins, such as kinesins and cytoplasmic dynein. Kinesin moves along the microtubule to the positive end of the microtubule, while dynein moves to the negative end of the microtubule. Kinesin-1 was first identified as a kinesin superfamily protein (KIF) that functions in the intracellular transport of various cargoes, including organelles, neurotransmitter receptors, and mRNA-protein complexes, through interactions between the carboxyl (C)-terminal domain and the cargo. It interacts with other cargoes, but the adapter/scaffold proteins that mediate between kinesin-1 and the cargo have yet to be fully identified. In this study, a yeast two-hybrid screen was used to identify adapter proteins that interact with the C-terminal region of KIF5A. We found an association between the C-terminal region of KIF5A and the cyclin-dependent kinase 2-associated protein 1 (CDK2AP1), originally identified in malignant hamster oral keratinocytes. CDK2AP1 bound to the C-terminal region of KIF5A and did not interact with KIF3A (the motor of kinesin-2), KIF5B, KIF5C, and kinesin light chain 1 (KLC1). The C-terminal region of CDK2AP1 is essential for its interaction with KIF5A. When co-expressed in HEK-293T cells, CDK2AP1 and kinesin-1 co-immunoprecipitated and co-localized in the cells. These results suggest that the KIF5A-CDK2AP1 interaction serves as an adapter protein connecting kinesin-1 and the cargo when kinesin-1 transports cargo in cells.

DNA Repair Activity of Human rpS3 is Operative to Genotoxic Damage in Bacteria

  • JANG CHANG-YOUNG;LEE JAE YUNG;KIM JOON
    • Journal of Microbiology and Biotechnology
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    • v.15 no.3
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    • pp.484-490
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    • 2005
  • Human ribosomal protein S3 (rpS3), which has a DNA repair endonuclease activity, is a multifunctional protein. This protein is involved in DNA repair, translation, and apoptosis. In particular, rpS3 has a lyase activity, which cleaves the phosphodiester bond of damaged sites such as cyclobutane pyrimidine dimers and AP sites. Here, using deletion analysis, we identified that the repair endonuclease domain resides in the C-terminal region (165-243 aa) of rpS3. We also found that ectopic expression of GST-rpS3 in bacterial strain BL21 promoted the resistance of these cells to ultraviolet (UV) radiation and hydrogen peroxide ($H_{2}O_{2}$) treatment. The repair domain of rpS3 was sufficient to exhibit the resistance to UV irradiation and recover cell growth and viability, showing that the repair activity of rpS3 is responsible for the resistance to UV irradiation. Our study suggests that rpS3 is able to process DNA damage in bacteria via its repair domain, showing the resistance to genotoxic stress. This implies that rpS3-like activity could be operative in bacteria.

L1 Cell Adhesion Molecule Suppresses Macrophage-mediated Inflammatory Responses (L1 Cell Adhesion Molecule에 의한 대식세포 매개 염증반응의 억제 기전 분석)

  • Yi, Young-Su
    • YAKHAK HOEJI
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    • v.60 no.3
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    • pp.128-134
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    • 2016
  • L1 cell adhesion molecule (L1CAM) is a cell surface molecule to initiate a variety of cellular responses through interacting with other cell adhesion molecules in a homophilic or heterophilic manner. Although its expression was found to be upregulated in some tumor cells, including cholangiocarcinomas, and ovarian cancers, and many studies have investigated the role of L1CAM in these cancers, its role in inflammatory responses has been poorly understood. In this study, we explored the role of L1CAM in macrophage-mediated inflammatory responses. L1CAM significantly suppressed the production of nitric oxide (NO), but induced cell proliferation in RAW264.7 cells. L1CAM expression was detectable, but its expression was markedly decreased by lipopolysaccharide (LPS) in RAW264.7 cells. In addition, the expression of pro-inflammatory genes, such as tumor necrosis factor (TNF)-${\alpha}$, cyclooxygenase (COX)-2, and inducible nitric oxide synthase (iNOS) induced by LPS was dramatically suppressed by L1CAM in RAW264.7 cells. L1CAM inhibited the transcriptional activities of NF-${\kappa}B$ and AP-1 while its cytoplasmic domain deletion form, $L1{\Delta}CD$ did not suppressed their activities in RAW264.7 cells. Moreover, L1CAM suppressed nuclear translocation of p65 and p50 as well as c-Jun, c-Fos and p-ATF2 which are transcription factors of NF-${\kappa}B$ and AP-1, respectively. In conclusion, L1CAM suppressed inflammatory responses in macrophages through inhibiting NF-${\kappa}B$ and AP-1 pathways.

POSITIVE SOLUTION FOR A CLASS OF NONLOCAL ELLIPTIC SYSTEM WITH MULTIPLE PARAMETERS AND SINGULAR WEIGHTS

  • AFROUZI, G.A.;ZAHMATKESH, H.
    • Journal of applied mathematics & informatics
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    • v.35 no.1_2
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    • pp.121-130
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    • 2017
  • This study is concerned with the existence of positive solution for the following nonlinear elliptic system $$\{-M_1(\int_{\Omega}{\mid}x{\mid}^{-ap}{\mid}{\nabla}u{\mid}^pdx)div({\mid}x{\mid}^{-ap}{\mid}{\nabla}u{\mid}^{p-2}{\nabla}u)\\{\hfill{120}}={\mid}x{\mid}^{-(a+1)p+c_1}\({\alpha}_1A_1(x)f(v)+{\beta}_1B_1(x)h(u)\),\;x{\in}{\Omega},\\-M_2(\int_{\Omega}{\mid}x{\mid}^{-bq}{\mid}{\nabla}v{\mid}^qdx)div({\mid}x{\mid}^{-bq}{\mid}{\nabla}v{\mid}^{q-2}{\nabla}v)\\{\hfill{120}}={\mid}x{\mid}^{-(b+1)q+c_2}\({\alpha}_2A_2(x)g(u)+{\beta}_2B_2(x)k(v)\),\;x{\in}{\Omega},\\{u=v=0,\;x{\in}{\partial}{\Omega},$$ where ${\Omega}$ is a bounded smooth domain of ${\mathbb{R}}^N$ with $0{\in}{\Omega}$, 1 < p, q < N, $0{\leq}a$ < $\frac{N-p}{p}$, $0{\leq}b$ < $\frac{N-q}{q}$ and ${\alpha}_i,{\beta}_i,c_i$ are positive parameters. Here $M_i,A_i,B_i,f,g,h,k$ are continuous functions and we discuss the existence of positive solution when they satisfy certain additional conditions. Our approach is based on the sub and super solutions method.

An ARIA-Interacting AP2 Domain Protein Is a Novel Component of ABA Signaling

  • Lee, Sun-ji;Cho, Dong-im;Kang, Jung-youn;Kim, Soo Young
    • Molecules and Cells
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    • v.27 no.4
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    • pp.409-416
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    • 2009
  • ADAP is an AP2-domain protein that interacts with ARIA, which, in turn, interacts with ABF2, a bZIP class transcription factor. ABF2 regulates various aspects of the abscisic acid (ABA) response by controlling the expression of a subset of ABA-responsive genes. Our expression analyses indicate that ADAP is expressed in roots, emerging young leaves, and flowers. We found that adap knockout mutant lines germinate more efficiently than wild-type plants and that the mutant seedlings grow faster. This suggests that ADAP is involved in the regulation of germination and seedling growth. Both germination and post-germination growth of the knockout mutants were partially insensitive to ABA, which indicates that ADAP is required for a full ABA response. The survival rates for mutants from which water was withheld were low compared with those for wild-type plants. The result shows that ADAP is necessary for the response to stress induced by water deprivation. Together, our data indicate that ADAP is a positive regulator of the ABA response and is also involved in regulating seedling growth. The role of ADAP is similar to that of ARIA, which is also a positive regulator of the ABA response. It appears that ADAP acts through the same ABA response pathway as ARIA.

Design and Implementation of ISO/IEEE 11073 DIM Transmission Structure Based on oneM2M for IoT Healthcare Service (사물인터넷 헬스케어 서비스를 위한 oneM2M기반 ISO/IEEE 11073 DIM 전송 구조 설계 및 구현)

  • Kim, Hyun Su;Chun, Seung Man;Chung, Yun Seok;Park, Jong Tae
    • Journal of the Institute of Electronics and Information Engineers
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    • v.53 no.4
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    • pp.3-11
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    • 2016
  • In the environment of Internet of Things (IoT), IoT devices are limited by physical components such as power supply and memory, and also limited to their network performance in bandwidth, wireless channel, throughput, payload, etc. Despite these limitations, resources of IoT devices are shared with other IoT devices. Especially, remote management of the information of devices and patients are very important for the IoT healthcare service, moreover, providing the interoperability between the healthcare device and healthcare platform is essential. To meet these requirements, format of the message and the expressions for the data information and data transmission need to comply with suitable international standards for the IoT environment. However, the ISO/IEEE 11073 PHD (Personal Healthcare Device) standards, the existing international standards for the transmission of health informatics, does not consider the IoT environment, and therefore it is difficult to be applied for the IoT healthcare service. For this matter, we have designed and implemented the IoT healthcare system by applying the oneM2M, standards for the Internet of Things, and ISO/IEEE 11073 DIM (Domain Information Model), standards for the transmission of health informatics. For the implementation, the OM2M platform, which is based on the oneM2M standards, has been used. To evaluate the efficiency of transfer syntaxes between the healthcare device and OM2M platform, we have implemented comparative performance evaluation between HTTP and CoAP, and also between XML and JSON by comparing the packet size and number of packets in one transaction.

Cloning And Characterization of Pathogen-Inducible EREBP-Like Transcription Factor(CaNR19) From Hot Pepper (Capsicum annuum L.)

  • Yi, So-Young;Kim, Jee-Hyub;Yu, Seung-Hun;Park, Doil
    • Proceedings of the Korean Society of Plant Pathology Conference
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    • 2003.10a
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    • pp.77.2-78
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    • 2003
  • An EREBP/AP2-type transcription factor (CaPFl) was isolated by DDRT-PCR following inoculation of soybean pustule pathogen Xanthomonas axonopodis pv. glycines Bra which induces HR on pepper leaves. Genomic Southern blot analysis revealed that the CaPFl gene is present as a single copy within the hot pepper genome. The deduced amino acid sequence of CaPFl has two potential nuclear localization signals, a possible acidic activation domain, and an EREBP/AP2 motif that could bind to a conserved cis- element present in promoter region of many stress-induced genes. The mRNA level of CaPFl was induced by both biotic and abiotic stresses. We observed higher-level transcripts in resistance-induced pepper tissues than diseased tissues. Expression of CaPFl is also induced upon various abiotic stresses including ethephon, MeJA, cold stress, drought stress and salt stress treatments. To study the role of CPFI in plant, transgenic Arabidopsis and tobacco plants which express higher level of pepper CaPFl were generated. Global gene expression analysis of transgenic Arabidopsis by cDNA microarray indicated that expression of CaPFl in transgenic plants affect the expression of quite a few GCC box and DRE/CRT box-containing genes. Furthermore, the transgenic Arabidopsis and tobacco plant, expressing CaPFl showed tolerance against freezing temperature and enhanced resistance to Pseudomonas syrnigae pv. tabaci. Taken together, these results indicated that CaPFl is a novel EREBP/AP2 transcription factor in hot pepper plant and it may has a significant role(s) in regulation of biotic and abiotic stresses in plant.

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ZNF435, a Novel Human SCAN-containing Zinc Finger Protein, Inhibits AP-1-mediated Transcriptional Activation

  • Gu, Xing;Zheng, Mei;Fei, Xiangwei;Yang, Zhenxing;Li, Fan;Ji, Chaoneng;Xie, Yi;Mao, Yumin
    • Molecules and Cells
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    • v.23 no.3
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    • pp.316-322
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    • 2007
  • Zinc finger transcription factor genes are a significant fraction of the genes in the vertebrate genome. Here we report the isolation and characterization of a human zinc finger-containing gene, ZNF435, from a fetal brain cDNA library. ZNF435 cDNA is 1290 base pairs in length and contains an open reading frame encoding 349 amino acids with four C2H2-type zinc fingers at its carboxyl terminus and a SCAN motif at its amino terminus. RT-PCR results showed that ZNF435 was expressed in all tested tissues. A ZNF435-GFP fusion protein was located in the nucleus and the four zinc fingers acted as nuclear localization signals (NLSs). ZNF435 was found to be capable of homo-association, and this effect was independent of its zinc fingers. Furthermore, ZNF435 proved to be a transcription repressor as its overexpression in AD293 cells inhibited the transcriptional activities of AP-1.

KBTBD7, a novel human BTB-kelch protein, activates transcriptional activities of SRE and AP-1

  • Hu, Junjian;Yuan, Wuzhou;Tang, Ming;Wang, Yuequn;Fan, Xiongwei;Mo, Xiaoyang;Li, Yongqing;Ying, Zaochu;Wan, Yongqi;Ocorr, Karen;Bodmer, Rolf;Deng, Yun;Wu, Xiushan
    • BMB Reports
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    • v.43 no.1
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    • pp.17-22
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    • 2010
  • In this study, a novel member of BTB-kelch proteins, named KBTBD7, was cloned from a human embryonic heart cDNA library. The cDNA of KBTBD7 is 3,008 bp long and encodes a protein product of 684 amino acids (77.2 kD). This protein is highly conserved in evolution across different species. Western blot analysis indicates that a 77 kD protein specific for KBTBD7 is wildly expressed in all embryonic tissues examined. In COS-7 cells, KBTBD7 proteins are localized to the cytoplasm. KBTBD7 is a transcription activator when fused to GAL4 DNA-binding domain. Deletion analysis indicates that the BTB domain and kelch repeat motif are main regions for transcriptional activation. Overexpression of KBTBD7 in MCF-7 cells activates the transcriptional activities of activator protein-1 (AP-1) and serum response element (SRE), which can be relieved by siRNA. These results suggest that KBTBD7 proteins may act as a new transcriptional activator in mitogen-activated protein kinase (MAPK) signaling.

ZNF552, a novel human KRAB/C2H2 zinc finger protein, inhibits AP-1- and SRE-mediated transcriptional activity

  • Deng, Yun;Liu, Bisheng;Fan, Xiongwei;Wang, Yuequn;Tang, Ming;Mo, Xiaoyang;Li, Yongqing;Ying, Zaochu;Wan, Yongqi;Luo, Na;Zhou, Junmei;Wu, Xiushan;Yuan, Wuzhou
    • BMB Reports
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    • v.43 no.3
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    • pp.193-198
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    • 2010
  • In this study, we report the identification and characterization of a novel C2H2 zinc finger protein, ZNF552, from a human embryonic heart cDNA library. ZNF552 is composed of three exons and two introns and maps to chromosome 19q13.43. The cDNA of ZNF552 is 2.3 kb, encoding 407 amino acids with an amino-terminal KRAB domain and seven carboxyl-terminal C2H2 zinc finger motifs in the nucleus and cytoplasm. Northern blotting analysis indicated that a 2.3 kb transcript specific for ZNF552 was expressed in liver, lung, spleen, testis and kidney, especially with a higher level in the lung and testis in human adult tissues. Reporter gene assays showed that ZNF552 was a transcriptional repressor, and overexpression of ZNF552 in the COS-7 cells inhibited the transcriptional activities of AP-1 and SRE, which could be relieved through RNAi analysis. Deletion studies showed that the KRAB domain of ZNF552 may be involved in this inhibition.