Relevant bibliographies by topics / Yes-associated protein 1 (YAP)

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  2. Dissertations / Theses
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  4. Conference papers
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Academic literature on the topic 'Yes-associated protein 1 (YAP)'

Author: Grafiati
Published: 5 April 2025

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Journal articles on the topic "Yes-associated protein 1 (YAP)"

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Qi, Qi, Dean Y. Li, Hongbo R. Luo, Kun-Liang Guan, and Keqiang Ye. "Netrin-1 exerts oncogenic activities through enhancing Yes-associated protein stability." Proceedings of the National Academy of Sciences 112, no. 23 (May 26, 2015): 7255–60. http://dx.doi.org/10.1073/pnas.1505917112.

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Yes-associated protein (YAP), a transcription coactivator, is the major downstream effector of the Hippo pathway, which plays a critical role in organ size control and cancer development. However, how YAP is regulated by extracellular stimuli in tumorigenesis remains incompletely understood. Netrin-1, a laminin-related secreted protein, displays proto-oncogenic activity in cancers. Nonetheless, the downstream signaling mediating its oncogenic effects is not well defined. Here we show that netrin-1 via its transmembrane receptors, deleted in colorectal cancer and uncoordinated-5 homolog, up-regulates YAP expression, escalating YAP levels in the nucleus and promoting cancer cell proliferation and migration. Inactivating netrin-1, deleted in colorectal cancer, or uncoordinated-5 homolog B (UNC5B) decreases YAP protein levels, abrogating cancer cell progression by netrin-1, whereas knockdown of mammalian STE20-like protein kinase 1/2 (MST1/2) or large tumor suppressor kinase 1/2 (Lats1/2), two sets of upstream core kinases of the Hippo pathway, has no effect in blocking netrin-1–induced up-regulation of YAP. Netrin-1 stimulates phosphatase 1A to dephosphorylate YAP, which leads to decreased ubiquitination and degradation, enhancing YAP accumulation and signaling. Hence, our findings support that netrin-1 exerts oncogenic activity through YAP signaling, providing a mechanism coupling extracellular signals to the nuclear YAP oncogene.
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Wu, Gaoliang, Chao Hao, Xueliang Qi, and Jianqiang Nie. "Effect of Yes Associated Protein 1 Silence on Proliferation and Apoptosis of Bladder Cancer Cells." Journal of Biomaterials and Tissue Engineering 11, no. 5 (May 1, 2021): 857–63. http://dx.doi.org/10.1166/jbt.2021.2637.

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Yes Associated Protein 1 (YAP) can act as either an oncoprotein or a tumor suppressor in different cellular contexts. However, the reports about the direct role of YAP silence in bladder cancer cells are rare. We designed loss-off-function experiments to investigate the effect of YAP knockdown on bladder cancer cell proliferation, cell cycle and cell apoptosis. We examined YAP expression in human bladder cancer and paracancerous tissues using RT-qPCR, western blot and immunohisto-chemistry. YAP short hairpin RNA (shRNA) was successfully constructed and transfected into T24 cells to knockdown YAP. Cell proliferation, cell cycle and cell apoptosis were analyzed by CCK-8 and flow cytometry. We found the expression levels of YAP mRNA and protein were significantly increased in the bladder cancer tissues when compared with that in the paracancerous tissues. shRNA YAP inhibited cell proliferation, induced cell cycle arrest at G1 phase, and induced cell apoptosis. In conclusion, our findings provided the first evidence that YAP knockdown could inhibit cell proliferation and induce cell apoptosis of bladder cancer cells. YAP inhibition may be beneficial in the treatment of bladder cancer.
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Khan, Kashif, Georges Makhoul, Bin Yu, Adel Schwertani, and Renzo Cecere. "The cytoprotective impact of yes-associated protein 1 after ischemia-reperfusion injury in AC16 human cardiomyocytes." Experimental Biology and Medicine 244, no. 10 (May 29, 2019): 802–12. http://dx.doi.org/10.1177/1535370219851243.

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The Hippo-signaling pathway is a mechanism implicated in cardiomyocyte cytoprotection and regeneration after a myocardial infarction. Yes-associated protein 1, the main effector protein of this pathway, acts as a co-transcriptional activator to promote cardiomyocyte proliferation and survival. However, the biological mechanisms by which yes-associated protein 1 protects the heart post-MI are currently unknown. Here, we propose that yes-associated protein 1 plays a critical role in cardiomyocyte cytoprotection after simulated ischemia-reperfusion injury. AC16 human cardiomyocytes were infected with lentiviral plasmids containing normal human yes-associated protein 1 and a constitutively active form of YAP, YAP1S127A. Cells were exposed to ischemia-reperfusion injury using a hypoxic chamber. Hippo-signaling characterization after ischemia-reperfusion injury was performed via Western blotting and reverse transcriptase polymerase chain reaction. Cell viability, apoptosis, and cellular hypertrophy were assessed as a measure of cytoprotection. The GSK3β inhibitor CHIR99021 was used to investigate cross-talk between Hippo and Wnt-signaling and their role in cytoprotection after ischemia-reperfusion-injury. Ischemia-reperfusion injury resulted in significant decreased expression of the non-phosphorylated Hippo signaling kinases MST1 and LATS1, along with decreased expression of YAP/TAZ. Overexpression of yes-associated protein 1 improved cellular viability, while reducing hypertrophy and apoptosis via the ATM/ATR DNA damage response pathway. Activation of β-catenin in YAP-infected cardiomyocytes synergistically reduced cellular hypertrophy after ischemia-reperfusion-injury. Our findings indicate that yes-associated protein 1 is cytoprotective in AC16 human cardiomyocytes after ischemia-reperfusion injury, which may be mediated by co-activation of the canonical Wnt/β-catenin pathway. Thus, activation of yes-associated protein 1 may be a novel therapeutic to repair the infarcted myocardium. Impact statement Genetically engineering the cells of the heart after myocardial infarction to display a more regenerative phenotype is a promising therapy for heart failure patients. Here, we support a regenerative role for yes-associated protein 1, the main effector protein of the Hippo signaling pathway, in AC16 human cardiomyocytes as a potential therapeutic gene target for cardiac repair after myocardial infarction.
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Irie, Kazuki, Tomoaki Nagai, and Kensaku Mizuno. "Furry protein suppresses nuclear localization of yes-associated protein (YAP) by activating NDR kinase and binding to YAP." Journal of Biological Chemistry 295, no. 10 (January 29, 2020): 3017–28. http://dx.doi.org/10.1074/jbc.ra119.010783.

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The Hippo signaling pathway suppresses cell proliferation and tumorigenesis. In the canonical Hippo pathway, large tumor suppressor kinases 1/2 (LATS1/2) phosphorylate the transcriptional coactivator yes-associated protein (YAP) and thereby suppress its nuclear localization and co-transcriptional activity. Nuclear Dbf2-related kinases 1/2 (NDR1/2), which are closely related to LATS1/2, also phosphorylate and inactivate YAP by suppressing its nuclear localization. Furry (FRY) is a cytoplasmic protein that associates with NDR1/2 and activates them, but its role in the nuclear/cytoplasmic localization of YAP remains unknown. Here, we constructed FRY-knockout cell lines to examine the role of FRY in YAP's cytoplasmic localization. FRY depletion markedly increased YAP nuclear localization and decreased NDR1/2 kinase activity and YAP phosphorylation levels, but did not affect LATS1/2 kinase activity. This indicated that FRY suppresses YAP's nuclear localization by promoting its phosphorylation via NDR1/2 activation. NDR1/2 depletion also promoted YAP nuclear localization, but depletion of both FRY and NDR1/2 increased the number of cells with YAP nuclear localization more strongly than did depletion of NDR1/2 alone, suggesting that FRY suppresses YAP nuclear localization by a mechanism in addition to NDR1/2 activation. Co-precipitation assays revealed that Fry uses its N-terminal 1–2400-amino-acid-long region to bind to YAP. Expression of full-length FRY or its 1–2400 N-terminal fragment restored YAP cytoplasmic localization in FRY-knockout cells. Taken together, these results suggest that FRY plays a crucial role in YAP cytoplasmic retention by promoting YAP phosphorylation via NDR1/2 kinase activation and by binding to YAP, leading to its cytoplasmic sequestration.
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Zhang, Heng, and Shengnan Wu. "Yes-Associated Protein (YAP) Promotes the Nuclear Import of p73." Journal of Physics: Conference Series 277 (January 1, 2011): 012050. http://dx.doi.org/10.1088/1742-6596/277/1/012050.

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Hsu, Ping-Chih, Cheng-Ta Yang, David Jablons, and Liang You. "The Role of Yes-Associated Protein (YAP) in Regulating Programmed Death-Ligand 1 (PD-L1) in Thoracic Cancer." Biomedicines 6, no. 4 (December 7, 2018): 114. http://dx.doi.org/10.3390/biomedicines6040114.

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The programmed death-ligand 1(PD-L1)/PD-1 pathway is an immunological checkpoint in cancer cells. The binding of PD-L1 and PD-1 promotes T-cell tolerance and helps tumor cells escape from host immunity. Immunotherapy targeting the PD-L1/PD-1 axis has been developed as an anti-cancer therapy and used in treating advanced human non-small cell lung cancer (NSCLC) and malignant pleural mesothelioma (MPM). Yes-associated protein (YAP) is a key mediator of the Hippo/YAP signaling pathway, and plays important roles in promoting cancer development, drug resistance and metastasis in human NSCLC and MPM. YAP has been suggested as a new therapeutic target in NSCLC and MPM. The role of YAP in regulating tumor immunity such as PD-L1 expression has just begun to be explored, and the correlation between YAP-induced tumorigenesis and host anti-tumor immune responses is not well known. Here, we review recent studies investigating the correlation between YAP and PD-L1 and demonstrating the mechanism by which YAP regulates PD-L1 expression in human NSCLC and MPM. Future work should focus on the interactions between Hippo/YAP signaling pathways and the immune checkpoint PD-L1/PD-1 pathway. The development of new synergistic drugs for immune checkpoint PD-L1/PD-1 blockade in NSCLC and MPM is warranted.
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DAREEN A. MOHAMED, M.D., RANIA A. R. EL-TATAWY, M. D., and YOMNA MAZID EL-HAMD A. NEINAA, M. D. HEBA A.A. EL-BANBI, M.Sc. "Immunohistochemical Expression of Yes-Associated Protein-1 (YAP-1) in Cutaneous Lichen Planus." Medical Journal of Cairo University 87, June (June 10, 2019): 1769–73. http://dx.doi.org/10.21608/mjcu.2019.53963.

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Sharifi-Sanjani, Maryam, Mariah Berman, Dmitry Goncharov, Mohammad Alhamaydeh, Theodore Guy Avolio, Jeffrey Baust, Baojun Chang, et al. "Yes-Associated Protein (Yap) Is Up-Regulated in Heart Failure and Promotes Cardiac Fibroblast Proliferation." International Journal of Molecular Sciences 22, no. 11 (June 7, 2021): 6164. http://dx.doi.org/10.3390/ijms22116164.

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Left ventricular (LV) heart failure (HF) is a significant and increasing cause of death worldwide. HF is characterized by myocardial remodeling and excessive fibrosis. Transcriptional co-activator Yes-associated protein (Yap), the downstream effector of HIPPO signaling pathway, is an essential factor in cardiomyocyte survival; however, its status in human LV HF is not entirely elucidated. Here, we report that Yap is elevated in LV tissue of patients with HF, and is associated with down-regulation of its upstream inhibitor HIPPO component large tumor suppressor 1 (LATS1) activation as well as upregulation of the fibrosis marker connective tissue growth factor (CTGF). Applying the established profibrotic combined stress of TGFβ and hypoxia to human ventricular cardiac fibroblasts in vitro increased Yap protein levels, down-regulated LATS1 activation, increased cell proliferation and collagen I production, and decreased ribosomal protein S6 and S6 kinase phosphorylation, a hallmark of mTOR activation, without any significant effect on mTOR and raptor protein expression or phosphorylation of mTOR or 4E-binding protein 1 (4EBP1), a downstream effector of mTOR pathway. As previously reported in various cell types, TGFβ/hypoxia also enhanced cardiac fibroblast Akt and ERK1/2 phosphorylation, which was similar to our observation in LV tissues from HF patients. Further, depletion of Yap reduced TGFβ/hypoxia-induced cardiac fibroblast proliferation and Akt phosphorylation at Ser 473 and Thr308, without any significant effect on TGFβ/hypoxia-induced ERK1/2 activation or reduction in S6 and S6 kinase activities. Taken together, these data demonstrate that Yap is a mediator that promotes human cardiac fibroblast proliferation and suggest its possible contribution to remodeling of the LV, opening the door to further studies to decipher the cell-specific roles of Yap signaling in human HF.
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Pilgrim, Adeiye A., Hunter C. Jonus, Andrew Ho, Anna Cole, Jenny Shim, and Kelly C. Goldsmith. "Abstract 3545: The Yes-associated protein (YAP) regulates GD2 immunotherapy response in high-risk neuroblastoma." Cancer Research 83, no. 7_Supplement (April 4, 2023): 3545. http://dx.doi.org/10.1158/1538-7445.am2023-3545.

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Abstract Background Patients with the pediatric solid tumor high-risk neuroblastoma (HR NB) receive intense multimodal therapy yet 50% still relapse with chemotherapy-resistant disease. Relapsed NBs harbor increased RAS/MAPK pathway mutations and increased expression and downstream activity of the transcriptional co-regulator YAP. We have previously shown that YAP mediates resistance to chemotherapy and MEK inhibitors in RAS mutant NBs (Shim et al., Cancer Res 2020). Patients with relapsed NB are treated with the GD2-targeting monoclonal antibody dinutuximab in combination with chemotherapy. Given the increased expression and activity of YAP in relapsed HR NB, we posited that YAP might also play a role in GD2 immunotherapy response. Methods/Results We stably knocked down YAP in the human derived NRAS mutant SK-N-AS NB cell line with a scrambled short hairpin (sh) control or 2 YAP-targeting shRNAs to generate 3 distinct cell lines. Dinutuximab requires antibody-dependent cellular cytotoxicity (ADCC) and we have shown that gamma delta (γδ) T cells augment dinutuximab in aggressive NB models. We exposed the shYAP1, shYAP2, and control SK-N-AS cells to γδ T cells with/without dinutuximab. YAP knockdown sensitized both SK-N-AS shYAP cell lines to γδ T cell killing both in the presence and absence of dinutuximab. To investigate the mechanism of increased dinutuximab sensitivity, we evaluated a panel of NB cell lines (MYCN amplified and MYCN single copy) for YAP protein and GD2 cell surface expression and noted an inverse relationship. That same inverse correlation was found for GD2 and YAP gene expression in primary HR NB tumor datasets. We therefore evaluated GD2 expression following YAP knockdown in SK-N-AS and show that GD2 significantly increased on the cell surface following YAP inhibition. PRRX1 is a master transcription factor that induces a mesenchymal NB phenotype which is one of high YAP expression with very low to no GD2 surface expression. Interestingly, PRRX1 expression increased in YAP knockdown cells yet GD2 expression also increased, suggesting YAP regulates GD2 expression more directly than PRRX1. In the GD2 biosynthesis pathway, GM3 is converted into GD3 by GD3 synthase (GD3S). GD2 synthase then catalyzes GD3 into GD2. GD3S gene (ST8SIA1) expression significantly increased (>100-fold) upon YAP knockdown. Furthermore, shRNA stable inhibition of GD3S in shYAP NB cells reverted the phenotype and decreased GD2 cell surface expression back to baseline. We then treated established SK-N-AS control or shYAP xenografts with an 18-day course of human γδ T cells, dinutuximab, and cyclophosphamide. Pilot results show significantly extended survival in mice harboring SK-N-AS shYAP tumors. Conclusion These results support YAP regulation of GD2 expression through transcriptional suppression of GD3 synthase and identify YAP as a therapeutic target to augment GD2 immunotherapy responses in HR and relapsed NB. Citation Format: Adeiye A. Pilgrim, Hunter C. Jonus, Andrew Ho, Anna Cole, Jenny Shim, Kelly C. Goldsmith. The Yes-associated protein (YAP) regulates GD2 immunotherapy response in high-risk neuroblastoma. [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2023; Part 1 (Regular and Invited Abstracts); 2023 Apr 14-19; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2023;83(7_Suppl):Abstract nr 3545.
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Venkatasubramanian, Gomathi, Devaki A. Kelkar, Susmita Mandal, Mohit Kumar Jolly, and Madhura Kulkarni. "Analysis of Yes-Associated Protein-1 (YAP1) Target Gene Signature to Predict Progressive Breast Cancer." Journal of Clinical Medicine 11, no. 7 (March 31, 2022): 1947. http://dx.doi.org/10.3390/jcm11071947.

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Breast cancers are treated according to the ER/PR or HER2 expression and show better survival outcomes with targeted therapy. Triple-negative breast cancers (TNBCs) with a lack of expression of ER/PR and HER2 are treated with systemic therapy with unpredictable responses and outcomes. It is essential to investigate novel markers to identify targeted therapies for TNBC. One such marker is YAP1, a transcription co-activator protein that shows association with poor prognosis of breast cancer. YAP1 transcriptionally regulates the expression of genes that drive the oncogenic phenotypes. Here, we assess a potential YAP target gene signature to predict a progressive subset of breast tumors from METABRIC and TCGA datasets. YAP1 target genes were shortlisted based on expression correlation and concordance with YAP1 expression and significant association with survival outcomes of patients. Hierarchical clustering was performed for the shortlisted genes. The utility of the clustered genes was assessed by survival analysis to identify a recurring subset. Expression of the shortlisted target genes showed significant association with survival outcomes of HER2-positive and TNBC subset in both datasets. The shortlisted genes were verified using an independent dataset. Further validation using IHC can prove the utility of this potential prognostic signature to identify a recurrent subset of HER2-positive and TNBC subtypes.
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Dissertations / Theses on the topic "Yes-associated protein 1 (YAP)"

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Nord, Dianna M. "Knockdown of the Yes-associated Protein 1 pathway provides a basis for targeted therapy to treat infantile hemangioma." Thesis, Georgia Institute of Technology, 2015. http://hdl.handle.net/1853/53736.

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Hemangioma is a type of tumor commonly found in infants that is characterized by heavy vascularization and a disfiguring appearance. Hemangioma, though benign, can sometimes proliferate and be threatening to infants. Current treatments for infantile hemangioma include surgical removal as well as the use of topical and oral medication. However, current therapies are often ineffective at treating lesions and are commonly accompanied by dangerous side effects, creating the need for a new, safer treatment. This study targets the Yes-Associated Protein-1 (YAP-1), which has been described as an oncogene, by use of an interfering RNA technique in attempts to mediate tumor growth and progression. Western blotting of treatment and control BEND3 murine cells reveals that YAP-1 is knocked-down in treatment groups which have been infected with shYAP-1 siRNA genes. By successfully knocking down the YAP-1 protein, the potential for developing a novel targeted therapy for infantile hemangioma has been established.
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Ruscica, Biagina. "The critical role of YAP and TAZ in tubular homeostasis." Electronic Thesis or Diss., Université Paris Cité, 2024. https://wo.app.u-paris.fr/cgi-bin/WebObjects/TheseWeb.woa/wa/show?t=6623&f=77103.

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Des études épidémiologiques et expérimentales suggèrent que la progression de la maladie rénale chronique (MRC) après une lésion initiale est génétiquement déterminée, mais les réseaux génétiques qui contribuent à cette prédisposition restent inconnus. Parmi les voies moléculaires potentielles impliquées dans la MRC, cette étude s'est concentrée sur la voie Hippo, une cascade de signalisation conservée au cours de l'évolution et cruciale pour la régulation de la taille des organes et de la prolifération cellulaire. Les protéines paralogues YAP et TAZ, deux coactivateurs transcriptionnels de la voie Hippo, ont récemment été identifiées comme étant également des mécanosenseurs, capables de détecter un large éventail de signaux mécaniques et de les traduire en programmes transcriptionnels spécifiques aux cellules. L'activation de YAP et TAZ a été impliquée dans la progression de plusieurs maladies rénales et dans la transition de la lésion rénale aiguë (LRA) à la MRC . Cependant, les mécanismes sous-jacents restent obscurs et leur rôle dans des conditions physiologiques n'est pas encore bien compris. L'objectif de ce projet est d'élucider le rôle de YAP et TAZ dans les tubules rénaux. Tout d'abord, en utilisant la combinaison de modèles de souris transgéniques et de néphrectomie comme modèle de MRC, nous avons étudié l'effet de l'inactivation sélective du gène Yap ou Taz dans les cellules tubulaires rénales dans ce contexte de maladie. Nos résultats ont révélé une redondance potentielle entre ces deux protéines dans les cellules épithéliales tubulaires. Il est intéressant de noter que nos souris déficientes à la fois en YAP et en TAZ ont développé spontanément un phénotype rénal sévère avec des lésions tubulaires, de la fibrose et de l'inflammation, qui a été décrit en détail dans ce travail. Grâce à l'analyse transcriptomique, nous avons identifié une nouvelle signature moléculaire qui pourrait permettre de mieux comprendre les mécanismes régulés par YAP et TAZ dans les cellules tubulaires. Paradoxalement, dans notre modèle de double knock-out, nous avons observé une aggravation de l'expression et de l'activation de YAP et TAZ, parallèlement à la progression des lésions. Ceci semble être le résultat d'une expansion des cellules « non recombinées », montrant les rôles complexes de YAP et TAZ dans la communication avec les cellules voisines. Ces données démontrent le rôle essentiel de YAP et TAZ dans le maintien de l'homéostasie tubulaire et l'équilibre complexe nécessaire à leur régulation. Cette complexité peut avoir des implications pour les stratégies thérapeutiques ciblant l'inhibition de YAP et TAZ dans les maladies rénales, surtout si l'on considère les effets secondaires potentiels qui pourraient rendre ces approches plus difficiles
Epidemiological and experimental studies suggest that the progression of Chronic Kidney Disease (CKD) after an initial injury is genetically determined, but the genetic networks that contribute to this predisposition remain unknown. Among the potential molecular pathways involved in CKD, this study focused on the Hippo pathway, an evolutionarily conserved signaling cascade crucial for regulating organ size and cell proliferation. The paralogs proteins YAP and TAZ, two transcriptional coactivators of the Hippo pathway, have recently been identified also as mechanosensors, capable of detecting a wide range of mechanical cues and translating them into cell-specific transcriptional programs. Activation of YAP and TAZ has been implicated to the progression of several kidney diseases and in the transition from acute kidney injury (AKI) to CKD. However, the underlying mechanisms remain unclear and their role under physiological conditions is still not well understood. The aim of this project is to elucidate the role of YAP and TAZ in the renal tubules. First, using the combination of inducing transgenic mouse models and nephrectomy as a model of CKD, we investigated the effect of the selective inactivation of Yap or Taz gene in renal tubular cells in this disease context. Our findings revealed a potential redundancy between these two proteins in tubular epithelial cells. Interestingly, our mice deficient in both YAP and TAZ developed a spontaneous severe renal phenotype with tubular injury, fibrosis and inflammation, which was described in detail in this work. Through transcriptomic analysis, we identified a new novel molecular signature that may provide further insight into the mechanisms regulated by YAP and TAZ in tubular cells. Paradoxically, in our double knock-out model, we observed a worsening of YAP and TAZ expression and activation, in parallel with the lesion progression. This appeared to be the result of an expansion of the "non-recombined" cells, showing the complex roles of YAP and TAZ in the cross-talk with the neighbouring cells. These data demonstrated the essential role of YAP and TAZ in maintaining tubular homeostasis and the intricate balance required for their regulation. This complexity may have implications for therapeutic strategies targeting the inhibition of YAP and TAZ in kidney disease, especially considering the potential side effects that could make such approaches more challenging
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Guinto, Ferdiemar Cardenas Jr. "Investigating Secondary Structure Features of YAP1 Protein Fragments Using Molecular Dynamics (MD) and Steered Molecular Dynamics (SMD) Simulations." Scholarly Commons, 2017. https://scholarlycommons.pacific.edu/uop_etds/2973.

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Molecular dynamics (MD) is a powerful tool that can be applied to protein folding and protein structure. MD allows for the calculation of movement, and final position, of atoms in a biomolecule. These movements can be used to investigate the pathways that allow proteins to fold into energetically favorable structures. While MD is very useful, it still has its limitations. Most notable, computing power and time are of constant concern. Protein structure is inherently important due to the direct link between the structure of a protein and its function. One of the four levels of protein structure, the secondary structure, is the first level to accommodate for the three-dimensional shape of a protein. The main driving force behind secondary structure is hydrogen bonding, which occurs between the carboxyl oxygen and the amine hydrogen of the backbone of a peptide. Determining a greater link between hydrogen bond patterns and types of secondary structure can provide more insight on how proteins fold. Because molecular dynamics allows for an atomic level view of the dynamics behind protein folding/unfolding, it becomes very useful in observing the effects of particular hydrogen bond patterns on the folding pathway and final structure formed of a protein. Using molecular dynamic simulations, a series of experiments in an attempt to alter structure, hydrogen bonding, and folding patterns, can be performed. This information can be used to better understand the driving force of secondary structure, and use the knowledge gained to manipulate these simulations to force folding events, and with that, desired secondary structure features.
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徐智 and Zhi Xu. "Yes associated protein (YAP) in hepatocellular carcinoma: oncogenic functions and molecular targeting." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2009. http://hub.hku.hk/bib/B43278589.

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Gesell, Anne E. "Investigating the role of Yes-associated protein (YAP) in neural crest development." Thesis, University of Bath, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.681035.

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The neural crest (NC) is a multipotent embryonic cell type derived from the ectoderm during neurulation giving rise to a variety of cell lineages such as neurons, glia and pigment cells. Most genes associated with the correct initiation, differentiation and migration of the neural crest have been found through reverse genetics. Similarities between neural crest development and some features of cancer progression are remarkable. For instance, it has been suggested that some cancer types recapitulate NC processes in an unregulated manner such as epithelial-mesenchymal transition or active cell migration throughout the body to form distant metastases. However, to date very little is known about initiators and drivers that direct neural crest cell migration to specific target sites. The Medaka mutant hirame represents an interesting melanocyte specific migration defect on the yolk sac caused by a loss of functional Yes-associated protein (YAP). Medaka hirame mutants were initially studied for their profound changes in body morphology. Genomic mapping identified the causal mutation as a nonsense point mutation within the first WW domain in the Yes-associated protein 1 (YAP1), causing translation of a dysfunctional YAP protein. YAP is a downstream transcriptional co-activator of the recently discovered and evolutionarily conserved Hippo pathway. Alterations within Hippo signalling are linked to cell survival, proliferation and abnormal tissue overgrowth. We demonstrate that hirame melanocyte precursors (melanoblasts) are initially present in normal abundance, but show an early migration defect with a lack of melanoblasts on the yolk sac, and corresponding accumulation in the lateral parts of the body. Subsequently, we observe an overall decline in differentiated melanocyte numbers during late stage embryogenesis. We designed an overexpression cassette linking enhanced GFP to either wild type or a mutated activated version of YAP and present evidence that it can efficiently rescue the melanocyte defect after injection of mRNA into one-cell stage embryos. Furthermore, analysis of the yolk sac anatomy via transmission electron microscopy indicates that a fraction of yolk membrane cells undergo apoptosis and we propose that this may contribute to the establishment of altered environmental cues leading to abnormal melanoblast migration onto the yolk sac. Injection of yap mRNA directly into the yolk sac however, failed to rescue melanoblast patterning. To advance our study, we isolated and characterised a 3.6 kb Medaka dopachrome tautomerase (Dct) promoter fragment, and used it to drive expression of enhanced green fluorescent protein (eGFP) in vivo. We generated germline transgenics with this construct that showed lineage-specific expression of eGFP within early migrating melanoblasts, a phenotype that is maintained in differentiated melanocytes throughout embryogenesis. In addition, using this promoter we overexpressed our egfp-yap fusion cassette and established transgenic lines to assess the cell autonomy of YAP within the melanocyte lineage. However, no fluorescent signal could be detected in the latter transgenics, necessitating future experimentation to properly characterise these lines. Finally, we analysed a range of neural crest markers to examine the extent of the neural crest defects in hirame mutants. In addition to the melanocyte phenotype, we identified a dramatic reduction in xanthophore numbers, although early leucophore development appears unaffected. We also observed a decreased number of dorsal root ganglia in the peripheral nervous system as well as smaller and partly ectopic cranial neural crest ganglia populations within the epibranchial arches. The characterisation of a novel Medaka melanocyte specific promoter as well as additional novel NC markers will be widely applicable and useful to the wider Medaka research community as a tool for the study of neural crest related mechanisms during development.
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Xu, Zhi. "Yes associated protein (YAP) in hepatocellular carcinoma oncogenic functions and molecular targeting /." Click to view the E-thesis via HKUTO, 2009. http://sunzi.lib.hku.hk/hkuto/record/B43278589.

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Granger, Paulnisha Davida. "Abundance and Localization of (Yes-associated protein) YAP in Prepubertal Bovine Mammary Tissue." Thesis, Virginia Tech, 2018. http://hdl.handle.net/10919/96240.

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Most mammary development is postnatal. Mammary growth that occurs before puberty is diminutive in amount but consequential for future milk production, especially in dairy heifers. With advanced knowledge on fundamental aspects that govern prepubertal mammary development, scientists and farmers alike can ensure that heifers perform their best once they become cows. The Hippo pathway has been identified as an evolutionarily conserved pathway that regulates organ size in many animal species; it might contribute to mammary growth in dairy heifers. This pathway is mediated by yes-associated protein (YAP) and through downstream gene transcription activation, results in cell proliferation. Because YAP has never been identified in bovine mammary tissue, questions examined in this body of work mainly focused on the abundance and localization of YAP in mammary tissue of prepubertal heifers. The first trial investigated effects of in vivo estradiol administration on YAP abundance and localization in prepubertal bovine mammary epithelial and myoepithelial cells. While YAP was present in nuclei and cytoplasm of both cell types, it was also discovered that estrogen did not influence YAP abundance or location. The second research trial focused on determining the effects of in vivo estradiol blockade on YAP abundance and localization in prepubertal bovine mammary epithelial and myoepithelial cells. Similar to the first experiment, results indicate that YAP abundance and localization was not influenced by estrogen blockade. Despite not being responsive to in vivo estradiol administration (experiment 1) or estradiol blockade (experiment 2) under the conditions of our experiments, YAP was present in nearly all mammary epithelial cells and myoepithelial cells of the 21 total prepubertal heifers examined. Its presence hints at an underlying biological function but that function was not ascertained here. It will be up to the next researcher to deduce what YAP contributes to mammary growth in prepubertal dairy heifers.
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Grant, Edwin Arthur. "Immuno-Labeling of Yes-associated Protein in the Crystalline Lens." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1460499774.

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Derwiysh, Alaa [Verfasser]. "Yes-associated protein (YAP) expression and its biological role in thyroid gland / Alaa Derwiysh." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2013. http://d-nb.info/1031100024/34.

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Judson, Robert Neil. "The role of Yes-associated protein (YAP) in skeletal muscle satellite cells and myofibres." Thesis, University of Aberdeen, 2012. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=189444.

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In spite of its post mitotic nature, skeletal muscle maintains remarkable plasticity. Muscle fibres (myofibres) are capable of large alterations in their size as well as an enormous ability to regenerate following injury – thanks to a potent population of resident stem cells (satellite cells). Deciphering the molecular signalling networks responsible for skeletal muscle growth and regeneration is of key scientific interest – not least because of the therapeutic potential these pathways may hold for the treatment of diseases such as muscular dystrophy. In this thesis, the transcriptional co-factor Yes-Associated protein (Yap), the downstream effector of the Hippo Pathway, was investigated in skeletal muscle. Using gain and loss of function approaches within in vitro, ex vivo and in vivo models, the contribution of Yap in regulating both satellite cell behaviour and myofibre growth was investigated. Yap expression and activity are dynamically regulated during satellite cell activation, proliferation and differentiation ex vivo. Overexpression of Yap increased satellite cell proliferation and maintained cells in a ‘naive’, ‘activated’ state by inhibiting myogenic commitment. Knock-down of Yap impaired satellite cell expansion, but did not influence myogenic differentiation. Yap interacts with Tead transcription factors in myoblasts to upregulate genes such as CyclinD1 and Myf5. Forced expression of Yap eventually led to the oncogenic transformation of myoblasts in vitro. Contrary to predictions, constitutive expression of Yap under an inducible muscle-specific promoter in adult mice failed to induce growth and instead led to muscle wasting, atrophy and degeneration – providing evidence against the notion that Yap represents a universal regulator of tissue growth. These data provide the first insight into the function of Yap in skeletal muscle. Results highlight a novel role for Yap in regulating myogenic progression in satellite cells, as well as its propensity to induce oncogenic transformation. The precise function of Yap in adult myofibres remains unclear however, data presented here demonstrates clear cell-type specific roles for Yap compared to observations made in other tissues.
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Book chapters on the topic "Yes-associated protein 1 (YAP)"

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Nazir, Aqsa, Muhammad Aqib, and Muhammad Usman. "Liver Cancer-Genesis, Progression and Metastasis." In Liver Cancer - Genesis, Progression and Metastasis [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.106020.

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Liver cancer or hepatocellular carcinoma (HCC) is a malignant tumor in liver tissue and worldwide it is fourth leading death cause among all cancers. The most common causes of liver cancer are hepatitis B or C virus infections, alcoholic liver disease (ALD), nonalcoholic fatty liver disease (NAFLD) to non-alcoholic steatohepatitis (NASH), smoking and obesity. The development and metastasis of liver cancer is a multistage and branched process of morphological and genetic traits. Various corresponding signaling pathways such as Yes-Associated Protein-Hippo Pathway (YAP-HIPPO), Wnt/β-catenin and inflammation by interleukin-6 (IL-6), tumor necrosis factor (TNF), nuclear factor-Κb (NF-κB), biological pathways including epithelial–mesenchymal transition (EMT), tumor microenvironment, tumor-stromal interactions and cancer stem cells and gut microbial dysbiosis are allied to both origination, progression and metastasis of liver cancer. Numerous therapeutic approaches are classified into different categories such as pharmacological therapy including sorafenib, lenvatinib and ramuciruma, surgery of HCC patients includes surgical resection, adjuvant therapy after surgical resection and liver transplantation. Loco-regional ablative therapy includes cryotherapy, ethanol injection and radiofrequency ablation, cytotoxic chemotherapy, natural compounds such as piperine, as curcumin and oleocanthal, oncolytic virus therapy, immunotherapies and nanotechnology.
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Conference papers on the topic "Yes-associated protein 1 (YAP)"

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Lv, Xiangmin, Chunbo He, Guohua Hua, Jixin Dong, John S. Davis, and Cheng Wang. "Abstract A37: Yes-associated protein 1 (YAP) in the growth and tumorigenesis of ovarian granulosa cells." In Abstracts: AACR Special Conference: Advances in Ovarian Cancer Research: Exploiting Vulnerabilities; October 17-20, 2015; Orlando, FL. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1557-3265.ovca15-a37.

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Hsu, Jessie Hao-Ru, Long Hung, and Elizabeth R. Lawlor. "Abstract 5169: The polycomb group protein BMI-1 cooperates with Yes-Associated Protein, YAP, to suppress cell contact inhibition in Ewing sarcoma cells." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5169.

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Kovacs, Szonja A., Tamás Kovács, András Lánczky, Ágnes Paál, Zsombor Hegedűs, Sayour Viktor Nabil, Lilla Szabó, et al. "5 Investigation of yes-associated protein 1 (YAP1) as a biomarker of anti-PD-1 resistance in melanoma." In SITC 39th Annual Meeting (SITC 2024) Abstracts, A8. BMJ Publishing Group Ltd, 2024. http://dx.doi.org/10.1136/jitc-2024-sitc2024.0005.

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Yin, Xue, Jun Liu, Naoki Akanuma, Michael Nipper, and Pei Wang. "Abstract 4075: Role of yes-associated protein 1 (YAP1) in human pancreatic ductal adenocarcinoma initiation and progression." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4075.

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Diep, Caroline H., Kelly Zucker, Aprill Watanabe, Galen Hostetter, Ruben Munoz, Daniel D. Von Hoff, and Haiyong Han. "Abstract B170: Downregulation of Yes‐associated protein 1 (YAP1) expression reduces cell proliferation and clonogenicity of pancreatic cancer cells." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-b170.

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Palanivel, Chitra, Bailey Gabler, Ying Yan, Surinder K. Batra, and Michel M. Ouellette. "Abstract 4366: The small GTPase Rac1 controls the stability of the Yes-associated protein 1 (YAP1) independently of the LATS1/2 kinases and SCF-βTRCP ubiquitin ligase." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4366.

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Lee, Seong Eun, Jung Uee Lee, Min Hee Lee, Min Jeong Ryu, Soung Joong Kim, Yong Kyung Kim, Koon Soon Kim, Min Jeong Choi, Young Suk Jo, and Minho Shong. "Abstract B149: Yes-associated protein (YAP) is associated with aggressive characteristics of BRAFV600E thyroid cancer." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-b149.

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Odackal, J., H. Roybal, K. Correll, D. W. H. Riches, J. P. Bridges, Y. Aschner, M. Koenigshoff, and G. P. Downey. "Yes-Associated Protein (YAP) Is Critical in Epithelial Repair After Acute Lung Injury." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a4368.

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Alptekin, Ahmet, Gamze Kuser Abali, Qiang Wang, and Bekir Cinar. "Abstract 759: Regulation of androgenic signaling by yes-associated protein, YAP, in prostate cancer cells." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-759.

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Thiess, L., N. Mwewa, P. Schirmacher, and K. Breuhahn. "The desmosomal cadherin desmoglein-2 regulates the Hippo pathway effector yes-associated protein (YAP) in liver cancer." In 36. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0039-3402211.

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Reports on the topic "Yes-associated protein 1 (YAP)"

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Sadot, Einat, Christopher Staiger, and Zvi Kam Weizmann. functional genomic screen for new plant cytoskeletal proteins and the determination of their role in actin mediated functions and guard cells regulation. United States Department of Agriculture, January 2003. http://dx.doi.org/10.32747/2003.7587725.bard.

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The original objectives of the approved proposal were: 1. To construct a YFP fused Arabidopsis cDNA library in a mammalian expression vector. 2. To infect the library into a host fibroblast cell line and to screen for new cytoskeletal associated proteins using an automated microscope. 3. Isolate the new genes. 4. Characterize their role in plants. The project was approved as a feasibility study to allow proof of concept that would entail building the YFP library and picking up a couple of positive clones using the fluorescent screen. We report here on the construction of the YFP library, the development of the automatic microscope, the establishment of the screen and the isolation of positive clones that are plant cDNAs encoding cytoskeleton associated proteins. The rational underling a screen of plant library in fibroblasts is based on the high conservation of the cytoskeleton building blocks, actin and tubulin, between the two kingdoms (80-90% homology at the level of amino acids sequence). In addition, several publications demonstrated the recognition of mammalian cytoskeleton by plant cytoskeletal binding proteins and vice versa. The major achievements described here are: 1. The development of an automated microscope equipped with fast laser auto-focusing for high magnification and a software controlling 6 dimensions; X, Y position, auto focus, time, color, and the distribution and density of the fields acquired. This system is essential for the high throughput screen. 2. The construction of an extremely competent YFP library efficiently cloned (tens of thousands of clones collected, no empty vectors detected) with all inserts oriented 5't03'. These parameters render it well representative of the whole transcriptome and efficient in "in-frame" fusion to YFP. 3. The strategy developed for the screen allowing the isolation of individual positive cDNA clones following three rounds of microscopic scans. The major conclusion accomplished from the work described here is that the concept of using mammalian host cells for fishing new plant cytoskeletal proteins is feasible and that screening system developed is complete for addressing one of the major bottlenecks of the plant cytoskeleton field: the need for high throughput identification of functionally active cytoskeletal proteins. The new identified plant cytoskeletal proteins isolated in the pilot screen and additional new proteins which will be isolated in a comprehensive screen will shed light on cytoskeletal mediated processes playing a major role in cellular activities such as cell division, morphogenesis, and functioning such as chloroplast positioning, pollen tube and root hair elongation and the movement of guard cells. Therefore, in the long run the screen described here has clear agricultural implications.
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Epel, Bernard, and Roger Beachy. Mechanisms of intra- and intercellular targeting and movement of tobacco mosaic virus. United States Department of Agriculture, November 2005. http://dx.doi.org/10.32747/2005.7695874.bard.

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To cause disease, plant viruses must replicate and spread locally and systemically within the host. Cell-to-cell virus spread is mediated by virus-encoded movement proteins (MPs), which modify the structure and function of plasmodesmata (Pd), trans-wall co-axial membranous tunnels that interconnect the cytoplasm of neighboring cells. Tobacco mosaic virus (TMV) employ a single MP for cell- cell spread and for which CP is not required. The PIs, Beachy (USA) and Epel (Israel) and co-workers, developed new tools and approaches for study of the mechanism of spread of TMV that lead to a partial identification and molecular characterization of the cellular machinery involved in the trafficking process. Original research objectives: Based on our data and those of others, we proposed a working model of plant viral spread. Our model stated that MPᵀᴹⱽ, an integral ER membrane protein with its C-terminus exposed to the cytoplasm (Reichel and Beachy, 1998), alters the Pd SEL, causes the Pd cytoplasmic annulus to dilate (Wolf et al., 1989), allowing ER to glide through Pd and that this gliding is cytoskeleton mediated. The model claimed that in absence of MP, the ER in Pd (the desmotubule) is stationary, i.e. does not move through the Pd. Based on this model we designed a series of experiments to test the following questions: -Does MP potentiate ER movement through the Pd? - In the presence of MP, is there communication between adjacent cells via ER lumen? -Does MP potentiate the movement of cytoskeletal elements cell to cell? -Is MP required for cell-to-cell movement of ER membranes between cells in sink tissue? -Is the binding in situ of MP to RNA specific to vRNA sequences or is it nonspecific as measured in vitro? And if specific: -What sequences of RNA are involved in binding to MP? And finally, what host proteins are associated with MP during intracellular targeting to various subcellular targets and what if any post-translational modifications occur to MP, other than phosphorylation (Kawakami et al., 1999)? Major conclusions, solutions and achievements. A new quantitative tool was developed to measure the "coefficient of conductivity" of Pd to cytoplasmic soluble proteins. Employing this tool, we measured changes in Pd conductivity in epidermal cells of sink and source leaves of wild-type and transgenic Nicotiana benthamiana (N. benthamiana) plants expressing MPᵀᴹⱽ incubated both in dark and light and at 16 and 25 ᵒC (Liarzi and Epel, 2005 (appendix 1). To test our model we measured the effect of the presence of MP on cell-to-cell spread of a cytoplasmic fluorescent probe, of two ER intrinsic membrane protein-probes and two ER lumen protein-probes fused to GFP. The effect of a mutant virus that is incapable of cell-to-cell spread on the spread of these probes was also determined. Our data shows that MP reduces SEL for cytoplasmic molecules, dilates the desmotubule allowing cell-cell diffusion of proteins via the desmotubule lumen and reduces the rate of spread of the ER membrane probes. Replicase was shown to enhance cell-cell spread. The data are not in support of the proposed model and have led us to propose a new model for virus cell-cell spread: this model proposes that MP, an integral ER membrane protein, forms a MP:vRNAER complex and that this ER-membrane complex diffuses in the lipid milieu of the ER into the desmotubule (the ER within the Pd), and spreads cell to cell by simple diffusion in the ER/desmotubule membrane; the driving force for spread is the chemical potential gradient between an infected cell and contingent non-infected neighbors. Our data also suggests that the virus replicase has a function in altering the Pd conductivity. Transgenic plant lines that express the MP gene of the Cg tobamovirus fused to YFP under the control the ecdysone receptor and methoxyfenocide ligand were generated by the Beachy group and the expression pattern and the timing and targeting patterns were determined. A vector expressing this MPs was also developed for use by the Epel lab . The transgenic lines are being used to identify and isolate host genes that are required for cell-to-cell movement of TMV/tobamoviruses. This line is now being grown and to be employed in proteomic studies which will commence November 2005. T-DNA insertion mutagenesis is being developed to identify and isolate host genes required for cell-to-cell movement of TMV.
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