Relevant bibliographies by topics / AMOT Proteins

Academic literature on the topic 'AMOT Proteins'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "AMOT Proteins"

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Ernkvist, Mira, Nathalie Luna Persson, Stéphane Audebert, Patrick Lecine, Indranil Sinha, Miaoliang Liu, Marc Schlueter, et al. "The Amot/Patj/Syx signaling complex spatially controls RhoA GTPase activity in migrating endothelial cells." Blood 113, no. 1 (January 1, 2009): 244–53. http://dx.doi.org/10.1182/blood-2008-04-153874.

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Abstract Controlled regulation of Rho GTPase activity is an essential component mediating growth factor–stimulated migration. We have previously shown that angiomotin (Amot), a membrane-associated scaffold protein, plays a critical role during vascular patterning and endothelial migration during embryogenesis. However, the signaling pathways by which Amot controls directional migration are not known. Here we have used peptide pull-down and yeast 2-hybrid (Y2H) screening to identify proteins that interact with the C-terminal PDZ-binding motifs of Amot and its related proteins AmotL1 and 2. We report that Amot and its related proteins bind to the RhoA GTPase exchange factor (RhoGEF) protein Syx. We show that Amot forms a ternary complex together with Patj (or its paralogue Mupp1) and Syx. Using FRET analysis, we provide evidence that Amot controls targeting of RhoA activity to lamellipodia in vitro. We also report that, similar to Amot, morpholino knockdown of Syx in zebrafish results in inhibition of migration of intersegmental arteries. Taken together, our results indicate that the directional migration of capillaries in the embryo is governed by the Amot:Patj/Mupp1:Syx signaling that controls local GTPase activity.
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Cox, Christopher M., Edward K. Mandell, Lorraine Stewart, Ruifeng Lu, Debra L. Johnson, Sarah D. McCarter, Andre Tavares, Ray Runyan, Sourav Ghosh, and Jean M. Wilson. "Endosomal regulation of contact inhibition through the AMOT:YAP pathway." Molecular Biology of the Cell 26, no. 14 (July 5, 2015): 2673–84. http://dx.doi.org/10.1091/mbc.e15-04-0224.

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Contact-mediated inhibition of cell proliferation is an essential part of organ growth control; the transcription coactivator Yes-associated protein (YAP) plays a pivotal role in this process. In addition to phosphorylation-dependent regulation of YAP, the integral membrane protein angiomotin (AMOT) and AMOT family members control YAP through direct binding. Here we report that regulation of YAP activity occurs at the endosomal membrane through a dynamic interaction of AMOT with an endosomal integral membrane protein, endotubin (EDTB). EDTB interacts with both AMOT and occludin and preferentially associates with occludin in confluent cells but with AMOT family members in subconfluent cells. EDTB competes with YAP for binding to AMOT proteins in subconfluent cells. Overexpression of the cytoplasmic domain or full-length EDTB induces translocation of YAP to the nucleus, an overgrowth phenotype, and growth in soft agar. This increase in proliferation is dependent upon YAP activity and is complemented by overexpression of p130-AMOT. Furthermore, overexpression of EDTB inhibits the AMOT:YAP interaction. EDTB and AMOT have a greater association in subconfluent cells compared with confluent cells, and this association is regulated at the endosomal membrane. These data provide a link between the trafficking of tight junction proteins through endosomes and contact-inhibition-regulated cell growth.
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Wang, Chenji, Jian An, Pingzhao Zhang, Chen Xu, Kun Gao, Di Wu, Dejie Wang, Hongxiu Yu, Jun O. Liu, and Long Yu. "The Nedd4-like ubiquitin E3 ligases target angiomotin/p130 to ubiquitin-dependent degradation." Biochemical Journal 444, no. 2 (May 11, 2012): 279–89. http://dx.doi.org/10.1042/bj20111983.

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AMOT (angiomotin) is a membrane-associated protein that is expressed in ECs (endothelial cells) and controls migration, TJ (tight junction) formation, cell polarity and angiogenesis. Recent studies have revealed that AMOT and two AMOT-like proteins, AMOTL1 and AMOTL2, play critical roles in the Hippo pathway by regulating the subcellular localization of the co-activators YAP (Yes-associated protein) and TAZ (transcriptional co-activator with PDZ-binding motif). However, it has been unclear how AMOT is regulated. In the present study, we report that AMOT undergoes proteasomal degradation. We identify three members of Nedd4 (neural-precursor-cell-expressed developmentally down-regulated)-like ubiquitin E3 ligases, Nedd4, Nedd4-2 and Itch, as the ubiquitin E3 ligases for the long isoform of AMOT, AMOT/p130. We demonstrate that Nedd4, Nedd4-2 and Itch mediate poly-ubiquitination of AMOT/p130 in vivo. Overexpression of Nedd4, Nedd4-2 or Itch leads to AMOT/p130 proteasomal degradation. Knockdown of Nedd4, Nedd4-2 and Itch causes an accumulation of steady-state level of AMOT/p130. We also show that three L/P-PXY motifs of AMOT/p130 and the WW domains of Nedd4 mediate their interaction. Furthermore, Nedd4-like ubiquitin E3 ligases might compete with YAP for the binding to AMOT/p130, and subsequently targeting AMOT/p130 for ubiquitin-dependent degradation. Together, these observations reveal a novel post-translational regulatory mechanism of AMOT/p130.
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Han, Ziying, Gordon Ruthel, Shantoshini Dash, Corbett T. Berry, Bruce D. Freedman, Ronald N. Harty, and Olena Shtanko. "Angiomotin regulates budding and spread of Ebola virus." Journal of Biological Chemistry 295, no. 25 (May 7, 2020): 8596–601. http://dx.doi.org/10.1074/jbc.ac120.013171.

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The Ebola virus (EBOV) VP40 matrix protein (eVP40) orchestrates assembly and budding of virions in part by hijacking select WW-domain–bearing host proteins via its PPxY late (L)-domain motif. Angiomotin (Amot) is a multifunctional PPxY-containing adaptor protein that regulates angiogenesis, actin dynamics, and cell migration/motility. Amot also regulates the Hippo signaling pathway via interactions with the WW-domain–containing Hippo effector protein Yes-associated protein (YAP). In this report, we demonstrate that endogenous Amot is crucial for positively regulating egress of eVP40 virus-like particles (VLPs) and for egress and spread of authentic EBOV. Mechanistically, we show that ectopic YAP expression inhibits eVP40 VLP egress and that Amot co-expression rescues budding of eVP40 VLPs in a dose-dependent and PPxY-dependent manner. Moreover, results obtained with confocal and total internal reflection fluorescence microscopy suggested that Amot's role in actin organization and dynamics also contributes to promoting eVP40-mediated egress. In summary, these findings reveal a functional and competitive interplay between virus and host proteins involving the multifunctional PPxY-containing adaptor Amot, which regulates both the Hippo pathway and actin dynamics. We propose that our results have wide-ranging implications for understanding the biology and pathology of EBOV infections.
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Shen, Pengfei, Hao Zeng, Angelica Ortiz, Chien-Jui Cheng, Yu-Chen Lee, Guoyu Yu, Song-Chang Lin, Li-Yuan Yu-Lee, and Sue-Hwa Lin. "Angiomotin to regulate prostate cancer cell proliferation by signaling through Hippo-YAP pathway." Journal of Clinical Oncology 35, no. 6_suppl (February 20, 2017): e559-e559. http://dx.doi.org/10.1200/jco.2017.35.6_suppl.e559.

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e559 Background: Angiomotin (AMOT) is a family of proteins found to be a component of the apical junctional complex of vertebrate epithelial cells and is recently found to play important roles in neurofibromatosis type 2 (NF-2). Whether AMOT plays a role in prostate cancer (PCa) is unknown. Methods: Purified GST-AMOTp80 was used as immunogen for antibody generation. Real-time PCR, western blot and immunohistochemistry were used to identify the expression of AMOT. To study the function of AMOT, retroviral vector were constructed, also shRNA was used to knockdown AMOT in cells. Cell migration and invasion assays were performed by using transwell chambers. Nuclear and cytoplasmic protein fractions were prepared by using NE-PER reagents (Pierce). The SPSS 19.0 software was used for statistical analysis. Chi-square test and t test were used for the comparisons between groups. Results: AMOT is expressed as two isoforms, AMOTp80 and AMOTp130, which has a 409 aa N-terminal domain that is absent in AMOTp80. Both AMOTp80 and AMOTp130 are expressed in LNCaP and C4-2B4, but at a low to undetectable level in PC3 cells. Further study showed that AMOTp130 and AMOTp80 have distinct functions in PCa cells. We found that AMOTp80 functioned as a tumor promoter by enhancing PCa cell proliferation while AMOTp130 did not. Mechanistic studies showed that AMOTp80 signaled through the Hippo pathway by promoting the nuclear translocation of YAP, resulting in an increased expression of YAP target protein BMP4. Moreover, inhibition of BMP receptor activity by LDN-193189 abrogates AMOTp80-mediated cell proliferation. Conclusions: Together, this study reveals a novel mechanism whereby the AMOTp80-Merlin-MST1-LATS-YAP-BMP4 pathway leads to AMOTp80-induced tumor cell proliferation.
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Wigerius, Michael, Dylan Quinn, and James P. Fawcett. "Emerging roles for angiomotin in the nervous system." Science Signaling 13, no. 655 (October 27, 2020): eabc0635. http://dx.doi.org/10.1126/scisignal.abc0635.

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Angiomotins are a family of molecular scaffolding proteins that function to organize contact points (called tight junctions in vertebrates) between adjacent cells. Some angiomotin isoforms bind to the actin cytoskeleton and are part of signaling pathways that influence cell morphology and migration. Others cooperate with components of the Hippo signaling pathway and the associated networks to control organ growth. The 130-kDa isoform, AMOT-p130, has critical roles in neural stem cell differentiation, dendritic patterning, and synaptic maturation—attributes that are essential for normal brain development and are consistent with its association with autism. Here, we review and discuss the evidence that supports a role for AMOT-p130 in neuronal development in the central nervous system.
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Peck, Cameron James, Piia Virtanen, Derrick Johnson, and Ann Kimble-Hill. "Using the Predicted Structure of the Amot Coiled Coil Homology Domain to Understand Lipid Binding." IU Journal of Undergraduate Research 4, no. 1 (December 16, 2018): 27–46. http://dx.doi.org/10.14434/iujur.v4i1.24528.

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Angiomotins (Amots) are a family of adapter proteins that modulate cellular polarity, differentiation, proliferation, and migration. Amot family members also have a characteristic lipid-binding domain, the coiled coil homology (ACCH) domain that selectively targets the protein to membranes, which has been directly linked to its regulatory role in the cell. Several spot blot assays were used to validate the regions of the domain that participate in its membrane association, deformation, and vesicle fusion activity, which suggested the need for a structure to define the mechanism. Therefore, we endeavored to understand the structure-function relationship of this domain with the desire to find ways to modulate these signaling pathways. After many failed attempts to crystallize the ACCH domain of each of the Amot family members for structural analysis, we decided to pursue homologous models that could be refined using small angle x-ray scattering data. Theoretical models were produced using the homology software SWISS-MODEL and threading software I-TASSER and LOMETS, followed by comparison to SAXS data for model selection and refinement. As a result, we present a theoretical model of the domain that is driven by alpha helices and short random coil regions. These alpha helical regions form a classic dimer interface followed by two wide spread legs that we predict to be the lipid binding interface.
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de Oliveira, Nathalia Barth, Ana Carolina Irioda, Priscila Elias Ferreira Stricker, Bassam Felipe Mogharbel, Nádia Nascimento da Rosa, Dilcele Silva Moreira Dziedzic, and Katherine Athayde Teixeira de Carvalho. "Natural Membrane Differentiates Human Adipose-Derived Mesenchymal Stem Cells to Neurospheres by Mechanotransduction Related to YAP and AMOT Proteins." Membranes 11, no. 9 (September 5, 2021): 687. http://dx.doi.org/10.3390/membranes11090687.

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Adipose tissue-derived mesenchymal stem cells (ADMSCs) are promising candidates for regenerative medicine, as they have good cell yield and can differentiate into several cell lines. When induced to the neuronal differentiation, they form neurospheres composed of neural precursors (NPs) that can be an alternative in treating neurodegenerative diseases. This study aimed to characterize NPs from neurospheres obtained after seeding ADMSCs on a natural polyisoprene-based membrane. The ADMSCs were isolated from adipose tissue by enzymatic dissociation, were subjected to trilineage differentiation, and were characterized by flow cytometry for specific ADMSC surface markers. For neuronal differentiation, the cells were seeded on polystyrene flasks coated with the membrane and were characterized by immunocytochemistry and RT-PCR. The results demonstrated that the isolated cells showed characteristics of ADMSCs. At 15 to 25 days, ADMSCs seeded on the natural membrane developed neurospheres. Then, after dissociation, the cells demonstrated characteristic neuronal markers expressed on NPs: nestin, ß-III tubulin, GFAP, NeuN, and the YAP1/AMOT in the cytoplasm. In conclusion, it was demonstrated that this membrane differentiates the ADMSCs to NPs without any induction factors, and suggests that their differentiation mechanisms are related to mechanotransduction regulated by the YAP and AMOT proteins.
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Wells, Clark D., James P. Fawcett, Andreas Traweger, Yojiro Yamanaka, Marilyn Goudreault, Kelly Elder, Sarang Kulkarni, et al. "A Rich1/Amot Complex Regulates the Cdc42 GTPase and Apical-Polarity Proteins in Epithelial Cells." Cell 125, no. 3 (May 2006): 535–48. http://dx.doi.org/10.1016/j.cell.2006.02.045.

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Paramasivam, Murugan, Ali Sarkeshik, John R. Yates, Maria J. G. Fernandes, and Dannel McCollum. "Angiomotin family proteins are novel activators of the LATS2 kinase tumor suppressor." Molecular Biology of the Cell 22, no. 19 (October 2011): 3725–33. http://dx.doi.org/10.1091/mbc.e11-04-0300.

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LATS2 kinase functions as part of the Hippo pathway to promote contact inhibition of growth and tumor suppression by phosphorylating and inhibiting the transcriptional coactivator YAP. LATS2 is activated by the MST2 kinase. How LATS2 is activated by MST2 in response to changes in cell density is unknown. Here we identify the angiomotin-family tight junction protein AMOTL2 as a novel activator of LATS2. Like AMOTL2, the other angiomotin-family proteins AMOT and AMOTL1 also activate LATS2 through a novel conserved domain that binds and activates LATS2. AMOTL2 binds MST2, LATS2, and YAP, suggesting that AMOTL2 might serve as a scaffold protein. We show that LATS2, AMOTL2, and YAP all localize to tight junctions, raising the possibility that clustering of Hippo pathway components at tight junctions might function to trigger LATS2 activation and growth inhibition in response to increased cell density.
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Dissertations / Theses on the topic "AMOT Proteins"

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Kumar, Amit [Verfasser], Stefan H. [Gutachter] Heinemann, Helmut [Gutachter] Pospiech, and Roberto [Gutachter] Fattorussa. "Structural investigations on heme-interacting proteins / Amit Kumar ; Gutachter: Stefan H. Heinemann, Helmut Pospiech, Roberto Fattorussa." Jena : Friedrich-Schiller-Universität Jena, 2019. http://d-nb.info/1207272841/34.

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Boeckstaens, Mélanie. "Les transporteurs d'ammonium Mep/Amt/Rh de la levure Saccharomyces cerevisiae: fonctions et régulations." Doctoral thesis, Universite Libre de Bruxelles, 2007. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/210669.

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Les protéines de la famille Mep/Amt/Rh sont largement conservées dans l’évolution. Cette famille comprend les facteurs Rhésus dont les antigènes Rh humains sont les membres les plus notoires. Le rôle des protéines de type Mep/Amt/Rh en tant que transporteurs d’ammonium a largement été décrit chez les bactéries, les champignons et les plantes. Néanmoins, leur mécanisme de fonctionnement demeure élusif et la régulation de leur activité a été peu abordée chez les organismes eucaryotes. En utilisant comme modèles de la famille Mep/Amt/Rh les trois transporteurs d’ammonium de la levure Saccharomyces cerevisiae, nous avons tenté de comprendre les mécanismes de fonctionnement et de régulation de cette famille de protéines membranaires.

Nous montrons qu’un résidu aspartate, conservé dans la famille Mep/Amt/Rh et situé à proximité d’un vestibule cation-attractif, joue un rôle structural dans la reconnaissance de l’ammonium chez le transporteur Mep2. De plus, un résidu histidine très conservé dans le pore hydrophobe des protéines Mep/Amt/Rh est substitué par un aspartate chez un sous-groupe de transporteurs d’ammonium fongiques. Cette substitution permet de définir deux sous-familles fonctionnelles possédant des propriétés bien distinctes.

Nous montrons également que la kinase Npr1 intervient dans la modulation de l’activité intrinsèque des trois protéines Mep qui demeurent inactives mais stables à la membrane plasmique en absence de la kinase.

Hormis leur rôle dans le transport d’ammonium en tant que source d’azote, nous montrons que l’activité des protéines Mep est requise pour différentes réponses physiologiques. Une diminution d’entrée d’ammonium en absence des protéines Mep ou de leur régulateur positif Npr1 entraîne une dérépression des gènes soumis à la répression catabolique azotée ainsi qu’un défaut dans le repompage de l’ammonium catabolique excrété durant la croissance en présence d’autres sources azotées. Un rôle supplémentaire de senseur d’ammonium avait été attribué au transporteur Mep2 dans l’induction de la croissance filamenteuse en réponse à une limitation en ammonium. Nous montrons que l’état d’activité de la protéine Mep2 est étroitement lié à sa capacité à induire le développement filamenteux.
Doctorat en Sciences
info:eu-repo/semantics/nonPublished

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Soto, Diaz Silvia. "Structure, function and regulation of ammonium transport proteins of the Mep-Amt-Rh superfamily in the yeast Saccharomyces cerevisiae." Doctoral thesis, Universite Libre de Bruxelles, 2020. https://dipot.ulb.ac.be/dspace/bitstream/2013/313552/4/TABLE.pdf.

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While ammonium is an excellent nitrogen source for microorganisms and plants, it is known as acytotoxic metabolite and for its critical role in acid/base homeostasis in animals. Ammonium transportinside the cells is ensured by proteins of the Mep-Amt-Rh superfamily, which are conserved frombacteria to humans.The main objective of the thesis is to refine the understanding of the regulation of the three ammoniumtransport proteins Mep1, Mep2 and Mep3 from Saccharomyces cerevisiae. The three Mep proteins areregulated by the Npr1 kinase and the conserved TORC1 signaling pathway. While the activity of Mep2is regulated by phosphorylation of the C-terminal 457 serine, the activity of Mep1 and Mep3 is inhibitedby the factor Amu1 / Par32. In the presence of a poor nitrogen source, Npr1 induces phosphorylation ofAmu1 which appears mainly cytosolic and, Mep1 and Mep3 are active. On the other hand, in thepresence of a good nitrogen source, the activity of TORC1 induces the inhibition of Npr1 and thereforethe dephosphorylation of Amu1 which accumulates at the cell surface and inactivates Mep1 and Mep3.In order to further study the regulation of Mep1 / 3, a genetic screen was performed to isolate suppressorsrecovering Mep1-dependent ammonium transport in the absence of Npr1. Several mutations, insertionsand deletions have been identified in the MEP1 and AMU1 genes allowing Mep1 to be activeindependently of Npr1. This work shows that all the point mutations in Mep1 delimit an area at theinterface between the hydrophobic body of Mep1 and the cytosol, and that part of the C-terminus (CTR)is required for optimal activity of Mep1 but appears dispensable for regulation by Amu1 and Npr1. Thegenetic screen also shows that the last 15 amino acids of Amu1 are required to inactivate Mep1. Finally,the isolation of suppressors showing no mutation in MEP1 and AMU1 could reveal new factors involvedin the control of Mep1.The results indicate that Mep1 is inactivated in the presence of glutamine, a good source of nitrogen,and that this inactivation requires Amu1. The glutamine-dependent inactivation of Mep2 was alsostudied in this manuscript. Mass spectrometry analysis revealed putative phosphorylation sites in CTRspecific to the presence or absence of glutamine.This work also addressed the role of Amu1 in the reactivation function of TORC1 after treatment withrapamycin, in particular by confirming that it requires the function of Mep1/3. The study leads to thehypothesis that the transport mechanism specific to Mep1 and Mep3 and different from Mep2 isinvolved in this function.Finally, in order to better understand the mechanisms of regulation and transport of Mep-Amt-Rhproteins, the experimental determination of the three-dimensional structure of different variants ofMep2, in open or closed conformation, and of Mep1 was undertaken. Throughout this work, thecharacterized Mep1 or Mep2 variants were analyzed in silico by using the available three-dimensionalstructures.
Doctorat en Sciences
info:eu-repo/semantics/nonPublished
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Amor, Houda [Verfasser]. "Impact of Tobacco smoking on sperm nuclear proteins genes : H2BFWT, TNP1, TNP2, PRM1, and PRM2 and its influence on male infertility / Houda Amor." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2019. http://d-nb.info/1233678930/34.

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Čebo, Daniel [Verfasser], and Susana [Akademischer Betreuer] Andrade. "Site-directed mutagenesis as a tool for functional characterization of the Ammonium Transport Protein Amt-1 from Archaeoglobus fulgidus = Ortsspezifische Mutagenese als ein Werkzeug für die funktionelle Charakterisierung des Ammoniumtransportproteins Amt-1 aus Archaeoglobus fulgidus." Freiburg : Universität, 2010. http://d-nb.info/1123458367/34.

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Ranahan, William P. "The oncogenic properties of Amot80 in mammary epithelia." Thesis, 2014. http://hdl.handle.net/1805/4082.

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Indiana University-Purdue University Indianapolis (IUPUI)
While breast cancer is the second most commonly diagnosed cancer worldwide, its causes and natural history are not well defined. The female mammary organ is unique in that it does not reach full maturity until the lactation cycle following pregnancy. This cycle entails extensive growth and reorganization of the primitive epithelial ductal network. Following lactation, these same epithelial cells undergo an equally extensive program of apoptosis and involution. The mammary gland's sensitivity to pro-growth and pro-apoptotic signals may partly explain its proclivity to develop cancers. For epithelial cells to become transformed they must lose intracellular organization known as polarity as differentiated epithelial tissues are refractory to aberrant growth. One essential component of epithelial to mesenchymal transition is the intrinsic capacity of cells to repurpose polarity constituents to promote growth. Recently, a novel mechanism of organ size control has been shown to repurpose the apical junctional associated protein Yap into the nucleus where it functions as a transcriptional coactivator promoting growth and dedifferentiation. The focus of my work has been on a family of adaptor proteins termed Amots that have been shown to scaffold Yap and inhibit growth signaling. Specifically, I have shown that the 80KDa form of Amot, termed Amot80, acts as a dominant negative to the other Amot proteins to promote cell growth while reducing cell differentiation. Amot80 was found to promote the prolonged activation of MAPK signaling. Further, Amot80 expression was also found to enhance the transcriptional activity of Yap. This effect likely underlies the ability of Amot80 to drive disorganized overgrowth of MCF10A cells grown in Matrigel̈™. Overall, these data suggest a mechanism whereby the balance of Amot proteins controls the equilibrium between growth and differentiation within mammary epithelial tissues.
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Tyagi, Amit [Verfasser]. "Photodynamics of a flavin based blue-light regulated phosphodiesterase protein and its photoreceptor BLUF domain / vorgelegt von Amit Tyagi." 2009. http://d-nb.info/994918348/34.

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Book chapters on the topic "AMOT Proteins"

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JÚLIA KAROLINE RODRIGUES DAS, MERCÊS, MEDELO MARIA JOSÉ YÁÑEZ, YANMEI LI, SILVA PAULO HENRIQUE SOARES, and REIS ISAÍAS DOS SANTOS. "PRODUTIVIDADE DA RÚCULA EM FUNÇÃO DE DOSES DE NITROGÊNIO." In PERSPECTIVAS DAS CIÊNCIAS AGRÁRIAS NA SOCIEDADE 5.0: EDUCAÇÃO, CIÊNCIA, TECNOLOGIA E AMOR, 267–73. Instituto Internacional Despertando Vocações, 2020. http://dx.doi.org/10.31692/978-65-88970-07-2.267-273.

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A rúcula (Eruca sativa Miller) é uma das hortaliças folhosas que mais ganhou importância econômica e maior espaço no mercado a partir da década de 90 (PURQUERIO et al., 2007). O sucesso da produção de hortaliças depende de diversos fatores ligados ao manejo da cultura, dentre esses fatores, a fertilização torna-se importante , pois o solo não é capaz de suprir, de forma adequada, as plantas com todos os elementos essenciais para seu desenvolvimento (PRADO, 2008). O fornecimento de N por meio de adubações se faz necessário porque apenas 5% do N no solo encontra-se na forma inorgânico, ou seja, na forma que as plantas conseguem absorver (NH4+ e NO3 -) (BRADY; WEIL, 2013). Após ser absorvido pelas plantas o N participa no processo de produção de proteínas, ácidos nucléicos, enzimas e muitos outros elementos essenciais para o crescimento e desenvolvimento vegetal. A alta demanda por N pela maioria das hortaliças é um dos motivos pelo uso de altas doses de fertilizantes nitrogenados. A adubação com N é essencial para o bom desenvolvimento da rúcula e produtividade, isso porque esta cultura apresenta ciclo curto, com isso demanda grande quantidade do nutriente em curto espaço de tempo (CAVARIANNI et al., 2004). Dada a dinâmica do N e suas interações com o ambiente, o estudo sobre a adubação nitrogenada em plantas de ciclo curto como as hortaliças folhosas torna-se imprescindível para que não ocorra uma aplicação excessiva de N no solo, o que pode levar à contaminação do lençol freático por causa da lixiviação de nitrato, além de perdas de volatilização. Dessa forma, o objetivo do trabalho foi avaliar a produtividade da rúcula submetida a doses de nitrogênio.
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EDILAYANE DA NÓBREGA, SANTOS, FEITOZA JOÃO VITOR FONSECA, FERREIRA VALQUÍRIA CARDOSO DA SILVA, and SILVA FÁBIO ANDERSON PEREIRA DA. "USO DE ANTIOXIDANTES NATURAIS EM CARNES E DERIVADOS: UMA REVISÃO." In PERSPECTIVAS DAS CIÊNCIAS AGRÁRIAS NA SOCIEDADE 5.0: EDUCAÇÃO, CIÊNCIA, TECNOLOGIA E AMOR, 75–88. Instituto Internacional Despertando Vocações, 2020. http://dx.doi.org/10.31692/978-65-88970-07-2.75-88.

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As reações de oxidação lipídica e proteica em carnes e derivados provocam impacto negativo na qualidade do produto, afetando as características nutricionais, sensoriais e tecnológicas, bem como causando efeitos adversos à saúde do consumidor. A indústria alimentícia, na busca de minimizar ou prevenir este problema, faz uso de antioxidantes sintéticos, os quais são efetivos, porém têm sido associados ao aparecimento de doenças carcinogênicas, o que provoca rejeição destes produtos por parte da população atual que buscam por alimentos mais saudáveis. Nesta perspectiva, estudos têm identificado compostos com ação antioxidante em vegetais que apresentam boa efetividade. Neste sentido, diversas pesquisas têm sido desenvolvidas no intuito de avaliar a viabilidade da obtenção de antioxidantes naturais e sua incorporação em carnes e produtos cárneos. Neste trabalho, objetivou-se realizar uma busca exploratória sobre o uso de antioxidantes naturais em carnes e derivados e sua forma de aplicação. As buscas ocorreram no período de fevereiro de 2019 a março de 2020, utilizando bases de dados como Google acadêmico, Science Direct e Scopus para realização da pesquisa, priorizando artigos mais atuais. Constatou-se que há uma busca crescente em relação a aplicação de antioxidantes naturais em carnes e derivados, visando substituir os sintéticos e que estes podem ser aplicados de diversas formas, seja através da alimentação animal, aplicação direta na massa cárnea ou através de sua incorporação em embalagens de alimentos. Desta forma, os dados indicam que a aplicação de antioxidantes naturais em carnes e seus produtos podem ser efetivas contra reações oxidativas, independente de sua forma de aplicação, configurando-se como um estratégia promissora na preservação destes produtos.
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