Role Of Actin Research Articles

The role of actin and myosin during spermatogenesis

Spermatogenesis is a transitionary process in which the diploid spermatogonia transform into haploid mature spermatozoa. Actin and myosin have been implicated in various aspects during spermatogenesis. Actin is present in the form of monomer, oligomer and polymer within cells, the latter is called microfilament. There are five actin-containing structures during spermatogenesis, i.e., ectoplasmic specialization, acroplaxome, manchette in mammals, actin cones in Drosophila and acroframosome in Caridean shrimp. They are involved in the shaping and differentiating of spermatids. Along with spermatogenesis, the actin cytoskeletons show active remodeling in this process. Some actin binding or actin regulated proteins have been demonstrated to regulate dynamic changes of the actin-containing structures. Myosin, actin-dependent molecular motor, plays an important role during spermatogenesis, such as involving in acrosome biogenesis, vesicle transport, gene transcription and nuclear shaping. The actin cytoskeleton and actin binding/regulated proteins cooperate to facilitate spermatogenesis. In this review, we summarize the existing knowledge about the cytoskeletal structures consisting of actin, actin binding/regulated proteins and myosin during spermatogenesis.

Role of Actin in Epidermal Cell Differentiation

Role of Actin in Epidermal Cell Differentiation

Role of Actin in Ca2+-induced Epidermal Cells Differentiation

Role of Actin in Ca2+-induced Epidermal Cells Differentiation

Cortical Actin Dynamics Facilitate Early-Stage Centrosome Separation

Proper centrosome separation is a prerequisite for positioning the bipolar spindle. Although studies demonstrate that microtubules (MTs) and their associated motors drive centrosome separation [1], the role of actin in centrosome separation remains less clear. Studies in tissue culture cells indicate that actin- and myosin-based cortical flow is primarily responsible for driving late centrosome separation [2], whereas other studies suggest that actin plays a more passive role by serving as an attachment site for astral MTs to pull centrosomes apart [3-6]. Here we demonstrate that prior to nuclear envelope breakdown (NEB) in Drosophila embryos, proper centrosome separation does not require myosin II but requires dynamic actin rearrangements at the growing edge of the interphase cap. Both Arp2/3- and Formin-mediated actin remodeling are required for separating the centrosome pairs before NEB. The Apc2-Armadillo complex appears to link cap expansion to centrosome separation. In contrast, the mechanisms driving centrosome separation after NEB are independent of the actin cytoskeleton and compensate for earlier separation defects. Our studies show that the dynamics of actin polymerization drive centrosome separation, and this has important implications for centrosome positioning during processes such as cell migration [7, 8], cell polarity maintenance [9, 10], and asymmetric cell division [11, 12].

Two CDC42 paralogues modulate Cryptococcus neoformans thermotolerance and morphogenesis under host physiological conditions

SummaryThe precise regulation of morphogenesis is a key mechanism by which cells respond to a variety of stresses, including those encountered by microbial pathogens in the host. The polarity protein Cdc42 regulates cellular morphogenesis throughout eukaryotes, and we explore the role of Cdc42 proteins in the host survival of the human fungal pathogen Cryptococcus neoformans. Uniquely, C. neoformans has two functional Cdc42 paralogues, Cdc42 and Cdc420. Here we investigate the contribution of each paralogue to resistance to host stress. In contrast to non‐pathogenic model organisms, C. neoformans Cdc42 proteins are not required for viability under non‐stress conditions but are required for resistance to high temperature. The paralogues play differential roles in actin and septin organization and act downstream of C. neoformans Ras1 to regulate its morphogenesis sub‐pathway, but not its effects on mating. Cdc42, and not Cdc420, is upregulated in response to temperature stress and is required for virulence in a murine model of cryptococcosis. The C. neoformans Cdc42 proteins likely perform complementary functions with other Rho‐like GTPases to control cell polarity, septin organization and hyphal transitions that allow survival in the environment and in the host.

Motoring down the microvilli. Focus on “PTH-induced internalization of apical membrane NaPi2a: role of actin and myosin VI”

the kidneys filter 120 ml/min at the renal glomeruli, and two thirds of this ultrafiltrate is reabsorbed in the proximal tubule. To accomplish this high rate of reabsorption, the proximal tubule has a tall brush border formed by densely packed microvilli each with a core of actin filaments bundled

PTH-induced internalization of apical membrane NaPi2a: role of actin and myosin VI

Parathyroid hormone (PTH) plays a critical role in the regulation of renal phosphorous homeostasis by altering the levels of the sodium-phosphate cotransporter NaPi2a in the brush border membrane (BBM) of renal proximal tubular cells. While details of the molecular events of PTH-induced internalization of NaPi2a are emerging, the precise events governing NaPi2a removal from brush border microvilli in response to PTH remain to be fully determined. Here we use a novel application of total internal reflection fluorescence microscopy to examine how PTH induces movement of NaPi2a out of brush border microvilli in living cells in real time. We show that a dynamic actin cytoskeleton is required for NaPi2a removal from the BBM in response to PTH. In addition, we demonstrate that a myosin motor that has previously been shown to be coregulated with NaPi2a, myosin VI, is necessary for PTH-induced removal of NaPi2a from BBM microvilli.

WASP and SCAR/WAVE proteins: the drivers of actin assembly

The actin cytoskeleton plays an essential role in numerous aspects of cell biology, such as cell morphology and motility. Actin's role in these processes is tightly regulated, in particular through the Arp2/3 complex ([Goley and Welch, 2006][1]), a major initiator of actin polymerisation that

Actin-Based Protrusions: Promoters or Inhibitors of Cancer Invasion?

In a recent issue of Cell, Silva and colleagues reported the identification of CYFIP1, a member of the actin-assembly-promoting Scar/WAVE complex, as an invasion suppressor in epithelial cancers. This study challenges ideas about the role of actin in cancer invasion.

Co‐localisation of membranes and actin in growing infected cells of Glycine max root nodules

The root nodule of Glycine max (L.) Merr. is almost spherical at maturity, and its central tissue consists of infected cells filled with numerous symbiosomes containing bacteroids, interspersed with uninfected cells. During the growth of the nodule, the volume of each infected cell and the number of bacteroids per cell increases, and thus abundant membranes are required for the proliferation of symbiosomes. In expanding infected cells, there are areas adjacent to the nucleus that are devoid of bacteroids, but these areas are filled with numerous membranes and actin filaments, surrounded by endoplasmic reticulum membranes, indicating a perinuclear reservoir of newly formed membranes and a role for actin in delivering membranes to proliferating symbiosomes.

Lifeact-mEGFP Reveals a Dynamic Apical F-Actin Network in Tip Growing Plant Cells

BackgroundActin is essential for tip growth in plants. However, imaging actin in live plant cells has heretofore presented challenges. In previous studies, fluorescent probes derived from actin-binding proteins often alter growth, cause actin bundling and fail to resolve actin microfilaments.Methodology/Principal FindingsIn this report we use Lifeact-mEGFP, an actin probe that does not affect the dynamics of actin, to visualize actin in the moss Physcomitrella patens and pollen tubes from Lilium formosanum and Nicotiana tobaccum. Lifeact-mEGFP robustly labels actin microfilaments, particularly in the apex, in both moss protonemata and pollen tubes. Lifeact-mEGFP also labels filamentous actin structures in other moss cell types, including cells of the gametophore.Conclusions/SignificanceLifeact-mEGFP, when expressed at optimal levels does not alter moss protonemal or pollen tube growth. We suggest that Lifeact-mEGFP represents an exciting new versatile probe for further studies of actin's role in tip growing plant cells.

Nuclear actin and actin‐binding proteins in the regulation of transcription and gene expression

Nuclear actin is involved in the transcription of all three RNA polymerases, in chromatin remodeling and in the formation of heterogeneous nuclear ribonucleoprotein complexes, as well as in recruitment of the histone modifier to the active gene. In addition, actin-binding proteins (ABPs) control actin nucleation, bundling, filament capping, fragmentation and monomer availability in the cytoplasm. In recent years, more and more attention has focused on the role of actin and ABPs in the modulation of the subcellular localization of transcriptional regulators. This review focuses on recent developments in the study of transcription and transcriptional regulation by nuclear actin, and the regulation of muscle-specific gene expression, nuclear receptor and transcription complexes by ABPs. Among the ABPs, striated muscle activator of Rho signaling and actin-binding LIM protein regulate actin dynamics and serum response factor-dependent muscle-specific gene expression. Functionally and structurally unrelated cytoplasmic ABPs interact cooperatively with nuclear receptor and regulate its transactivation. Furthermore, ABPs also participate in the formation of transcription complexes.

Inhibition of Tobacco Mosaic Virus Movement by Expression of an Actin-Binding Protein

The tobacco mosaic virus (TMV) movement protein (MP) required for the cell-to-cell spread of viral RNA interacts with the endoplasmic reticulum (ER) as well as with the cytoskeleton during infection. Whereas associations of MP with ER and microtubules have been intensely investigated, research on the role of actin has been rather scarce. We demonstrate that Nicotiana benthamiana plants transgenic for the actin-binding domain 2 of Arabidopsis (Arabidopsis thaliana) fimbrin (AtFIM1) fused to green fluorescent protein (ABD2:GFP) exhibit a dynamic ABD2:GFP-labeled actin cytoskeleton and myosin-dependent Golgi trafficking. These plants also support the movement of TMV. In contrast, both myosin-dependent Golgi trafficking and TMV movement are dominantly inhibited when ABD2:GFP is expressed transiently. Inhibition is mediated through binding of ABD2:GFP to actin filaments, since TMV movement is restored upon disruption of the ABD2:GFP-labeled actin network with latrunculin B. Latrunculin B shows no significant effect on the spread of TMV infection in either wild-type plants or ABD2:GFP transgenic plants under our treatment conditions. We did not observe any binding of MP along the length of actin filaments. Collectively, these observations demonstrate that TMV movement does not require an intact actomyosin system. Nevertheless, actin-binding proteins appear to have the potential to exert control over TMV movement through the inhibition of myosin-associated protein trafficking along the ER membrane.

Coordination of Eukaryotic Translation Elongation Factor 1A (eEF1A) Function in Actin Organization and Translation Elongation by the Guanine Nucleotide Exchange Factor eEF1Bα

Eukaryotic translation elongation factor 1A (eEF1A) both shuttles aminoacyl-tRNA (aa-tRNA) to the ribosome and binds and bundles actin. A single domain of eEF1A is proposed to bind actin, aa-tRNA and the guanine nucleotide exchange factor eEF1Balpha. We show that eEF1Balpha has the ability to disrupt eEF1A-induced actin organization. Mutational analysis of eEF1Balpha F163, which binds in this domain, demonstrates effects on growth, eEF1A binding, nucleotide exchange activity, and cell morphology. These phenotypes can be partially restored by an intragenic W130A mutation. Furthermore, the combination of F163A with the lethal K205A mutation restores viability by drastically reducing eEF1Balpha affinity for eEF1A. This also results in a consistent increase in actin bundling and partially corrected morphology. The consequences of the overlapping functions in this eEF1A domain and its unique differences from the bacterial homologs provide a novel function for eEF1Balpha to balance the dual roles in actin bundling and protein synthesis.

B203 細胞伸展ダイナミクスに与えるアクチン骨格構造の役割 : マイクロパターンによる検討(B2-1 細胞工学・マイクロバイオメカニクス2)

B203 細胞伸展ダイナミクスに与えるアクチン骨格構造の役割 : マイクロパターンによる検討(B2-1 細胞工学・マイクロバイオメカニクス2)

Peptide Nanoparticles Serve as a Powerful Platform for the Immunogenic Display of Poorly Antigenic Actin Determinants

The role of actin in transcription and RNA processing is now widely accepted but the form of nuclear actin remains enigmatic. Monomeric, oligomeric or polymeric forms of actin seem to be involved in nuclear functions. Moreover, uncommon forms of actin such as the "lower dimer" have been observed in vitro. Antibodies have been pivotal in revealing the presence and distribution of different forms of actin in different cellular locations. Because of its high degree of conservation, actin is a poor immunogen and only few specific actin antibodies are available. To unravel the mystery of less common forms of actin, in particular those in the nucleus, we chose to tailor monoclonal antibodies to recognize distinct forms of actin. To increase the immune response, we used a new approach based on peptide nanoparticles, which are designed to mimic an icosahedral virus capsid and allow the repetitive, ordered display of a specific epitope on their surface. Actin sequences representing the highly conserved "hydrophobic loop," which is buried in the filamentous actin filament, were grafted onto the surface of nanoparticles by genetic engineering. After immunization with "loop nanoparticles," a number of monoclonal antibodies were established that bind to the hydrophobic loop both in vitro and in situ. Immunofluorescence studies on cells revealed that filamentous actin filaments were only labeled once the epitope had been exposed. Our studies indicate that self-assembling peptide nanoparticles represent a versatile platform that can easily be customized to present antigenic determinants in repetitive, ordered arrays and elicit an immune response against poor antigens.

Mitosis: New Roles for Myosin-X and Actin at the Spindle

Roles for actin and myosin in positioning mitotic spindles in the cell are well established. A recent study of myosin-X function in early Xenopus embryo mitosis now reports that this unconventional myosin is required for pole integrity and normal spindle length by localizing to poles and exerting pulling forces on actin filaments within the spindle.

S2-03-04: Role of aminopeptidase NPPS in tauopathy

Abstract not available.

S2-03-05: The role of actin and oxidative stress in tau-associated neurodegeneration

S2-03-05: The role of actin and oxidative stress in tau-associated neurodegeneration

Exploitation of cytoplasmic and nuclear actin by baculoviruses

Diverse bacterial and viral pathogens hijack the actin cytoskeleton of host cells to facilitate processes such as attachment, internalization, or spread. Among known pathogens, baculoviruses are unique in their ability to manipulate actin both in the cell cytoplasm and nucleus. We seek to determine how baculoviruses exploit actin to reveal new roles for actin in pathogenesis, and to illuminate the poorly understood function and regulation of nuclear actin. Using time‐lapse microscopy, we find that Autographa californica Multiple Nucleopolyhedrovirus (AcMNPV) undergoes actin‐based motility within the cell cytoplasm. Motility requires p78/83, a viral capsid protein that mimics host WASP proteins and activates actin assembly with the host Arp2/3 complex. As with other pathogens, moving AcMNPV are propelled into surface projections that may function in cell‐to‐cell spread. However, unlike other pathogens, motility also enhances viral collision with the nucleus, enabling translocation into the nucleus, where replication takes place. Once in the nucleus, AcMNPV induces nuclear actin accumulation, and then assembles nuclear actin using p78/83 to activate the host Arp2/3 complex. Nuclear actin assembly by p78/83 and Arp2/3 complex is essential for progeny production. Further study of this novel mode of pathogenesis will likely reveal elusive details about the regulation and function of nuclear actin.