Elongation of cytoplasmic processes during gametic mating: Models for actin-based motility

1985 ◽  
Vol 63 (6) ◽  
pp. 599-607 ◽  
Author(s):  
Patricia A. Detmers
Keyword(s):  
Actin Cytoskeleton ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Cellular Motility ◽  
Intracellular Signals ◽  
Intracellular Ca ◽  
Cytoplasmic Processes ◽  
Uniform Polarity

The acrosomal processes of Thyone and Limulus sperm and the fertilization tubule of mt+ gametes of Chlamydomonas are interesting models for actin-based motility. Each is a long thin process that elongates rapidly and contains a core of actin filaments having uniform polarity: arrowheads formed by myosin subfragments point toward the base of the processes. In Limulus, directed outgrowth of the acrosomal process is achieved by a rearrangement in the packing of superhelically coiled actin filaments that form during spermatogenesis. In contrast, outgrowth of the acrosomal process in Thyone and the fertilization tubule in Chlamydomonas is accompanied by actin polymerization. Both Thyone and Chlamydomonas possess structures, the actomere and the doublet zone, respectively, that serve as microfilament organizing centers, nucleating actin polymerization and defining the polarity of the growing filaments. Alkalinization of the cytoplasm may promote polymerization of actin in Thyone, whereas an apparent rise in the intracellular Ca2+ concentration is associated with the transmission of intracellular signals during mating in Chlamydomonas. Further examination of these three actin-based motile systems should provide new insights into the assembly of the actin cytoskeleton, a process critical for many forms of nonmuscle cellular motility.

scholarly journals Actin dynamics rapidly reset chemoattractant receptor sensitivity following adaptation in neutrophils

2013 ◽  
Vol 368 (1629) ◽  
pp. 20130008 ◽  
Author(s):  
Sheel N. Dandekar ◽  
Jason S. Park ◽  
Grace E. Peng ◽  
James J. Onuffer ◽  
Wendell A. Lim ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Actin Polymerization ◽  
Innate Immune ◽  
Actin Dynamics ◽  
Receptor Desensitization ◽  
Receptor Sensitivity ◽  
Reciprocal Interactions ◽  
Intracellular Signals ◽  
Spatial Differences

Neutrophils are cells of the innate immune system that hunt and kill pathogens using directed migration. This process, known as chemotaxis, requires the regulation of actin polymerization downstream of chemoattractant receptors. Reciprocal interactions between actin and intracellular signals are thought to underlie many of the sophisticated signal processing capabilities of the chemotactic cascade including adaptation, amplification and long-range inhibition. However, with existing tools, it has been difficult to discern actin's role in these processes. Most studies investigating the role of the actin cytoskeleton have primarily relied on actin-depolymerizing agents, which not only block new actin polymerization but also destroy the existing cytoskeleton. We recently developed a combination of pharmacological inhibitors that stabilizes the existing actin cytoskeleton by inhibiting actin polymerization, depolymerization and myosin-based rearrangements; we refer to these processes collectively as actin dynamics. Here, we investigated how actin dynamics influence multiple signalling responses (PI3K lipid products, calcium and Pak phosphorylation) following acute agonist addition or during desensitization. We find that stabilized actin polymer extends the period of receptor desensitization following agonist binding and that actin dynamics rapidly reset receptors from this desensitized state. Spatial differences in actin dynamics may underlie front/back differences in agonist sensitivity in neutrophils.

scholarly journals Mechanisms of actin disassembly

2013 ◽  
Vol 24 (15) ◽  
pp. 2299-2302 ◽  
Author(s):  
William Brieher
Keyword(s):  
Actin Cytoskeleton ◽  
Cell Motility ◽  
Actin Filament ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Actin Depolymerization ◽  
Filament Dynamics ◽  
Physiological Demands ◽  
In Cells

The actin cytoskeleton is constantly assembling and disassembling. Cells harness the energy of these turnover dynamics to drive cell motility and organize cytoplasm. Although much is known about how cells control actin polymerization, we do not understand how actin filaments depolymerize inside cells. I briefly describe how the combination of imaging actin filament dynamics in cells and using in vitro biochemistry progressively altered our views of actin depolymerization. I describe why I do not think that the prevailing model of actin filament turnover—cofilin-mediated actin filament severing—can account for actin filament disassembly detected in cells. Finally, I speculate that cells might be able to tune the mechanism of actin depolymerization to meet physiological demands and selectively control the stabilities of different actin arrays.

Actin and the coordination of protrusion, attachment and retraction in cell crawling

1996 ◽  
Vol 16 (5) ◽  
pp. 351-368 ◽  
Author(s):  
J. Victor Small ◽  
Kurt Anderson ◽  
Klemens Rottner
Keyword(s):  
Actin Cytoskeleton ◽  
Actin Filament ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
The Other ◽  
Coordination Mechanism ◽  
Over Expression ◽  
Cell Crawling ◽  
Cell Front ◽  
A Cell

To crawl over a substrate a cell must first protrude in front, establish new attachments to the substrate and then retract its rear. Protrusion and retraction utilise different subcompartments of the actin cytoskeleton and operate by different mechanisms, one involving actin polymerization and the other myosin-based contraction. Using as examples the rapidly locomoting keratocyte and the slowly moving fibroblast we illustrate how over expression of one or the other actin subcompartments leads to the observed differences in motility. We also propose, that despite these differences there is a common coordination mechanism underlying the genesis of the actin cytoskeleton that involves the nucleation of actin filaments at the protruding cell front, in the lamellipodium, and the relocation of these filaments, via polymerization and flow, to the more posterior actin filament compartments.

scholarly journals A Modified Actin (Gly65Val Substitution) Expressed in Cotton Disrupts Polymerization of Actin Filaments Leading to the Phenotype of Ligon Lintless-1 (Li1) Mutant

2021 ◽  
Vol 22 (6) ◽  
pp. 3000
Author(s):  
Yuefen Cao ◽  
Hui Huang ◽  
Yanjun Yu ◽  
Huaqin Dai ◽  
Huanfeng Hao ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Actin Filaments ◽  
Textile Industry ◽  
Actin Polymerization ◽  
Natural Fibers ◽  
Wild Type ◽  
Over Expression ◽  
High Resolution Mapping ◽  
In The Wild ◽  
Resolution Mapping

Dynamic remodeling of the actin cytoskeleton plays a central role in the elongation of cotton fibers, which are the most important natural fibers in the global textile industry. Here, a high-resolution mapping approach combined with comparative sequencing and a transgenic method revealed that a G65V substitution in the cotton actin Gh_D04G0865 (GhACT17D in the wild-type) is responsible for the Gossypium hirsutum Ligon lintless-1 (Li1) mutant (GhACT17DM). In the mutant GhACT17DM from Li1 plant, Gly65 is substituted with valine on the lip of the nucleotide-binding domain of GhACT17D, which probably affects the polymerization of F-actin. Over-expression of GhACT17DM, but not GhACT17D, driven by either a CaMV35 promoter or a fiber-specific promoter in cotton produced a Li1-like phenotype. Compared with the wild-type control, actin filaments in Li1 fibers showed higher growth and shrinkage rates, decreased filament skewness and parallelness, and increased filament density. Taken together, our results indicate that the incorporation of GhACT17DM during actin polymerization disrupts the establishment and dynamics of the actin cytoskeleton, resulting in defective fiber elongation and the overall dwarf and twisted phenotype of the Li1 mutant.

scholarly journals A mitochondria-anchored isoform of the actin-nucleating spire protein regulates mitochondrial division

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Uri Manor ◽  
Sadie Bartholomew ◽  
Gonen Golani ◽  
Eric Christenson ◽  
Michael Kozlov ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Actin Assembly ◽  
Mitochondrial Division

Mitochondrial division, essential for survival in mammals, is enhanced by an inter-organellar process involving ER tubules encircling and constricting mitochondria. The force for constriction is thought to involve actin polymerization by the ER-anchored isoform of the formin protein inverted formin 2 (INF2). Unknown is the mechanism triggering INF2-mediated actin polymerization at ER-mitochondria intersections. We show that a novel isoform of the formin-binding, actin-nucleating protein Spire, Spire1C, localizes to mitochondria and directly links mitochondria to the actin cytoskeleton and the ER. Spire1C binds INF2 and promotes actin assembly on mitochondrial surfaces. Disrupting either Spire1C actin- or formin-binding activities reduces mitochondrial constriction and division. We propose Spire1C cooperates with INF2 to regulate actin assembly at ER-mitochondrial contacts. Simulations support this model's feasibility and demonstrate polymerizing actin filaments can induce mitochondrial constriction. Thus, Spire1C is optimally positioned to serve as a molecular hub that links mitochondria to actin and the ER for regulation of mitochondrial division.

scholarly journals Elongation of the fertilization tubule in Chlamydomonas: new observations on the core microfilaments and the effect of transient intracellular signals on their structural integrity.

1983 ◽  
Vol 97 (2) ◽  
pp. 522-532 ◽  
Author(s):  
P A Detmers ◽  
U W Goodenough ◽  
J Condeelis
Keyword(s):  
Mating Type ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Time Course ◽  
Structural Integrity ◽  
Cytochalasin D ◽  
Ultrastructural Observation ◽  
Intracellular Signals ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

Experimental manipulations of gametes of Chlamydomonas reinhardi and ultrastructural observation were used to examine the composition of the microfilaments in the fertilization tubule, their probable mode of formation, and their interaction with intracellular signals. Decoration with myosin subfragment-1 was used to demonstrate that the microfilaments in the fertilization tubule were actin filaments having uniform polarity: Myosin subfragment-1 arrowheads pointed away from the membrane at the tip of the process. Filaments were attached to the cone-shaped "doublet zone" at the base of the process by their pointed ends. Discrete attachment sites for filaments on the surface of the doublet zone were seen in stereo view. To test whether actin polymerization might accompany elongation of the fertilization tubule, mating gametes were exposed to cytochalasin D in an attempt to block actin polymerization. Treatment of mating type "plus" gametes with cytochalasin D prior to and during mating inhibited the appearance of actin filaments in fertilization tubules, suppressed fertilization tubule outgrowth, and lowered mating efficiency from 90 to 15%. The role of signals generated by flagellar adhesion in maintaining the structural integrity of the microfilament-doublet zone complex was examined by correlating flagellar disadhesion with the kinetics of breakdown of the complex. In zygotes, where flagellar disadhesion occurred after cell fusion, the complex disassembled within 3 h after mating. In gametes that had been agglutinated by isolated mating type "minus" flagella, microfilaments and fertilization tubules progressively disassembled over a 3-h time course following flagellar disadhesion. Disassembly of microfilaments was inhibited by maintaining flagellar agglutination, suggesting that signals generated by flagellar adhesion were necessary to maintain microfilaments intact.

scholarly journals EVL and MIM/MTSS1 regulate actin cytoskeletal remodeling to promote dendritic filopodia in developing neurons

2021 ◽  
Author(s):  
Sara Shannon Parker ◽  
Kenneth Tran Ly ◽  
Adam D Grant ◽  
Ashley M Wang ◽  
James D Parker ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Dendritic Spines ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Synapse Formation ◽  
Synaptic Connectivity ◽  
Critical Function ◽  
Actin Remodeling ◽  
Cytoskeletal Remodeling ◽  
Developing Neurons

Dendritic spines are the postsynaptic compartment of a functional neuronal synapse, and are critical for synaptic connectivity and plasticity. The developmental precursor to dendritic spines, dendritic filopodia, are highly motile protrusions that facilitate synapse formation by sampling the environment for suitable axon partners during development and learning. Despite the significance of the actin cytoskeleton in driving these protrusions, the actin remodeling factors involved in this process are not fully characterized. In this work, we identify a critical function for the Ena/VASP protein EVL in the regulation of dendritic filopodia. Amongst the Ena/VASP proteins, EVL is uniquely required for the characteristic morphology and dynamics of dendritic filopodia. Using a combination of genetic and optogenetic manipulations, we demonstrate that EVL promotes protrusive motility through membrane-direct actin polymerization at dendritic filopodia tips. EVL forms a complex at nascent protrusions and dendritic filopodia tips with MIM/MTSS1, an I-BAR protein recently discovered to be important for initiation of dendritic filopodia. We propose a model in which EVL cooperates with MIM to elongate and coalesce branched actin filaments, establishing the dynamic lamellipodia-like architecture of dendritic filopodia in developing neurons.

scholarly journals Cofilin, But Not Profilin, Is Required for Myosin-I-Induced Actin Polymerization and the Endocytic Uptake in Yeast

2002 ◽  
Vol 13 (11) ◽  
pp. 4074-4087 ◽  
Author(s):  
Fatima-Zahra Idrissi ◽  
Bianka L. Wolf ◽  
M. Isabel Geli
Keyword(s):  
Plasma Membrane ◽  
Fluorescence Microscopy ◽  
Actin Cytoskeleton ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Cortical Actin ◽  
Myosin I ◽  
Robust Evidence

Mutations in the budding yeast myosins-I (MYO3 andMYO5) cause defects in the actin cytoskeleton and in the endocytic uptake. Robust evidence also indicates that these proteins induce Arp2/3-dependent actin polymerization. Consistently, we have recently demonstrated, using fluorescence microscopy, that Myo5p is able to induce cytosol-dependent actin polymerization on the surface of Sepharose beads. Strikingly, we now observed that, at short incubation times, Myo5p induced the formation of actin foci that resembled the yeast cortical actin patches, a plasma membrane-associated structure that might be involved in the endocytic uptake. Analysis of the machinery required for the formation of the Myo5p-induced actin patches in vitro demonstrated that the Arp2/3 complex was necessary but not sufficient in the assay. In addition, we found that cofilin was directly involved in the process. Strikingly though, the cofilin requirement seemed to be independent of its ability to disassemble actin filaments and profilin, a protein that closely cooperates with cofilin to maintain a rapid actin filament turnover, was not needed in the assay. In agreement with these observations, we found that like the Arp2/3 complex and the myosins-I, cofilin was essential for the endocytic uptake in vivo, whereas profilin was dispensable.

scholarly journals Dephosphorylated synapsin I anchors synaptic vesicles to actin cytoskeleton: an analysis by videomicroscopy.

1995 ◽  
Vol 128 (5) ◽  
pp. 905-912 ◽  
Author(s):  
P E Ceccaldi ◽  
F Grohovaz ◽  
F Benfenati ◽  
E Chieregatti ◽  
P Greengard ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Synaptic Vesicle ◽  
Nerve Terminal ◽  
Actin Filaments ◽  
Neurotransmitter Release ◽  
Synaptic Vesicles ◽  
Actin Polymerization ◽  
Synapsin I ◽  
Cam Kinase Ii ◽  
Cam Kinase

Synapsin I is a synaptic vesicle-associated protein which inhibits neurotransmitter release, an effect which is abolished upon its phosphorylation by Ca2+/calmodulin-dependent protein kinase II (CaM kinase II). Based on indirect evidence, it was suggested that this effect on neurotransmitter release may be achieved by the reversible anchoring of synaptic vesicles to the actin cytoskeleton of the nerve terminal. Using video-enhanced microscopy, we have now obtained experimental evidence in support of this model: the presence of dephosphorylated synapsin I is necessary for synaptic vesicles to bind actin; synapsin I is able to promote actin polymerization and bundling of actin filaments in the presence of synaptic vesicles; the ability to cross-link synaptic vesicles and actin is specific for synapsin I and is not shared by other basic proteins; the cross-linking between synaptic vesicles and actin is specific for the membrane of synaptic vesicles and does not reflect either a non-specific binding of membranes to the highly surface active synapsin I molecule or trapping of vesicles within the thick bundles of actin filaments; the formation of the ternary complex is virtually abolished when synapsin I is phosphorylated by CaM kinase II. The data indicate that synapsin I markedly affects synaptic vesicle traffic and cytoskeleton assembly in the nerve terminal and provide a molecular basis for the ability of synapsin I to regulate the availability of synaptic vesicles for exocytosis and thereby the efficiency of neurotransmitter release.

scholarly journals Dynamic cortical actin remodeling by ERM proteins controls BCR microcluster organization and integrity

2011 ◽  
Vol 208 (5) ◽  
pp. 1055-1068 ◽  
Author(s):  
Bebhinn Treanor ◽  
David Depoil ◽  
Andreas Bruckbauer ◽  
Facundo D. Batista
Keyword(s):  
Actin Cytoskeleton ◽  
B Cell ◽  
Protein Function ◽  
Actin Polymerization ◽  
Lymphocyte Activation ◽  
Dominant Negative ◽  
Temporary Increase ◽  
Cortical Actin ◽  
Erm Proteins ◽  
Diffusion Dynamics

Signaling microclusters are a common feature of lymphocyte activation. However, the mechanisms controlling the size and organization of these discrete structures are poorly understood. The Ezrin-Radixin-Moesin (ERM) proteins, which link plasma membrane proteins with the actin cytoskeleton and regulate the steady-state diffusion dynamics of the B cell receptor (BCR), are transiently dephosphorylated upon antigen receptor stimulation. In this study, we show that the ERM proteins ezrin and moesin influence the organization and integrity of BCR microclusters. BCR-driven inactivation of ERM proteins is accompanied by a temporary increase in BCR diffusion, followed by BCR immobilization. Disruption of ERM protein function using dominant-negative or constitutively active ezrin constructs or knockdown of ezrin and moesin expression quantitatively and qualitatively alters BCR microcluster formation, antigen aggregation, and downstream BCR signal transduction. Chemical inhibition of actin polymerization also altered the structure and integrity of BCR microclusters. Together, these findings highlight a crucial role for the cortical actin cytoskeleton during B cell spreading and microcluster formation and function.

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