Relevant bibliographies by topics / Actin

Academic literature on the topic 'Actin'

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Published: 4 June 2021
Last updated: 30 July 2024

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Journal articles on the topic "Actin"

1

Roberts, Thomas M., and Murray Stewart. "Acting like Actin." Journal of Cell Biology 149, no. 1 (April 3, 2000): 7–12. http://dx.doi.org/10.1083/jcb.149.1.7.

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2

Vinson, V. "Acting Like Actin." Science 330, no. 6009 (December 2, 2010): 1289. http://dx.doi.org/10.1126/science.330.6009.1289-b.

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Marx, Vivien. "Actin in action." Nature Methods 20, no. 2 (February 2023): 178–82. http://dx.doi.org/10.1038/s41592-022-01762-2.

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Muscat, G. E., T. A. Gustafson, and L. Kedes. "A common factor regulates skeletal and cardiac alpha-actin gene transcription in muscle." Molecular and Cellular Biology 8, no. 10 (October 1988): 4120–33. http://dx.doi.org/10.1128/mcb.8.10.4120-4133.1988.

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The skeletal and cardiac alpha-actin genes are coexpressed in muscle development but exhibit distinctive tissue-specific patterns of expression. We used an in vivo competition assay and an in vitro electrophoretic mobility shift assay to demonstrate that both genes interact with a common trans-acting factor(s). However, there was at least one gene-specific cis-acting sequence in the skeletal alpha-actin gene that interacted with a trans-acting factor which was not rate limiting in the expression of the cardiac alpha-actin gene. The common factor(s) interacted with several cis-acting regions that corresponded to sequences that are required for the transcriptional modulation of these sarcomeric alpha-actin genes in muscle cells. These regulatory regions contained the sequence motif CC(A + T-rich)6GG, which is known as a CArG box. Results of in vivo competition assays demonstrated that the factor(s) bound by the skeletal alpha-actin gene is also essential for the maximal activity of the cardiac alpha-actin, simian virus 40 (SV40), alpha 2(I)-collagen, and the beta-actin promoters in muscle cells. In contrast, fibroblastic cells contained functionally distinct transcription factor(s) that were used by the SV40 enhancer but that did not interact with the sarcomeric alpha-actin cis-acting sequences. The existence of functionally different factors in these cell types may explain the myogenic specificity of these sarcomeric alpha-actin genes. Results of in vitro studies suggested that both the sarcomeric alpha-actin genes interact with the CArG box-binding factor CBF and that the skeletal alpha-actin promoter contains multiple CBF-binding sites. In contrast, CBF did not interact in vitro with a classical CAAT box, the SV40 enhancer, or a linker scanner mutation of an alpha-actin CArG box. Furthermore, methylation interference and DNase I footprinting assays demonstrated the precise sites of interaction of CBF with three CArG motifs at positions -98, -179, and -225 in the human skeletal alpha-actin gene.
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Muscat, G. E., T. A. Gustafson, and L. Kedes. "A common factor regulates skeletal and cardiac alpha-actin gene transcription in muscle." Molecular and Cellular Biology 8, no. 10 (October 1988): 4120–33. http://dx.doi.org/10.1128/mcb.8.10.4120.

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The skeletal and cardiac alpha-actin genes are coexpressed in muscle development but exhibit distinctive tissue-specific patterns of expression. We used an in vivo competition assay and an in vitro electrophoretic mobility shift assay to demonstrate that both genes interact with a common trans-acting factor(s). However, there was at least one gene-specific cis-acting sequence in the skeletal alpha-actin gene that interacted with a trans-acting factor which was not rate limiting in the expression of the cardiac alpha-actin gene. The common factor(s) interacted with several cis-acting regions that corresponded to sequences that are required for the transcriptional modulation of these sarcomeric alpha-actin genes in muscle cells. These regulatory regions contained the sequence motif CC(A + T-rich)6GG, which is known as a CArG box. Results of in vivo competition assays demonstrated that the factor(s) bound by the skeletal alpha-actin gene is also essential for the maximal activity of the cardiac alpha-actin, simian virus 40 (SV40), alpha 2(I)-collagen, and the beta-actin promoters in muscle cells. In contrast, fibroblastic cells contained functionally distinct transcription factor(s) that were used by the SV40 enhancer but that did not interact with the sarcomeric alpha-actin cis-acting sequences. The existence of functionally different factors in these cell types may explain the myogenic specificity of these sarcomeric alpha-actin genes. Results of in vitro studies suggested that both the sarcomeric alpha-actin genes interact with the CArG box-binding factor CBF and that the skeletal alpha-actin promoter contains multiple CBF-binding sites. In contrast, CBF did not interact in vitro with a classical CAAT box, the SV40 enhancer, or a linker scanner mutation of an alpha-actin CArG box. Furthermore, methylation interference and DNase I footprinting assays demonstrated the precise sites of interaction of CBF with three CArG motifs at positions -98, -179, and -225 in the human skeletal alpha-actin gene.
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P, RAGHAVENDRA K., RAKESH KUMAR, JOY DAS, SANTOSH H. B, SACHIN A. MORE, RAMAKRISHNA N, SHILPA G. CHAWLA, SANDHYA KRANTHI, and KESHAV RAJ KRANTHI. "Quantitative real-time PCR based evaluation and validation of reference genes in Gossypium arboreum." Indian Journal of Agricultural Sciences 90, no. 1 (March 2, 2020): 40–47. http://dx.doi.org/10.56093/ijas.v90i1.98527.

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Estimation of gene expression levels plays a crucial role in understanding the function of the target gene(s). Intersample variance in gene expression can be more precisely measured if transcripts levels are accurately normalized. Normalization is pre-requisite step prior to the determination of candidate gene expression by qPCR. In this study conducted at ICAR-Central Institute for Cotton Research, Nagpur during 2015–16, six candidate reference genes, viz. actin4 (ACT4), actin7(ACT7), RNA Helicase (RNAH), Serine/threonine-protein phosphatase PP2A-1(PP2A1), ubiquitin7 (UBQ7) and α tubulin (αTUB) were systematically analysed for their expression patterns in different tissues pertaining to three development stages of cotton namely seedling, early reproductive and fiber development. The study has identified actin-4/actin-7/ubiquitin-7 as the most ideal reference genes for fiber development stages whereas actin-4/ ubiquitin-7 and actin-7/RNA helicases for seedling and early reproductive development stages, respectively. Validation of identified reference genes for relative expression analysis of Gacobl9, a COBRA-like protein, demonstrated their usefulness in qPCR analysis in Gossypium arboreum.
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Hurtley, Stella M. "Parasite actin in action." Science 366, no. 6465 (October 31, 2019): 584.6–585. http://dx.doi.org/10.1126/science.366.6465.584-f.

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Hurtley, S. M. "Nuclear Actin in Action." Science Signaling 6, no. 276 (May 21, 2013): ec116-ec116. http://dx.doi.org/10.1126/scisignal.2004335.

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9

Geitmann, Anja. "Actuators Acting without Actin." Cell 166, no. 1 (June 2016): 15–17. http://dx.doi.org/10.1016/j.cell.2016.06.030.

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WINDER, Steven J., Thomas JESS, and Kathryn R. AYSCOUGH. "SCP1 encodes an actin-bundling protein in yeast." Biochemical Journal 375, no. 2 (October 15, 2003): 287–95. http://dx.doi.org/10.1042/bj20030796.

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The association of F-actin (filamentous actin) with a large number of binding proteins is essential for cellular function. Actin-binding proteins control the dynamics of actin filaments, nucleate new filaments and facilitate formation of higher-order structures such as actin bundles. The yeast gene SCP1 encodes a small protein with significant homology to mammalian SM22/transgelin. We have investigated the role of Scp1p in budding yeast to probe the fundamental role of this family of proteins. Here, we demonstrate that Scp1p binds to F-actin and induces the formation of tight F-actin bundles in vitro. Deletion of SCP1 in yeast lacking the actin-bundling protein, fimbrin (Sac6p), exacerbates the disrupted actin phenotype and enhances latrunculin-A sensitivity. Furthermore, Scp1p co-localizes with actin in cortical patches and its localization is lost in the presence of latrunculin-A. Our data support a role for Scp1p in bundling actin filaments and, in concert with Sac6p, acting as a second actin-bundling activity crucial to the stability of the yeast actin cytoskeleton.
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Dissertations / Theses on the topic "Actin"

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Wang, Hui. "Structural studies of actin and actin-binding proteins." Thesis, University of British Columbia, 2009. http://hdl.handle.net/2429/10916.

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Actin is involved in cell movement, maintaining cell shape and anchoring cytoskeletal proteins. These functions are regulated by many actin-binding proteins, including those of the gelsolin superfamily. Gelsolin superfamily members regulate actin organization by severing, capping F-actin, nucleating the formation of F-actin and/or bundling F-actin. Although abundant structures are available for gelsolin and gelsolin fragments in complexes with actin, the detailed mechanisms for gelsolin activation, and for gelsolin severing and capping of F-actin are still unknown. Structures for gelsolin family members and their complexes with actin help elucidate these mechanisms. In this thesis, I describe the purification, crystallization and solution of the structures of the following four proteins and protein complexes, including human G1-G3/actin complex, a novel equine G1-G3/actin complex, human villin domain V6 and actin monomer. The structure of human G1-G3/actin indicates cooperative binding of calcium ions in G2 and G6 is responsible for opening the G2/G6 latch to expose the F-actin binding site on G2. A new equine G1-G3/actin structure suggests G2-G3 can adopt a CapG-like conformation and reveals novel interactions between gelsolin and actin. The villin V6 structure implies a common spring-loaded activation mechanism in the gelsolin superfamily. Finally, a new actin monomer structure is the first reported for G-actin in an ATP state, without ABPs or modification. All these structures contribute to our understanding of actin's physiological roles and their regulation by the gelsolin superfamily.
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Hull, Richard Alan. "Actin and actin-binding proteins in higher plants." Thesis, University of Oxford, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.279874.

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Heisler, David Bruce. "Role of Actin and Actin-binding Proteins in the Pathogenesis of Actin-targeting Bacterial Toxins." The Ohio State University, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=osu1501519777175964.

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Gholami, Azam. "Actin-based motility." Diss., lmu, 2007. http://nbn-resolving.de/urn:nbn:de:bvb:19-72151.

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Yeoh, Sharon I.-Wen. "Molecular interactions of human actin depolymerizing factor and cofilin with actin." Thesis, University of Cambridge, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621255.

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Gallinger, Julia. "WH2 domains and actin variants as multifunctional organizers of the actin cytoskeleton." Diss., Ludwig-Maximilians-Universität München, 2013. http://nbn-resolving.de/urn:nbn:de:bvb:19-161698.

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Actin is one of the most abundant proteins in eukaryotic cells and regulation of the microfilament system is crucial for a wide range of cellular functions including cell shape, cell motility, cell division and membrane dynamics. The aim of this thesis was (1) to gain a better understanding of the function of distinct actin binding domains in the regulation of the actin cytoskeleton and (2) to elucidate the role of actin variants. WH2 domains (WH2, Wiskott-Aldrich syndrome protein homology 2) are ubiquitous multifunctional regulators of actin dynamics. The protein Spire contains four central WH2 domains A-B-C-D with about 20 amino acids each and the cyclase-associated protein CAP2 contains only one WH2 domain. Under certain conditions, they can (1) nucleate actin polymerization, (2) disintegrate actin filaments and (3) sequester actin monomers. Here, the influence of selected Drosophila melanogaster Spire-WH2 and Mus musculus CAP2-WH2 domain constructs on actin dynamics was tested in vitro. To act as a filament nucleator, at least two WH2 domains are required, and nucleation of actin polymerization was only observed at substoichiometric concentrations of WH2 domains over actin. At higher concentrations, the sequestering activity of WH2 domains takes over. Preformed and purified SpireWH2-actin complexes act as extremely efficient nuclei for actin polymerization, even at superstoichiometric WH2 concentrations, under which free WH2 domains would sequester actin. All analyzed constructs, including these with only a single WH2 domain, sequester actin as well as they can disrupt filaments. This latter and most peculiar behavior of WH2 domains was observed in fluorometric, viscometric and TIRF assays. The WH2 domains seem to have such a high affinity for actin that they can forcefully sequester monomers even from filaments and filament bundles, thus breaking the whole structures. Taken together, the data clearly show that SpireWH2-actin complexes are the intermediates that account for the observed nucleating activity, whereas free WH2 domains can disrupt filaments and filament bundles within seconds, again underlining the intrinsic versatility of this regulator of actin dynamics. These data have been confirmed by crystallography in collaboration with the groups of Prof. Dr. Tad Holak and Prof. Dr. Robert Huber (Martinsried, Germany). Besides the well-studied conventional actins many organisms harbor actin variants with unknown function. The model organism Dictyostelium discoideum comprises an actinome of a total of 41 actins, actin isoforms and actin-related proteins. Among them is filactin, a highly conserved actin with an elongated N-terminus. The 105 kDa protein has a distinct domain organization and homologs of this protein are present in other Dictyosteliidae and in some pathogenic Entamoebae. Here, the functions of filactin were studied in vivo and in vitro. Immunofluorescence studies in D. discoideum localize endogenous and GFP-filactin in the cytoplasm at vesicle-like structures and in cortical regions of the cell. A most peculiar behavior is the stress-induced appearance of full length filactin in nuclear actin rods. To perform in vitro analyses recombinant filactin was expressed in Sf9 cells. Fluorescence studies with the filactin actin domain suggest that it interferes with actin polymerization by sequestering G-actin or even capping filaments. Gel filtration assays propose a tetrameric structure of full length filactin. Protein interaction studies suggest that filactin is involved in the ESCRT (endosomal sorting complexes required for transport) pathway which is responsible for multivesicular body formation. The data on filactin suggest that only the conventional actins are the backbone for the microfilamentous system whereas less related actin isoforms have highly specific and perhaps cytoskeleton-independent subcellular functions.
Aktin ist als Bestandteil des Zytoskeletts eines der häufigsten Proteine in allen eukaryontischen Zellen. Eine genaue Regulation des Mikrofilamentsystems ist essentiell für Zellform, Zellmigration, Zellteilung und Membrandynamik. Ziel dieser Arbeit war (1) die Funktion von ausgewählten Aktin Bindedomänen in der Regulation des Aktin Zytoskeletts zu untersuchen und (2) die Funktion von Aktinvarianten zu verstehen. WH2 Domänen (WH2, Wiskott-Aldrich Syndrom Protein Homologie 2) sind kurze, konservierte Sequenzmotive (ca. 20 Aminosäuren), welche bevorzugt monomere Aktinmoleküle binden. Von besonderem Interesse waren Drosophila melanogaster Spire-WH2 und Mus musculus CAP2-WH2 Konstrukte. Das Protein Spire enthält vier WH2 Domänen (A-B-C-D) wohingegen CAP2 (Cyclase-assoziiertes Protein 2) nur eine WH2 Domäne besitzt. Diese WH2 Domänen können unter bestimmten Bedingungen (1) die Aktinpolymerisation stimulieren, (2) Aktinfilamente zerstückeln und (3) Aktinmonomere sequestrieren. Für die Nukleation der Aktinpolymerisation müssen mindestens zwei hintereinander angeordnete WH2 Domänen vorhanden sein und unterstöchiometrische Mengen an WH2 Domänen im Vergleich zur Aktinkonzentration vorliegen. Bei höheren WH2 Konzentrationen überwiegt die Sequestrierungsaktivität. Polymerisationsexperimente mit vorgefertigten SpireWH2-Aktin Komplexen bestätigen, dass diese Komplexe für die beobachtete Nukleation der Aktinpolymerisation verantwortlich sind. Im Gegensatz zu ungebundenen WH2 Domänen sind diese WH2-Aktin Komplexe selbst bei überstöchiometrischen WH2 Konzentrationen äußerst effiziente Nukleatoren. Alle untersuchten WH2 Konstrukte zeigen die bereits bekannte Bindung an G-Aktin, können aber auch vorgeformte Aktinfilamente sogar auseinanderreißen. Diese letztere und besonders auffällige Eigenschaft von WH2 Domänen wurde in fluorometrischen, viskometrischen und TIRF Experimenten nachgewiesen. Anscheinend ist die Affinität der WH2 Domänen zu Aktinmonomeren so stark, dass sie diese aus den Filamenten entfernen können und damit ganze Filamente und Filamentbündel zerstückeln. Für die Multifunktionalität der analysierten konservierten WH2 Domänen spricht zusammenfassend, dass sie neben der Aktinfilament Nukleation auch Filamente und Filamentbündel innerhalb von Sekunden fragmentieren können. Diese Daten wurden in Kollaboration mit den Gruppen Prof. Dr. Tad Holak und Prof. Dr. Robert Huber (Martinsried) durch kristallographische Versuchsansätze bestätigt. Neben den gut untersuchten konventionellen Aktinisoformen liegen oft auch Aktinvarianten vor, deren Funktion bisher unbekannt ist. Der Modellorganismus Dictyostelium discoideum besitzt mit seinen 41 Aktinen und Aktin-verwandten Proteinen ein umfangreiches „Aktinom”. Dazu gehört auch das Protein Filaktin (105 KDa), eine besonders außergewöhnliche Aktinvariante, die neben der konservierten Aktin-ähnlichen Domäne zusätzlich einen verlängerten N-Terminus mit einer definierten Domänenstruktur besitzt. Homologe von Filaktin wurden bisher in Dictyosteliden und einigen pathogenen Entamoeben identifiziert. Im zweiten Teil dieser Arbeit wurden die Funktionen von Filaktin in vivo und in vitro analysiert. Immunfluoreszenz Experimente zeigen, dass Filaktin mit konventionellem Aktin kolokalisiert und zusätzlich im Zytoplasma an Vesikel-artigen Strukturen zu sehen ist. Ein besonderes Merkmal von Filaktin ist zudem, dass es Teil von Stress-induzierten, intranukleären, stäbchenförmigen Proteinaggregaten, sogenannten „nuclear rods” ist. Für umfassende in vitro Experimente wurden rekombinante Filaktin Konstrukte mithilfe von Sf9 Insektenzellen exprimiert. Die Ergebnisse von fluorometrischen und viskometrischen Experimenten deuten darauf hin, dass die Aktin Domäne von Filaktin Aktinmonomere sequestrieren oder sogar Aktinfilamente verkappen kann. Gelfiltrationsexperimente ergaben zusätzlich, dass Filaktin wohl als Tetramer vorliegt. Außerdem verbinden Protein-Interaktionsstudien Filaktin mit dem ESCRT Signalweg (Endosomal Sorting Complexes Required for Transport), der unter anderem bei der Entstehung von multivesikulären Körpern wichtig ist. Zusammengefasst besteht das Mikrofilamentsystem vermutlich hauptsächlich aus konventionellen Aktinen, wohingegen spezielle Aktinvarianten andere zusätzliche und sogar Zytoskelett-unabhängige Funktionen übernehmen können.
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Broderick, Michael James Francis. "The utrophin-actin interface." Thesis, University of Glasgow, 2005. http://theses.gla.ac.uk/30889/.

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The spectrin superfamily is a diverse group of proteins variously involved in cross- linking, bundling and binding to the F-actin cytoskeleton. These proteins are modular in nature and interaction with actin occurs, at least in part, via CH domain containing ABDs. The actin binding domains of the spectrin superfamily proteins are all very similar in overall structure however the functions of the individual proteins differ greatly. Utrophin is a member of the spectrin superfamily and has been used extensively to investigate and model the association of actin-binding domains with F- actin; however, much controversy exists as to whether binding occurs when the domain is in an open or a closed conformation. The data herein specifically investigates the importance of the utrophin ABD inter- CH domain linker to the conformation of the domain and how this domain associates with F-actin. We provide evidence that this particular region of the ABD is particularly sensitive to mutation and that the conformation of the domain when in solution cannot be altered by affecting the electrostatic environment surrounding the protein. It has been assumed previously that the utrophin ABD adopts a closed and compact configuration in solution similar to the fimbrin crystal structure conformation; however we present evidence that suggests this is not the case. It has been proposed that the utrophin ABD may open from this closed conformation to bind F-actin in a more open manner, we present data that demonstrates that opening of the domain is not essential to F-actin binding and that there is very little conformation change associated with the domain upon interaction with F-actin. It appears that the utrophin ABD can bind F actin in two conformations. This supports current models of utrophin ABD binding where interaction with F-actin occurs in either an open or closed conformation. The data presented here provides an interesting insight into the utrophin ABD/F-actin interaction and raises many questions regarding the evaluation of current binding models. Future research stemming from this work will serve to further the understanding of how utrophin and related actin-binding proteins interact with F-actin.
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McGrath, James L. (James Lionel). "Actin dynamics in the cell cytoplasm and the role of actin associated proteins." Thesis, Massachusetts Institute of Technology, 1998. http://hdl.handle.net/1721.1/50446.

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Singh, Anish D. "Regulation and function of the non-muscle [beta]-actin and [gamma]-actin genes." Phd thesis, Department of Paediatrics and Child Health, Faculty of Medicine, 2004. http://hdl.handle.net/2123/11556.

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Kruth, Karina Annette. "Effects of three deafness-causing gamma-actin mutations on actin structure and function." Diss., University of Iowa, 2013. https://ir.uiowa.edu/etd/1475.

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Hearing requires proper function of the auditory hair cell, which is critically dependent upon its actin-based cytoskeletal structure. Eleven point mutations in gamma (γ) nonmuscle actin have been identified as causing progressive autosomal dominant nonsyndromic hearing loss (DFNA20/26); however, exactly why these mutations lead to deafness is unclear. Organization, stability, and repair of the hair cell cytoskeleton are highly regulated by actin binding proteins (ABPs), and two of the mutations, K118M and K118N, are located near an area of the actin monomer believed to be important in actin-ABP interactions. A third mutation, D51N, is located in a region of the actin monomer believed to be important for polymerization dynamics and stability in filamentous actin. I therefore hypothesized that the K118M/N mutations cause hearing loss due to impaired regulation of the actin cytoskeleton within the hair cell, whereas the D51N mutation likely interferes with polymerization dynamics and actin filament stability or flexibility. The goal of my thesis was to investigate the effects of these three mutations, K118M, K118N, and D51N, on actin dynamics and regulation. I show in Chapter 2 that the K118M/N mutations differentially affect regulation of actin by the Arp2/3 complex, but also, surprisingly, that the K118N mutation accelerates polymerization dynamics. Chapter 3 details a continued investigation of the K118M/N mutations to ascertain their effects on actin structure and dynamics, particularly with regard to how they may affect polymerization. Chapter 4 provides both an in vivo and in vitro characterization of the D51N mutation, which revealed that not only does the mutation significantly accelerate actin polymerization, it also causes significant effects on yeast mitochondrial morphology and cytoskeletal regulation. The work detailed within this thesis provides new insight into how the K118M/N and D51N mutations affect actin structure and dynamics and how these effects could lead to deafness. More importantly, this work provides a strong foundation for many future studies, ranging from structural investigation of the K118N and D51N actins as F-actin mimics, to the potential role of mitochondria in actin-based disease.
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Books on the topic "Actin"

1

Sheterline, Peter. Actin. London: Academic Press, 1994.

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Sheterline, Peter. Actin. London: Academic Press, 1995.

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Jon, Clayton, and Sparrow John C. 1947-, eds. Actin. 4th ed. Oxford: Oxford University Press, 1998.

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Estes, James E., and Paul J. Higgins, eds. Actin. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2578-3.

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Remedios, Cristobal G. Molecular Interactions of Actin: Actin Structure and Actin-Binding Proteins. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001.

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Thomas, D. D. Molecular Interactions of Actin: Actin-Myosin Interaction and Actin-Based Regulation. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002.

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Gallo, Gianluca, and Lorene M. Lanier, eds. Neurobiology of Actin. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-7368-9.

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Carlier, Marie-France, ed. Actin-based Motility. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9301-1.

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Jockusch, Brigitte M., ed. The Actin Cytoskeleton. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-46371-1.

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Kale, Avinash, ed. Actin Polymerization in Apicomplexan. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-7450-0.

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Book chapters on the topic "Actin"

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Wu, Yuntao. "Actin." In Encyclopedia of AIDS, 1–9. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-9610-6_70-1.

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Mehlhorn, Heinz. "Actin." In Encyclopedia of Parasitology, 59. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-43978-4_52.

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Böning, Dieter, Michael I. Lindinger, Damian M. Bailey, Istvan Berczi, Kameljit Kalsi, José González-Alonso, David J. Dyck, et al. "Actin." In Encyclopedia of Exercise Medicine in Health and Disease, 7. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2010.

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Dugina, Vera, Richard Arnoldi, Paul A. Janmey, and Christine Chaponnier. "ACTIN." In Cytoskeleton and Human Disease, 3–28. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-788-0_1.

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Farmer, Stephen R. "Actin." In Cell and Molecular Biology of the Cytoskeleton, 131–49. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2151-4_6.

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Mehlhorn, Heinz. "Actin." In Encyclopedia of Parasitology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27769-6_52-2.

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Wu, Yuntao. "Actin." In Encyclopedia of AIDS, 6–13. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7101-5_70.

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Isenberg, Gerhard. "Actin and Actin-Associated Proteins." In Cytoskeleton Proteins, 25–149. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79632-6_8.

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Amos, Linda A., and W. Bradshaw Amos. "Actin Filaments." In Molecules of the Cytoskeleton, 42–55. London: Macmillan Education UK, 1991. http://dx.doi.org/10.1007/978-1-349-21739-7_3.

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Schröer, Elke, Klaus Ruhnau, Norma Selve, and Albrecht Wegner. "Actin Polymerization." In Signal Transduction and Protein Phosphorylation, 141–47. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4757-0166-1_19.

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Conference papers on the topic "Actin"

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Wegner, Albrecht, Andrea Gaertner, and Thekla Ohm. "The actin treadmill." In The living cell in four dimensions. AIP, 1991. http://dx.doi.org/10.1063/1.40588.

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Bidone, Tamara C., Marco A. Deriu, Giacomo Di Benedetto, Diana Massai, and Umberto Morbiducci. "Insights Into the Molecular Mechanisms of Actin Dynamics: A Multiscale Modeling Approach." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53417.

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Actin dynamics, which is at the basis of many fundamental cellular processes as cell migration [1], is governed by the self-assembly and disassembly of actin monomers (G-actin) that, in turn, are determined by the kinetics of ATP hydrolysis and by the local concentrations of Mg2+ and Ca2+ [2]. During cell migration, interactions of the actin filaments (F-actin) with different nucleotide-cation complexes induce local topological rearrangements, because the filament building G-actins undergo conformational shifts between multiple equilibrium states separated by low-energy barriers. For example, the structural rearrangements of the DNase-I binding loop (residues 38–52) in subdomain 2 are driven by ATP hydrolysis and the changes in the conformation of subdomain 4 are induced by the presence of a tightly-bound Mg2+ or Ca2+ ion (Figure 1a). These conformational shifts alter the cross-linking between monomers, varying the contact surfaces among adjacent inter- and intrasubdomains of G-actin, and reflect on the overall properties of F-actin.
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Chaudhuri, Ovijit, Sapun H. Parekh, Allen Liu, and Daniel A. Fletcher. "Viscoelasticity of Growing Actin Networks." In ASME 2004 International Mechanical Engineering Congress and Exposition. ASMEDC, 2004. http://dx.doi.org/10.1115/imece2004-60076.

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Actin self-assembles to form filaments that can organize into dendritic networks through interactions with various actin binding proteins. Growing actin filament networks produce significant mechanical forces that play a key role in many dynamic cellular processes such as motility, cytokinesis, and phagocytosis. We investigated the mechanical properties of growing actin networks with atomic force microscopy and found the actin networks to behave as viscoelastic solids.
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Watanabe, Shun N., and Kenichi Yoshikawa. "Bundling Transition of F-actin." In 2006 IEEE International Symposium on Micro-NanoMechatronics and Human Science. IEEE, 2006. http://dx.doi.org/10.1109/mhs.2006.320320.

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Ronaghi, Zahra, Yongkuk Lee, Chenbo Dong, Cerasela Zoica Dinu, and Parviz Famouri. "Carbon nanotube - actin hybrid assemblies." In 2012 IEEE 12th International Conference on Nanotechnology (IEEE-NANO). IEEE, 2012. http://dx.doi.org/10.1109/nano.2012.6322145.

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Yamazaki, Shota, Masahiko Harata, Toshitaka Idehara, Keiji Konagaya, Ginji Yokoyama, Hiromichi Hoshina, and Yuichi Ogawa. "Terahertz irradiation stimulates actin polymerization." In 2018 43rd International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz 2018). IEEE, 2018. http://dx.doi.org/10.1109/irmmw-thz.2018.8510110.

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Liu, Yi, and Juan Ren. "Modeling and Control of Dynamic Cellular Mechanotransduction: Part I — Actin Cytoskeleton Quantification." In ASME 2018 Dynamic Systems and Control Conference. American Society of Mechanical Engineers, 2018. http://dx.doi.org/10.1115/dscc2018-9180.

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Living cells respond to external stimuli through the reorganization of the actin cytoskeleton, and the actin cytoskeleton significantly affects the cellular mechanical behavior. However, due to the lack of approaches to actin cytoskeleton quantification, the dynamics of mechanotransduction is still poorly understood. In this study, we propose an image recognition-based quantification (IRQ) approach to actin cytoskeleton quantification. IRQ quantifies the actin cytoskeleton through three parameters: the partial actin-cytoskeletal deviation (PAD), the total actin-cytoskeletal deviation (TAD) and the average actin-cytoskeletal intensity (AAI). First, Canny and Sobel edge detectors are applied to skeletonize the actin cytoskeleton images, then PAD and TAD are quantified using the direction of lines detected by Hough transform, and AAI is calculated through the summational brightness over the detected cell area. For validation, six different actin cytoskeleton meshwork models were generated to verify the quantification accuracy of IRQ. The average error for both the quantified PAD and TAD was less than 1.22°. Then IRQ was implemented to quantify the actin cytoskeleton of NIH/3T3 cells treated with an F-actin inhibitor. The quantification results suggest that the local and total actin-cytoskeletal organization of treated cells were more disordered than untreated cells, and the quantity of the actin cytoskeleton decreased significantly after the F-actin treatment.
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Nikmaneshi, Mohammad Reza, Bahar Firoozabadi, and Mohammad Said Saidi. "Continuum model of actin-myosin flow." In 2013 20th Iranian Conference on Biomedical Engineering (ICBME). IEEE, 2013. http://dx.doi.org/10.1109/icbme.2013.6782200.

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Springer, Michael, Jeffrey W. Leon, Tiecheng Qiao, Jon Hammerschmidt, and James L. McGrath. "Metallization of surface- attached actin networks." In Conference Proceedings. Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2006. http://dx.doi.org/10.1109/iembs.2006.260512.

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Springer, Michael, Jeffrey W. Leon, Tiecheng Qiao, Jon Hammerschmidt, and James L. McGrath. "Metallization of surface- attached actin networks." In Conference Proceedings. Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2006. http://dx.doi.org/10.1109/iembs.2006.4397689.

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Reports on the topic "Actin"

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Zhan, Xi. The Role of Actin Polymerization in Tumor Metastasis. Fort Belvoir, VA: Defense Technical Information Center, August 2004. http://dx.doi.org/10.21236/ada431324.

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Zhan, Xi. The Role of Actin Polymerization in Tumor Metastasis. Fort Belvoir, VA: Defense Technical Information Center, August 2002. http://dx.doi.org/10.21236/ada411545.

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Zhan, Xi. The Role of Actin Polymerization in Tumor Metastasis. Fort Belvoir, VA: Defense Technical Information Center, August 2003. http://dx.doi.org/10.21236/ada420763.

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Staiger, C. J. Identification of Actin-Binding Proteins from Maize Pollen. Office of Scientific and Technical Information (OSTI), January 2004. http://dx.doi.org/10.2172/820708.

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Reecy, James M., and David Morris. β-agonist Regulate Skeletal Actin Gene Expression Post-transcriptionally. Ames (Iowa): Iowa State University, January 2004. http://dx.doi.org/10.31274/ans_air-180814-616.

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Chew, Teng-Leong. Regulation of Actin-Myosin Cytoskeletal Changes Involved in Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada396798.

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Daniel Szymanski. The Arabidopsis Wave Complex: Mechanisms Of Localized Actin Polymerization And Growth. Office of Scientific and Technical Information (OSTI), October 2012. http://dx.doi.org/10.2172/1053522.

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Ramesh, Vijaya. Neurofibromatosis 2 Tumor Suppressor Protein, Merlin, in Cellular Signaling to Actin Cytoskeleton. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada395581.

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Tran, Emily, Jasmine J. Park, Nandini N. Kulkarni, and Vinay S. Gundlapalli. Left Facial Primary Leiomyosarcoma Misdiagnosed as Atypical Fibroxanthoma and Immunochemical Markers Relevant to Diagnosis: A Case Report. Science Repository, February 2024. http://dx.doi.org/10.31487/j.ajscr.2023.04.03.

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Soft tissue sarcomas are relatively rare neoplasms of mesenchymal origin that generally make up less than 2% of all adult malignant neoplasms. Atypical fibroxanthoma is a benign soft tissue tumor often confused with malignant variants of similar tumors such as leiomyosarcoma due to similar staining markers and cell morphology. We report a case of a 70-year-old caucasian male who initially presented with a 2 cm exophytic left facial lesion that was misdiagnosed as atypical fibroxanthoma upon biopsy. The patient underwent a wide local excision of the growing 11 cm mass and immediate reconstruction with a cervicofacial flap and full thickness skin graft. Pathological analysis of the specimen revealed the final diagnosis as confirmed primary leiomyosarcoma. Both the patient’s biopsy report and the surgical pathology report revealed similar negative findings (desmin, cytokeratin AE1/AE3, p63, SOX10) as well as similar positive findings (smooth muscle actin and CD68). Critical distinctions that led to a change in diagnosis from atypical fibroxanthoma to leiomyosarcoma emerged during the final pathological analysis, which revealed more widespread positive staining for smooth muscle actin and muscle-specific actin throughout the surgical specimen along with detailed cell and nucleus morphology of atypical spindle cells in the dermis and subcutis. This valuable information was not available during the initial biopsy when the lesion was smaller. It is possible that earlier diagnosis of primary leiomyosarcoma could have resulted in advanced pre-operative treatment and excision of the facial lesion, preventing involvement of surrounding areas such as the patient’s left eye, ear, and facial nerve.
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Broadley, Caroline, Debra A. Gonzalez, Rhada Nair, and Jeffrey M. Davidson. Canine Vocal Fold Fibroblasts in Culture: Expression of alpha-Smooth Muscle Actin and Modulation of Elastin Synthesis. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada302739.

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