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1.
Mol Syst Biol ; 17(11): e10396, 2021 11.
Artigo em Inglês | MEDLINE | ID: mdl-34709727

RESUMO

Treatment options for COVID-19, caused by SARS-CoV-2, remain limited. Understanding viral pathogenesis at the molecular level is critical to develop effective therapy. Some recent studies have explored SARS-CoV-2-host interactomes and provided great resources for understanding viral replication. However, host proteins that functionally associate with SARS-CoV-2 are localized in the corresponding subnetwork within the comprehensive human interactome. Therefore, constructing a downstream network including all potential viral receptors, host cell proteases, and cofactors is necessary and should be used as an additional criterion for the validation of critical host machineries used for viral processing. This study applied both affinity purification mass spectrometry (AP-MS) and the complementary proximity-based labeling MS method (BioID-MS) on 29 viral ORFs and 18 host proteins with potential roles in viral replication to map the interactions relevant to viral processing. The analysis yields a list of 693 hub proteins sharing interactions with both viral baits and host baits and revealed their biological significance for SARS-CoV-2. Those hub proteins then served as a rational resource for drug repurposing via a virtual screening approach. The overall process resulted in the suggested repurposing of 59 compounds for 15 protein targets. Furthermore, antiviral effects of some candidate drugs were observed in vitro validation using image-based drug screen with infectious SARS-CoV-2. In addition, our results suggest that the antiviral activity of methotrexate could be associated with its inhibitory effect on specific protein-protein interactions.


Assuntos
Antivirais/farmacologia , COVID-19/tratamento farmacológico , Descoberta de Drogas , Interações Hospedeiro-Patógeno/efeitos dos fármacos , Proteoma/efeitos dos fármacos , SARS-CoV-2/fisiologia , COVID-19/virologia , Reposicionamento de Medicamentos , Humanos , Espectrometria de Massas , Metotrexato/farmacologia , Proteômica , Replicação Viral/efeitos dos fármacos
2.
Artigo em Inglês | MEDLINE | ID: mdl-33288541

RESUMO

Recent years have provided considerable insights into the dynamic nature of the cell nucleus, which is constantly reorganizing its genome, controlling its size and shape, as well as spatiotemporally orchestrating chromatin remodeling and transcription. Remarkably, it has become clear that the ancient and highly conserved cytoskeletal protein actin plays a crucial part in these processes. However, the underlying mechanisms, regulations, and properties of actin functions inside the nucleus are still not well understood. Here we summarize the diverse and distinct roles of monomeric and filamentous actin as well as the emerging roles for actin dynamics inside the nuclear compartment for genome organization and nuclear architecture.

3.
Curr Opin Cell Biol ; 64: 18-24, 2020 06.
Artigo em Inglês | MEDLINE | ID: mdl-32088545

RESUMO

Actin has essential functions both in the cytoplasm and in the nucleus, where it has been linked to key nuclear processes, from transcription to DNA damage response. The multifunctional nature of actin suggests that the cell must contain mechanisms to accurately control the cellular actin balance. Indeed, recent results have demonstrated that nuclear actin levels fluctuate to regulate the transcriptional activity of the cell and that controlled nuclear actin polymerization is required for transcription activation, cell cycle progression, and DNA repair. Intriguingly, aberrant nuclear actin regulation has been observed, for example, in cancer, signifying the importance of this process for cellular homeostasis. This review discussed the latest research on how nuclear actin is regulated, and how this influences actin-dependent nuclear processes.


Assuntos
Actinas/metabolismo , Núcleo Celular/metabolismo , Animais , Regulação da Expressão Gênica , Genoma , Humanos , Polimerização , Transcrição Genética
4.
Nat Commun ; 11(1): 605, 2020 01 30.
Artigo em Inglês | MEDLINE | ID: mdl-32001718

RESUMO

Techniques of protein regulation, such as conditional gene expression, RNA interference, knock-in and knock-out, lack sufficient spatiotemporal accuracy, while optogenetic tools suffer from non-physiological response due to overexpression artifacts. Here we present a near-infrared light-activatable optogenetic system, which combines the specificity and orthogonality of intrabodies with the spatiotemporal precision of optogenetics. We engineer optically-controlled intrabodies to regulate genomically expressed protein targets and validate the possibility to further multiplex protein regulation via dual-wavelength optogenetic control. We apply this system to regulate cytoskeletal and enzymatic functions of two non-tagged endogenous proteins, actin and RAS GTPase, involved in complex functional networks sensitive to perturbations. The optogenetically-enhanced intrabodies allow fast and reversible regulation of both proteins, as well as simultaneous monitoring of RAS signaling with visible-light biosensors, enabling all-optical approach. Growing number of intrabodies should make their incorporation into optogenetic tools the versatile technology to regulate endogenous targets.


Assuntos
Optogenética , Proteínas/metabolismo , Actinas/metabolismo , Movimento Celular/efeitos da radiação , Núcleo Celular/metabolismo , Núcleo Celular/efeitos da radiação , GTP Fosfo-Hidrolases/metabolismo , Células HeLa , Humanos , Luz , Engenharia de Proteínas
5.
Semin Cell Dev Biol ; 102: 105-112, 2020 06.
Artigo em Inglês | MEDLINE | ID: mdl-31735514

RESUMO

Although best known from its functions in the cytoplasm, actin also localizes to the cell nucleus, where it has been linked to many essential functions from regulation of gene expression to maintenance of genomic integrity. While majority of cytoplasmic functions of actin depend on controlled actin polymerization, in the nucleus both actin monomers and filaments have their own specific roles. Actin monomers are core components of several chromatin remodeling and modifying complexes and can also regulate the activity of specific transcription factors, while actin filaments have been linked to DNA damage response and cell cycle progression. Consequently the balance between monomeric and filamentous actin must be precise controlled also in the nucleus, since their effects are dynamically coupled. In this review, we discuss the recent data on how actin dynamics is regulated within the nucleus and how this influences the different nuclear processes dependent on actin.


Assuntos
Actinas/metabolismo , Núcleo Celular/genética , Núcleo Celular/metabolismo , Expressão Gênica , Genoma/genética , Animais , Humanos
7.
J Cell Sci ; 132(8)2019 04 17.
Artigo em Inglês | MEDLINE | ID: mdl-30890647

RESUMO

In addition to its essential functions within the cytoskeleton, actin also localizes to the cell nucleus, where it is linked to many important nuclear processes from gene expression to maintenance of genomic integrity. However, the molecular mechanisms by which actin operates in the nucleus remain poorly understood. Here, we have used two complementary mass spectrometry (MS) techniques, AP-MS and BioID, to identify binding partners for nuclear actin. Common high-confidence interactions highlight the role of actin in chromatin-remodeling complexes and identify the histone-modifying complex human Ada-Two-A-containing (hATAC) as a novel actin-containing nuclear complex. Actin binds directly to the hATAC subunit KAT14, and modulates its histone acetyl transferase activity in vitro and in cells. Transient interactions detected through BioID link actin to several steps of transcription as well as to RNA processing. Alterations in nuclear actin levels disturb alternative splicing in minigene assays, likely by affecting the transcription elongation rate. This interactome analysis thus identifies both novel direct binding partners and functional roles for nuclear actin, as well as forms a platform for further mechanistic studies on how actin operates during essential nuclear processes.This article has an associated First Person interview with the first author of the paper.


Assuntos
Actinas/metabolismo , Proteínas Adaptadoras de Transdução de Sinal/metabolismo , Núcleo Celular/química , Citoesqueleto/metabolismo , Histona Acetiltransferases/metabolismo , Splicing de RNA , Proteínas Adaptadoras de Transdução de Sinal/genética , Núcleo Celular/metabolismo , Montagem e Desmontagem da Cromatina , Expressão Gênica , Células HeLa , Histona Acetiltransferases/genética , Humanos , Espectrometria de Massas , Ativação Transcricional
8.
iScience ; 9: 63-70, 2018 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-30384134

RESUMO

Actin has been linked to processes spanning the whole gene expression cascade, from regulating specific transcription factors, such as myocardin-related transcription factor, to chromatin remodeling and RNA polymerase function. However, whether actin controls the transcription of only specific genes or has a global role in gene expression has remained elusive. Our genome-wide analysis reveals, for the first time, that actin interacts with essentially all transcribed genes in Drosophila ovaries. Actin co-occupies the majority of gene promoters together with Pol II, and on highly expressed genes, these two proteins also associate with gene bodies. Mechanistically, actin is required for Pol II recruitment to gene bodies, and manipulation of nuclear transport factors for actin leads to the decreased expression of eggshell genes. Collectively, these results uncover a global role for actin in transcription and demonstrate the in vivo importance of balanced nucleocytoplasmic shuttling of actin in the transcriptional control of a developmental process.

9.
EMBO Rep ; 19(2): 290-304, 2018 02.
Artigo em Inglês | MEDLINE | ID: mdl-29330316

RESUMO

Accurate control of macromolecule transport between nucleus and cytoplasm underlines several essential biological processes, including gene expression. According to the canonical model, nuclear import of soluble proteins is based on nuclear localization signals and transport factors. We challenge this view by showing that nuclear localization of the actin-dependent motor protein Myosin-1C (Myo1C) resembles the diffusion-retention mechanism utilized by inner nuclear membrane proteins. We show that Myo1C constantly shuttles in and out of the nucleus and that its nuclear localization does not require soluble factors, but is dependent on phosphoinositide binding. Nuclear import of Myo1C is preceded by its interaction with the endoplasmic reticulum, and phosphoinositide binding is specifically required for nuclear import, but not nuclear retention, of Myo1C. Our results therefore demonstrate, for the first time, that membrane association and binding to nuclear partners is sufficient to drive nuclear localization of also soluble proteins, opening new perspectives to evolution of cellular protein sorting mechanisms.


Assuntos
Miosina Tipo I/metabolismo , Fosfatidilinositóis/metabolismo , Transdução de Sinais , Transporte Ativo do Núcleo Celular , Animais , Núcleo Celular/metabolismo , Cromatina/genética , Cromatina/metabolismo , Citoplasma/metabolismo , Expressão Gênica , Genes Reporter , Humanos , Imuno-Histoquímica , Camundongos , Miosina Tipo I/química , Miosina Tipo I/genética , Sinais de Localização Nuclear/química , Ligação Proteica , Proteínas Recombinantes de Fusão
10.
Nat Cell Biol ; 19(12): 1386-1388, 2017 Nov 29.
Artigo em Inglês | MEDLINE | ID: mdl-29184179

RESUMO

After mitosis, the nucleus must be rebuilt and chromatin decondensed to permit interphase genomic functions, but decondensation mechanisms are poorly understood. Now, the traditional cytoskeletal protein actin is shown to form transient nuclear filaments that are required for chromatin decondensation and nuclear expansion at mitotic exit.


Assuntos
Actinas/metabolismo , Núcleo Celular/metabolismo , Cromatina/metabolismo , Montagem e Desmontagem da Cromatina/fisiologia , Interfase/fisiologia , Mitose/fisiologia , Modelos Biológicos
11.
Biochim Biophys Acta Mol Cell Res ; 1864(10): 1589-1604, 2017 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-28554770

RESUMO

Current models imply that the evolutionarily conserved, actin-binding Ezrin-Radixin-Moesin (ERM) proteins perform their activities at the plasma membrane by anchoring membrane proteins to the cortical actin network. Here we show that beside its cytoplasmic functions, the single ERM protein of Drosophila, Moesin, has a novel role in the nucleus. The activation of transcription by heat shock or hormonal treatment increases the amount of nuclear Moesin, indicating biological function for the protein in the nucleus. The distribution of Moesin in the nucleus suggests a function in transcription and the depletion of mRNA export factors Nup98 or its interacting partner, Rae1, leads to the nuclear accumulation of Moesin, suggesting that the nuclear function of the protein is linked to mRNA export. Moesin localizes to mRNP particles through the interaction with the mRNA export factor PCID2 and knock down of Moesin leads to the accumulation of mRNA in the nucleus. Based on our results we propose that, beyond its well-known, manifold functions in the cytoplasm, the ERM protein of Drosophila is a new, functional component of the nucleus where it participates in mRNA export.


Assuntos
Proteínas de Drosophila/genética , Proteínas dos Microfilamentos/genética , Proteínas Associadas à Matriz Nuclear/genética , Complexo de Proteínas Formadoras de Poros Nucleares/genética , Proteínas de Transporte Nucleocitoplasmático/genética , RNA Mensageiro/genética , Animais , Proteínas do Citoesqueleto/genética , Proteínas do Citoesqueleto/metabolismo , Proteínas de Drosophila/metabolismo , Drosophila melanogaster/genética , Drosophila melanogaster/metabolismo , Proteínas de Membrana/genética , Proteínas dos Microfilamentos/metabolismo , Proteínas Associadas à Matriz Nuclear/metabolismo , Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo , Proteínas de Transporte Nucleocitoplasmático/metabolismo , Fosforilação , Ligação Proteica , Transporte de RNA/genética , RNA Mensageiro/metabolismo , Ribonucleoproteínas/genética
12.
Curr Opin Cell Biol ; 46: 33-38, 2017 06.
Artigo em Inglês | MEDLINE | ID: mdl-28092729

RESUMO

In addition to its essential roles as part of the cytoskeleton, actin has also been linked to many processes in the nucleus. Recent data has demonstrated the presence of both monomeric and polymeric actin in the nucleus, and implied distinct functional roles for these actin pools. Monomeric actin seems to be involved in regulation of gene expression through transcription factors, chromatin regulating complexes and RNA polymerases. In addition to cytoplasmic actin regulators, nuclear proteins, such as emerin, can regulate actin polymerization properties specifically in this compartment. Besides of structural roles, nuclear actin filaments may be required for organizing the nuclear contents and for the maintenance of genomic integrity.


Assuntos
Actinas/metabolismo , Proteínas Nucleares/metabolismo , Actinas/química , Animais , Núcleo Celular/metabolismo , Cromatina/metabolismo , Citoplasma/metabolismo , Humanos , Proteínas Nucleares/química
13.
Handb Exp Pharmacol ; 235: 311-329, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-27316910

RESUMO

Although most people still associate actin mainly with the cytoskeleton, several lines of evidence, with the earliest studies dating back to decades ago, have emphasized the importance of actin also inside the cell nucleus. Actin has been linked to many gene expression processes from gene activation to chromatin remodeling, but also to maintenance of genomic integrity and intranuclear movement of chromosomes and chromosomal loci. Recent advances in visualizing different forms and dynamic properties of nuclear actin have clearly advanced our understanding of the basic concepts by which actin operates in the nucleus. In this chapter we address the different breakthroughs in nuclear actin studies, as well as discuss the regulation nuclear actin and the importance of nuclear actin dynamics in relation to its different nuclear functions. Our aim is to highlight the fact that actin should be considered as an essential component of the cell nucleus, and its nuclear actions should be taken into account also in experiments on cytoplasmic actin networks.


Assuntos
Actinas/fisiologia , Núcleo Celular/química , Citoesqueleto/fisiologia , Actinas/análise , Transporte Ativo do Núcleo Celular , Animais , Núcleo Celular/metabolismo , Montagem e Desmontagem da Cromatina , RNA Polimerases Dirigidas por DNA/genética , Expressão Gênica , Humanos , Ativação Transcricional
14.
Sci Rep ; 6: 33893, 2016 09 21.
Artigo em Inglês | MEDLINE | ID: mdl-27650314

RESUMO

The actin cytoskeleton is a classic biomechanical mediator of cell migration. While it is known that actin also shuttles in and out of the nucleus, its functions within this compartment remain poorly understood. In this study, we investigated how nuclear actin regulates keratinocyte gene expression and cell behavior. Gene expression profiling of normal HaCaT keratinocytes compared to HaCaTs over-expressing wild-type ß-actin or ß-actin tagged with a nuclear localization sequence (NLS-actin), identified multiple adhesive and cytoskeletal genes, such as MYL9, ITGB1, and VCL, which were significantly down-regulated in keratinocytes with high levels of nuclear actin. In addition, genes associated with transcriptional regulation and apoptosis were up-regulated in cells over expressing NLS-actin. Functionally, accumulation of actin in the nucleus altered cytoskeletal and focal adhesion organization and inhibited cell motility. Exclusion of endogenous actin from the nucleus by knocking down Importin 9 reversed this phenotype and enhanced cell migration. Based on these findings, we conclude that the level of actin in the nucleus is a transcriptional regulator for tuning keratinocyte migration.


Assuntos
Actinas/metabolismo , Moléculas de Adesão Celular/biossíntese , Citoesqueleto/metabolismo , Regulação da Expressão Gênica/fisiologia , Queratinócitos/metabolismo , Proteínas Nucleares/metabolismo , Transcrição Genética/fisiologia , Actinas/genética , Moléculas de Adesão Celular/genética , Citoesqueleto/genética , Células HeLa , Humanos , Queratinócitos/citologia , Proteínas Nucleares/genética
15.
J Cell Sci ; 128(13): 2388-400, 2015 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-26021350

RESUMO

Nuclear actin plays an important role in many processes that regulate gene expression. Cytoplasmic actin dynamics are tightly controlled by numerous actin-binding proteins, but regulation of nuclear actin has remained unclear. Here, we performed a genome-wide RNA interference (RNAi) screen in Drosophila cells to identify proteins that influence either nuclear polymerization or import of actin. We validate 19 factors as specific hits, and show that Chinmo (known as Bach2 in mammals), SNF4Aγ (Prkag1 in mammals) and Rab18 play a role in nuclear localization of actin in both fly and mammalian cells. We identify several new regulators of cofilin activity, and characterize modulators of both cofilin kinases and phosphatase. For example, Chinmo/Bach2, which regulates nuclear actin levels also in vivo, maintains active cofilin by repressing the expression of the kinase Cdi (Tesk in mammals). Finally, we show that Nup98 and lamin are candidates for regulating nuclear actin polymerization. Our screen therefore reveals new aspects of actin regulation and links nuclear actin to many cellular processes.


Assuntos
Fatores de Despolimerização de Actina/metabolismo , Núcleo Celular/metabolismo , Testes Genéticos , Genoma , Interferência de RNA , Actinas , Animais , Sequência Conservada , Proteínas de Drosophila/metabolismo , Drosophila melanogaster/genética , Evolução Molecular , Camundongos , Modelos Biológicos , Proteínas do Tecido Nervoso/metabolismo , Fosforilação , Polimerização , Proteínas Serina-Treonina Quinases/metabolismo
16.
Nat Commun ; 6: 5978, 2015 Jan 14.
Artigo em Inglês | MEDLINE | ID: mdl-25585691

RESUMO

Controlled transport of macromolecules between the cytoplasm and nucleus is essential for homeostatic regulation of cellular functions. For instance, gene expression entails coordinated nuclear import of transcriptional regulators to activate transcription and nuclear export of the resulting messenger RNAs for cytoplasmic translation. Here we link these two processes by reporting a novel role for the mRNA export factor Ddx19/Dbp5 in nuclear import of MKL1, the signal-responsive transcriptional activator of SRF. We show that Ddx19 is not a general nuclear import factor, and that its specific effect on MKL1 nuclear import is separate from its role in mRNA export. Both helicase and nuclear pore-binding activities of Ddx19 are dispensable for MKL1 nuclear import, but RNA binding is required. Mechanistically, Ddx19 operates by modulating the conformation of MKL1, which affects its interaction with Importin-ß for efficient nuclear import. Thus, Ddx19 participates in mRNA export, translation and nuclear import of a key transcriptional regulator.


Assuntos
Transporte Ativo do Núcleo Celular , RNA Helicases DEAD-box/metabolismo , Proteínas de Transporte Nucleocitoplasmático/metabolismo , Transativadores/metabolismo , Animais , Núcleo Celular/metabolismo , Citoplasma/metabolismo , Células HeLa , Homeostase , Humanos , Camundongos , Microscopia de Fluorescência , Células NIH 3T3 , Ligação Proteica , Conformação Proteica , RNA/metabolismo , beta Carioferinas/metabolismo
17.
Dev Cell ; 28(5): 588-602, 2014 Mar 10.
Artigo em Inglês | MEDLINE | ID: mdl-24636260

RESUMO

Epithelial reorganization involves coordinated changes in cell shapes and movements. This restructuring occurs during formation of placodes, ectodermal thickenings that initiate the morphogenesis of epithelial organs including hair, mammary gland, and tooth. Signaling pathways in ectodermal placode formation are well known, but the cellular mechanisms have remained ill defined. We established imaging methodology for live visualization of embryonic skin explants during the first wave of hair placode formation. We found that the vast majority of placodal cells were nonproliferative throughout morphogenesis. We show that cell compaction and centripetal migration are the main cellular mechanisms associated with hair placode morphogenesis and that inhibition of actin remodeling suppresses placode formation. Stimulation of both ectodysplasin/NF-κB and Wnt/ß-catenin signaling increased cell motility and the number of cells committed to placodal fate. Thus, cell fate choices and morphogenetic events are controlled by the same molecular pathways, providing the framework for coordination of these two processes.


Assuntos
Movimento Celular , Proliferação de Células , Embrião de Mamíferos/citologia , Folículo Piloso/citologia , Queratinas/fisiologia , Morfogênese/fisiologia , Animais , Western Blotting , Ciclo Celular , Ectodisplasinas/fisiologia , Embrião de Mamíferos/metabolismo , Feminino , Proteínas de Fluorescência Verde/genética , Proteínas de Fluorescência Verde/metabolismo , Folículo Piloso/embriologia , Folículo Piloso/metabolismo , Processamento de Imagem Assistida por Computador , Camundongos , Camundongos Transgênicos , Microscopia Confocal , Microscopia de Fluorescência , NF-kappa B/metabolismo , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Proteínas Wnt/metabolismo , beta Catenina/metabolismo
18.
Small GTPases ; 5: e27539, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-24603113

RESUMO

Actin cytoskeleton is one of the main targets of Rho GTPases, which act as molecular switches on many signaling pathways. During the past decade, actin has emerged as an important regulator of gene expression. Nuclear actin plays a key role in transcription, chromatin remodeling, and pre-mRNA processing. In addition, the "status" of the actin cytoskeleton is used as a signaling intermediate by at least the MKL1-SRF and Hippo-pathways, which culminate in the transcriptional regulation of cytoskeletal and growth-promoting genes, respectively. Rho GTPases may therefore regulate gene expression by controlling either cytoplasmic or nuclear actin dynamics. Although the regulation of nuclear actin polymerization is still poorly understood, many actin-binding proteins, which are downstream effectors of Rho, are found in the nuclear compartment. In this review, we discuss the possible mechanisms and key proteins that may mediate the transcriptional regulation by Rho GTPases through actin.


Assuntos
Actinas/metabolismo , Proteínas dos Microfilamentos/metabolismo , Proteínas rho de Ligação ao GTP/metabolismo , Citoesqueleto de Actina , Actinas/genética , Núcleo Celular/metabolismo , Expressão Gênica , Humanos , Proteínas dos Microfilamentos/genética , Proteínas Serina-Treonina Quinases/metabolismo , Transdução de Sinais , Proteínas rho de Ligação ao GTP/genética
19.
Mol Biol Cell ; 25(7): 1111-26, 2014 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-24523293

RESUMO

The endoplasmic reticulum (ER) comprises a dynamic three-dimensional (3D) network with diverse structural and functional domains. Proper ER operation requires an intricate balance within and between dynamics, morphology, and functions, but how these processes are coupled in cells has been unclear. Using live-cell imaging and 3D electron microscopy, we identify a specific subset of actin filaments localizing to polygons defined by ER sheets and tubules and describe a role for these actin arrays in ER sheet persistence and, thereby, in maintenance of the characteristic network architecture by showing that actin depolymerization leads to increased sheet fluctuation and transformations and results in small and less abundant sheet remnants and a defective ER network distribution. Furthermore, we identify myosin 1c localizing to the ER-associated actin filament arrays and reveal a novel role for myosin 1c in regulating these actin structures, as myosin 1c manipulations lead to loss of the actin filaments and to similar ER phenotype as observed after actin depolymerization. We propose that ER-associated actin filaments have a role in ER sheet persistence regulation and thus support the maintenance of sheets as a stationary subdomain of the dynamic ER network.


Assuntos
Citoesqueleto de Actina/metabolismo , Retículo Endoplasmático/metabolismo , Miosina Tipo I/metabolismo , Actinas/metabolismo , Linhagem Celular Tumoral , Humanos , Microtúbulos/metabolismo , Miosina Tipo I/química , Fenótipo , Polimerização , Ligação Proteica , Estrutura Terciária de Proteína , Relação Estrutura-Atividade
20.
Nat Rev Mol Cell Biol ; 14(11): 693-7, 2013 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-24088744

RESUMO

The paradigm states that cytoplasmic actin operates as filaments and nuclear actin is mainly monomeric, acting as a scaffold in transcription complexes. However, why should a powerful function of actin, namely polymerization, not be used in the nucleus? Recent progress in the field forces us to rethink this issue, as many actin filament assembly proteins have been linked to nuclear functions and new experimental approaches have provided the first direct visualizations of polymerized nuclear actin.


Assuntos
Citoesqueleto de Actina/metabolismo , Núcleo Celular/metabolismo , Animais , Humanos , Modelos Biológicos , Polimerização
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