Relevant bibliographies by topics / PLEKHA1 [Pleckstrin homology domain containing

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Academic literature on the topic 'PLEKHA1 [Pleckstrin homology domain containing'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 February 2022

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Journal articles on the topic "PLEKHA1 [Pleckstrin homology domain containing"

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Rouaud, Florian, Francesca Tessaro, Laura Aimaretti, Leonardo Scapozza, and Sandra Citi. "Cooperative binding of the tandem WW domains of PLEKHA7 to PDZD11 promotes conformation-dependent interaction with tetraspanin 33." Journal of Biological Chemistry 295, no. 28 (May 5, 2020): 9299–312. http://dx.doi.org/10.1074/jbc.ra120.012987.

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Pleckstrin homology domain–containing A7 (PLEKHA7) is a cytoplasmic protein at adherens junctions that has been implicated in hypertension, glaucoma, and responses to Staphylococcus aureus α-toxin. Complex formation between PLEKHA7, PDZ domain–containing 11 (PDZD11), tetraspanin 33, and the α-toxin receptor ADAM metallopeptidase domain 10 (ADAM10) promotes junctional clustering of ADAM10 and α-toxin–mediated pore formation. However, how the N-terminal region of PDZD11 interacts with the N-terminal tandem WW domains of PLEKHA7 and how this interaction promotes tetraspanin 33 binding to the WW1 domain is unclear. Here, we used site-directed mutagenesis, glutathione S-transferase pulldown experiments, immunofluorescence, molecular modeling, and docking experiments to characterize the mechanisms driving these interactions. We found that Asp-30 of WW1 and His-75 of WW2 interact through a hydrogen bond and, together with Thr-35 of WW1, form a binding pocket that accommodates a polyproline stretch within the N-terminal PDZD11 region. By strengthening the interactions of the ternary complex, the WW2 domain stabilized the WW1 domain and cooperatively promoted the interaction with PDZD11. Modeling results indicated that, in turn, PDZD11 binding induces a conformational rearrangement, which strengthens the ternary complex, and contributes to enlarging a “hydrophobic hot spot” region on the WW1 domain. The last two lipophilic residues of tetraspanin 33, Trp-283 and Tyr-282, were required for its interaction with PLEKHA7. Docking of the tetraspanin 33 C terminus revealed that it fits into the hydrophobic hot spot region of the accessible surface of WW1. We conclude that communication between the two tandem WW domains of PLEKHA7 and the PLEKHA7–PDZD11 interaction modulate the ligand-binding properties of PLEKHA7.
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Yayici Köken, Özlem, Ülkühan Öztoprak, Vehap Topçu, Büsranur Çavdarli, Çagri Mesut Temucin, Üstün Aydingöz, Özge Dedeoglu Toptas, Hulya Kayilioglu, and Deniz Yuksel. "Expanding the genotype-phenotype spectrum of autosomal recessive Charcot-Marie-Tooth disease: A novel PLEKHG5 gene mutation." Neurology Asia 26, no. 3 (September 2021): 607–12. http://dx.doi.org/10.54029/2021jmr.

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Autosomal recessive intermediate Charcot Marie Tooth (CMT) disease type C is a very rarely-seen neurogenetic disorder. Homozygous or compound heterozygous mutation in the Pleckstrin homology domain-containing family G member 5 (PLEKHG5) gene on chromosome 1p36 was recently reported in patients with CMT. From the first description of the disease to date, almost 40 different variants associated with the PLEKHG5 gene were identified. Here, we present an adolescent girl who was thought initially to be myopathy because of progressive proximal muscle weakness. The electrophysiologic study revealed axonal sensory and motor neuropathy with some demyelinating features. She was diagnosed with autosomal recessive inheritance, intermediate CMT disease type C with a novel homozygous mutation in the PLEKHG5 gene in clinical exome sequencing as c.1600- 2A>G by next-generation sequencing. We describe here the novel mutation in the PLEKHG5 gene and the genotype-phenotype correlation.
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Xing, Xiangling, Ninni Mu, Xiaotian Yuan, Na Wang, C. Christofer Juhlin, Klas Strååt, Catharina Larsson, and Dawei Xu. "PLEKHS1 Over-Expression is Associated with Metastases and Poor Outcomes in Papillary Thyroid Carcinoma." Cancers 12, no. 8 (July 31, 2020): 2133. http://dx.doi.org/10.3390/cancers12082133.

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Pleckstrin homology domain containing S1 (PLEKHS1) is a poorly characterized factor, although its promoter mutations were identified in human malignancies including thyroid carcinoma (TC). This study was designed to determine PLEKHS1 promoter hotspot mutations in papillary and anaplastic thyroid carcinomas (PTCs and ATCs) and to evaluate if PLEKHS1 expression influences clinical outcome. The PLEKHS1 promoter mutation was observed in 1/93 of PTCs and none of 18 ATCs in our cohort; however, PLEKHS1 expression was aberrantly up-regulated in TCs compared to adjacent non-tumorous thyroid tissues. ATC tumors, an undifferentiated TC, exhibited the highest PLEKHS1 expression. In both TCGA and present cohorts of PTCs, PLEKHS1 gene methylation density was inversely correlated with its mRNA expression and demethylation at the PLEKHS1 locus occurred at two CpGs. Higher PLEKHS1 expression was associated with lymph node and distant metastases, and shorter overall and disease-free survival in our cohort of PTC patients. Importantly, PLEKHS1 over-expression predicted shorter patient survival in PTCs lacking TERT promoter mutations. Cellular experiments showed that PLEKHS1 over-expression enhanced AKT phosphorylation and invasiveness. Collectively, the PLEKHS1 gene demethylation causes its over-expression in PTCs. PLEKHS1 promotes aggressive behavior of TCs possibly by increasing AKT activity, and its over-expression predicts poor patient outcomes.
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Spellmann, Ilja, Dan Rujescu, Richard Musil, Ina Giegling, Just Genius, Peter Zill, Sandra Dehning, et al. "Pleckstrin homology domain containing 6 protein (PLEKHA6) polymorphisms are associated with psychopathology and response to treatment in schizophrenic patients." Progress in Neuro-Psychopharmacology and Biological Psychiatry 51 (June 2014): 190–95. http://dx.doi.org/10.1016/j.pnpbp.2014.02.006.

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Reyes, H. D., E. Devor, A. M. Newtson, Y. A. Lyons, M. McDonald, V. M. Wagner, J. N. Mattson, K. K. Leslie, and J. Gonzalez-Bosquet. "Expression of Pleckstrin Homology and RUN Domain Containing M1 (PLEKHM1) is significantly associated with Grade and Prognosis in Endometrial Adenocarcinoma." Gynecologic Oncology 156, no. 3 (March 2020): e18. http://dx.doi.org/10.1016/j.ygyno.2019.11.071.

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Nguyen, Trang Thi Thu, Wei Sun Park, Byung Ouk Park, Cha Yeon Kim, Yohan Oh, Jin Man Kim, Hana Choi, et al. "PLEKHG3 enhances polarized cell migration by activating actin filaments at the cell front." Proceedings of the National Academy of Sciences 113, no. 36 (August 23, 2016): 10091–96. http://dx.doi.org/10.1073/pnas.1604720113.

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Cells migrate by directing Ras-related C3 botulinum toxin substrate 1 (Rac1) and cell division control protein 42 (Cdc42) activities and by polymerizing actin toward the leading edge of the cell. Previous studies have proposed that this polarization process requires a local positive feedback in the leading edge involving Rac small GTPase and actin polymerization with PI3K likely playing a coordinating role. Here, we show that the pleckstrin homology and RhoGEF domain containing G3 (PLEKHG3) is a PI3K-regulated Rho guanine nucleotide exchange factor (RhoGEF) for Rac1 and Cdc42 that selectively binds to newly polymerized actin at the leading edge of migrating fibroblasts. Optogenetic inactivation of PLEKHG3 showed that PLEKHG3 is indispensable both for inducing and for maintaining cell polarity. By selectively binding to newly polymerized actin, PLEKHG3 promotes local Rac1/Cdc42 activation to induce more local actin polymerization, which in turn promotes the recruitment of more PLEKHG3 to induce and maintain cell front. Thus, autocatalytic reinforcement of PLEKHG3 localization to the leading edge of the cell provides a molecular basis for the proposed positive feedback loop that is required for cell polarization and directed migration.
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AshaRani, P. V., Syidda Amron, Noor Azizah Bte Zainuldin, Sumanty Tohari, Alvin Y. J. Ng, Guo Song, Byrappa Venkatesh, and Ajay S. Mathuru. "Whole-Exome Sequencing to Identify Potential Genetic Risk in Substance Use Disorders: A Pilot Feasibility Study." Journal of Clinical Medicine 10, no. 13 (June 25, 2021): 2810. http://dx.doi.org/10.3390/jcm10132810.

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Genetics intersects with environmental, cultural, and social factors in the development of addictive disorders. This study reports the feasibility of whole-exome sequencing of trios (subject and two family members) to discover potential genetic variants in the development of substance use disorders (SUD). Family trios were recruited from the National Addictions Management Service in Singapore during the 2016–2018 period. Recruited subjects had severe alcohol use disorder (AUD) or opioid use disorder (OUD), with nicotine dependence (ND) and a family history of addictive disorders. Demographic characteristics and severity of addiction were captured. Whole-exome sequencing (WES) and analysis were performed on salivary samples collected from the trios. WES revealed variants in several genes in each individual and disruptive protein mutations in most. Variants were identified in genes previously associated with SUDs, such as Pleckstrin homology domain-containing family M member 3 (PLEKHM3), coiled-coil serine-rich protein 1 (CCSER1), LIM and calponin homology domains-containing protein 1 (LIMCH1), dynein axonemal heavy chain 8 (DNAH8), and the taste receptor type 2 member 38 (TAS2R38) involved in the perception of bitterness. The feasibility study suggests that subjects with a severe addiction profile, polysubstance use, and family history of addiction may often harbor gene variants that may predispose them to SUDs. This study could serve as a model for future precision medicine-based personalized interventional strategies for behavioral addictions and SUDs and for the discovery of potentially pathogenic genetic variants.
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Tran, Thuy T., Chetan K. Rane, Christopher R. Zito, Sarah A. Weiss, Shlomit Jessel, Liliana Lucca, Benjamin Y. Lu, et al. "Clinical Significance of PDCD4 in Melanoma by Subcellular Expression and in Tumor-Associated Immune Cells." Cancers 13, no. 5 (March 2, 2021): 1049. http://dx.doi.org/10.3390/cancers13051049.

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Little is known about the subcellular localization and function of programmed cell death 4 (PDCD4) in melanoma. Our past studies suggest PDCD4 interacts with Pleckstrin Homology Domain Containing A5 (PLEKHA5) to influence melanoma brain metastasis outcomes, as high intracranial PDCD4 expression leads to improved survival. We aimed to define the subcellular distribution of PDCD4 in melanoma and in the tumor microenvironment during neoplastic progression and its impact on clinical outcomes. We analyzed multiple tissue microarrays with well-annotated clinicopathological variables using quantitative immunofluorescence and evaluated single-cell RNA-sequencing on a brain metastasis sample to characterize PDCD4+ immune cell subsets. We demonstrate differences in PDCD4 expression during neoplastic progression, with high tumor and stromal PDCD4 levels associated with improved survival in primary melanomas and in intracranial metastases, but not in extracranial metastatic disease. While the expression of PDCD4 is well-documented on CD8+ T cells and natural killer cells, we show that it is also found on B cells and mast cells. PDCD4 expression in the tumor microenvironment is associated with increased immune cell infiltration. Further studies are needed to define the interaction of PDCD4 and PLEKHA5 and to evaluate the utility of this pathway as a therapeutic target in melanoma brain metastasis.
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Tellermann, A., T. Witte, C. Lansche, M. Stoll, RE Schmidt, and NT Baerlecken. "Autoantibodies binding to ubiquitin-fold modifier-conjugating enzyme 1 (Ufc1) and pleckstrin homology domain containing, family G (with RhoGef domain) member 2 (Plekhg2) are associated with mycobacterial infections." HIV Medicine 16, no. 2 (September 12, 2014): 114–21. http://dx.doi.org/10.1111/hiv.12194.

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Spellmann, Ilja, Dan Rujescu, Richard Musil, Sebastian Meyer, Ina Giegling, Just Genius, Peter Zill, et al. "Corrigendum to “Pleckstrin homology domain containing 6 protein (PLEKHA6) polymorphisms are associated with psychopathology and response to treatment in schizophrenic patients” [Prog Neuro-Psychopharmacol Biol Psychiatry 51 (2014) 190–195]." Progress in Neuro-Psychopharmacology and Biological Psychiatry 58 (April 2015): 106. http://dx.doi.org/10.1016/j.pnpbp.2014.11.007.

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Dissertations / Theses on the topic "PLEKHA1 [Pleckstrin homology domain containing"

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Leveziel, Nicolas. "Génétique de la dégénérescence maculaire liée à l'âge variants majeurs de prédisposition à la forme exsudative." Paris 6, 2008. http://www.theses.fr/2008PA066183.

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Dhamodharan, Neelamegan. "Characterisation of PhdB, a pleckstrin homology domain containing protein in Dictyostelium discoideum." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972300252.

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Wang, Chi-Tang, and 王啓唐. "Investigating the role of pleckstrin homology domain containing, family A member 1 (PLEKHA1) in Age-related macular degeneration(AMD)." Thesis, 2015. http://ndltd.ncl.edu.tw/handle/68389305876457615594.

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碩士
國立陽明大學
生命科學系暨基因體科學研究所
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Age-related macular degeneration (AMD) is a multifactorial disease for visual impairment in the senior population in developed countries. Clinical manifestations of AMD include the extracellular deposits of oxidized proteins and lipids within the retinal pigment epithelium (RPE). During the visual cycle, RPE supports the photoreceptor cells for the regeneration of visual pigments and breakdown of byproducts. Thus, dysfunction of RPE may result in metabolic burden to the photoreceptor cells. Although the exact cause of AMD is not clear, many studies have indicated that aging, oxidative stress, light damage and genetic factors may play significantly pathogenic roles. Both family and case-control studies revealed that genetic variants at 1q31 and 10q26 are the major genetic contributors. Further functional studies support that complement factor H (CFH) is the main player on chromosome 1q31, while the susceptibility gene on 10q26 remains to be elucidated. The aims of this study are (1) to reconstruct the risk haplotypes at 10q26 in exudative AMD, the prominent form of AMD in Asians strongly associated with the 10q26 variants, and (2) to investigate the role of candidate genes in this region during oxidative stress. Based on meta-analysis of GWAS data from studies of AMD, it was found that the risk locus extends more to the proximal region on 10q26 rather than to the distal region. In addition, due to no consensus on the functional roles for the other two candidates, ARMS2 and HTRA1, we therefore focused on PLEKHA1 as the candidate to investigate its possible role in AMD. So far, we have found that the two major isoforms of PLEKHA1 expressed differently in various tissues and the treatments of hydrogen peroxide, which mimics oxidative stress, induced translocations of PLEKHA1 isoform 1 to the plasma membrane but not isoform 2 in ARPE-19 cells. We further investigated the response of the two isoforms of PLEKHA1 under light exposure in the presence of N-retinyl-N-retinylidene ethanolamine (A2E), an autofluorescent pigment that accumulates in RPE cells in aging and some retinal disorders, which can induce generation of reactive oxygen species and cause serious toxicity to RPE cells. Similarly, A2E oxidative stress could induced translocations of PLEKHA1 isoform 1 to the plasma membrane in ARPE-19 cells. Induced phosphorylation of Akt (v-akt murine thymoma viral oncogen) in ARPE-19 cells under hydrogen peroxide or A2E oxidative stress was observed, but decreased level of phosphorylated Akt were observed in cells overexpressing PLEKHA1 isoform 1 rather than isoform 2. Both hydrogen peroxide and A2E oxidative stress induced cell death in ARPE-19 cells, but overexpressing PLEKHA1 isoform 1 slightly decrease resistance to oxidative stress whereas overexpression of PLEKHA1 isoform 2 slightly increase resistance to oxidative stress. To sum up, PLEKHA1 may play a role in cell survival under oxidative stress, thus it is a putative pathological cause for AMD.
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KALTENBRUNNER, Sabine. "Characterization of TbPH1, a kinetoplastid-specific pleckstrin homology domain containing kinesin-like protein." Master's thesis, 2017. http://www.nusl.cz/ntk/nusl-317938.

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The aim of this master thesis was the investigation of the uncharacterized protein TbPH1, by in silico studies, determining effects of its knock-down, studying the effect of a knock-down on the cell cycle, examining its cellular localization, and finding out about possible complexes and interaction-partners.
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Dhamodharan, Neelamegan [Verfasser]. "Characterisation of PhdB, a pleckstrin homology domain containing protein in Dictyostelium discoideum / vorgelegt von Dhamodharan Neelamegan." 2004. http://d-nb.info/972300252/34.

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Book chapters on the topic "PLEKHA1 [Pleckstrin homology domain containing"

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "PLEKHO1 (Pleckstrin-Homology Domain Containing, Family O Member 1)." In Encyclopedia of Signaling Molecules, 1446. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101066.

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"Pleckstrin Homology Domain Containing, Family Member 1." In Encyclopedia of Signaling Molecules, 4077. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_102969.

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