Effects of latrunculin A on the relocation of sperm IZUMO1 during gamete interaction in mouse

Abstract During their differentiation epidermal cells of Drosophila form a rich variety of polarized structures. These include the epidermal hairs that decorate much of the adult cuticular surface, the shafts of the bristle sense organs, the lateral extensions of the arista, and the larval denticles. These cuticular structures are produced by cytoskeletal-mediated outgrowths of epidermal cells. Mutations in the tricornered gene result in the splitting or branching of all of these structures. Thus, tricornered function appears to be important for maintaining the integrity of the outgrowths. tricornered mutations however do not have major effects on the growth or shape of these cellular extensions. Inhibiting actin polymerization in differentiating cells by cytochalasin D or latrunculin A treatment also induces the splitting of hairs and bristles, suggesting that the actin cytoskeleton might be a target of tricornered. However, the drugs also result in short, fat, and occasionally malformed hairs and bristles. The data suggest that the function of the actin cytoskeleton is important for maintaining the integrity of cellular extensions as well as their growth and shape. Thus, if tricornered causes the splitting of cellular extensions by interacting with the actin cytoskeleton it likely does so in a subtle way. Consistent with this possibility we found that a weak tricornered mutant is hypersensitive to cytochalasin D. We have cloned the tricornered gene and found that it encodes the Drosophila NDR kinase. This is a conserved ser/thr protein kinase found in Caenorhabditis elegans and humans that is related to a number of kinases that have been found to be important in controlling cell structure and proliferation.

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Structures and absolute configurations of the marine toxins, latrunculin A and laulimalide

Tetrahedron Letters ◽

10.1016/0040-4039(95)02113-2 ◽

1996 ◽

Vol 37 (2) ◽

pp. 159-162 ◽

Cited By ~ 79

Author(s):

Charles W. Jefford ◽

Gérald Bernardinelli ◽

Jun-ichi Tanaka ◽

Tatsuo Higa

Keyword(s):

Marine Toxins ◽

Latrunculin A

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Counterregulation of clathrin-mediated endocytosis by the actin and microtubular cytoskeleton in human neutrophils

AJP Cell Physiology ◽

10.1152/ajpcell.00454.2008 ◽

2009 ◽

Vol 296 (4) ◽

pp. C857-C867 ◽

Cited By ~ 20

Author(s):

Silvia M. Uriarte ◽

Neelakshi R. Jog ◽

Gregory C. Luerman ◽

Samrath Bhimani ◽

Richard A. Ward ◽

...

Keyword(s):

Plasma Membrane ◽

Actin Cytoskeleton ◽

Human Neutrophils ◽

Functional Responses ◽

Membrane Expression ◽

Granule Exocytosis ◽

Plasma Membrane Expression ◽

Microtubular Cytoskeleton ◽

Latrunculin A ◽

Azurophil Granule

We have recently reported that disruption of the actin cytoskeleton enhanced N-formylmethionyl-leucyl-phenylalanine (fMLP)-stimulated granule exocytosis in human neutrophils but decreased plasma membrane expression of complement receptor 1 (CR1), a marker of secretory vesicles. The present study was initiated to determine if reduced CR1 expression was due to fMLP-stimulated endocytosis, to determine the mechanism of this endocytosis, and to examine its impact on neutrophil functional responses. Stimulation of neutrophils with fMLP or ionomycin in the presence of latrunculin A resulted in the uptake of Alexa fluor 488-labeled albumin and transferrin and reduced plasma membrane expression of CR1. These effects were prevented by preincubation of the cells with sucrose, chlorpromazine, or monodansylcadaverine (MDC), inhibitors of clathrin-mediated endocytosis. Sucrose, chlorpromazine, and MDC also significantly inhibited fMLP- and ionomycin-stimulated specific and azurophil granule exocytosis. Disruption of microtubules with nocodazole inhibited endocytosis and azurophil granule exocytosis stimulated by fMLP in the presence of latrunculin A. Pharmacological inhibition of phosphatidylinositol 3-kinase, ERK1/2, and PKC significantly reduced fMLP-stimulated transferrin uptake in the presence of latrunculin A. Blockade of clathrin-mediated endocytosis had no significant effect on fMLP-stimulated phosphorylation of ERK1/2 in neutrophils pretreated with latrunculin A. From these data, we conclude that the actin cytoskeleton functions to limit microtubule-dependent, clathrin-mediated endocytosis in stimulated human neutrophils. The limitation of clathrin-mediated endocytosis by actin regulates the extent of both specific and azurophilic granule exocytosis.

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Improved Development of Somatic Cell Cloned Mouse Embryos by Vitamin C and Latrunculin A

PLoS ONE ◽

10.1371/journal.pone.0120033 ◽

2015 ◽

Vol 10 (3) ◽

pp. e0120033 ◽

Cited By ~ 22

Author(s):

Anna Mallol ◽

Josep Santaló ◽

Elena Ibáñez

Keyword(s):

Vitamin C ◽

Somatic Cell ◽

Mouse Embryos ◽

Latrunculin A

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Matroclinic Haploidy and Gamete Interaction in Maize

Russian Journal of Genetics ◽

10.1134/s1022795418100058 ◽

2018 ◽

Vol 54 (10) ◽

pp. 1137-1141 ◽

Cited By ~ 1

Author(s):

M. I. Chumakov

Keyword(s):

Gamete Interaction

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Latex production with depolymerizing compounds of actin cytoskeleton in rubber trees

Pesquisa Agropecuária Brasileira ◽

10.1590/s0100-204x2008000200018 ◽

2008 ◽

Vol 43 (2) ◽

pp. 275-279 ◽

Cited By ~ 1

Author(s):

Gao Zheng-Quan ◽

Meng Chun-Xiao ◽

Ye Nai-Hao

Keyword(s):

Actin Cytoskeleton ◽

Potassium Iodide ◽

Hevea Brasiliensis ◽

Total Solid ◽

Inorganic Phosphorus ◽

Latrunculin A ◽

Tapping Panel Dryness ◽

Latex Production

The objective of this work was to assess stimulated latex flow from rubber trees (Hevea brasiliensis) with saturated macrolide (latrunculin A), 1, 5, and 10% potassium iodide in 2% methylcellulose compared with 0.3% ethylene in 2% methylcellulose (check) and 2% methylcellulose (blank). Latex output and contents of pure rubber, total solid, sucrose, inorganic phosphorus, thiol, and Mg2+ were measured. The treatments containing 1% KI or saturated macrolide increased latex yields compared to the blank with 2% methylcellulose alone. The 1% KI or saturated macrolide treatments were equal to that of 0.3% ethylene check treatment. However, 5 and 10% KI were harmful to bark of rubber trees, even caused prolonged tapping panel dryness.

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ChemInform Abstract: Structures and Absolute Configurations of the Marine Toxins, Latrunculin A and Laulimalide.

ChemInform ◽

10.1002/chin.199620212 ◽

2010 ◽

Vol 27 (20) ◽

pp. no-no

Author(s):

C. W. JEFFORD ◽

G. BERNARDINELLI ◽

J. TANAKA ◽

T. HIGA

Keyword(s):

Marine Toxins ◽

Latrunculin A

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Actin and agonist MHC–peptide complex–dependent T cell receptor microclusters as scaffolds for signaling

Journal of Experimental Medicine ◽

10.1084/jem.20051182 ◽

2005 ◽

Vol 202 (8) ◽

pp. 1031-1036 ◽

Cited By ~ 442

Author(s):

Gabriele Campi ◽

Rajat Varma ◽

Michael L. Dustin

Keyword(s):

T Cell ◽

T Cell Receptor ◽

Actin Polymerization ◽

Kinase Inhibitor ◽

Cell Receptor ◽

Intercellular Adhesion Molecule ◽

Cell Contact ◽

Intercellular Adhesion Molecule 1 ◽

Planar Bilayers ◽

Latrunculin A

T cell receptor (TCR) microclusters form within seconds of T cell contact with supported planar bilayers containing intercellular adhesion molecule-1 and agonist major histocompatibility complex (MHC)–peptide complexes, and elevation of cytoplasmic Ca2+ is observed within seconds of the first detectable microclusters. At 0–30 s after contact, TCR microclusters are colocalized with activated forms of Lck, ZAP-70, and the linker for activation of T cells. By 2 min, activated kinases are reduced in the older central microclusters, but are abundant in younger peripheral microclusters. By 5 min, TCR in the central supramolecular activation cluster have reduced activated kinases, whereas faint peripheral TCR microclusters efficiently generated activated Lck and ZAP-70. TCR microcluster formation is resistant to inhibition by Src family kinase inhibitor PP2, but is abrogated by actin polymerization inhibitor latrunculin A. We propose that Src kinase–independent formation of TCR microclusters in response to agonist MHC–peptide provides an actin-dependent scaffold for signal amplification.

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Dual pools of actin at presynaptic terminals

Journal of Neurophysiology ◽

10.1152/jn.00789.2011 ◽

2012 ◽

Vol 107 (12) ◽

pp. 3479-3492 ◽

Cited By ~ 22

Author(s):

Adam Bleckert ◽

Huzefa Photowala ◽

Simon Alford

Keyword(s):

Synaptic Transmission ◽

Synaptic Vesicle ◽

Synaptic Vesicles ◽

Repetitive Stimulation ◽

Filamentous Actin ◽

Cortical Actin ◽

Vesicle Recycling ◽

Latrunculin A ◽

Kinetics Of

We investigated actin's function in vesicle recycling and exocytosis at lamprey synapses and show that FM1-43 puncta and phalloidin-labeled filamentous actin (F-actin) structures are colocalized, yet recycling vesicles are not contained within F-actin clusters. Additionally, phalloidin also labels a plasma membrane-associated cortical actin. Injection of fluorescent G-actin revealed activity-independent dynamic actin incorporation into presynaptic synaptic vesicle clusters but not into cortical actin. Latrunculin-A, which sequesters G-actin, dispersed vesicle-associated actin structures and prevented subsequent labeled G-actin and phalloidin accumulation at presynaptic puncta, yet cortical phalloidin labeling persisted. Dispersal of presynaptic F-actin structures by latrunculin-A did not disrupt vesicle clustering or recycling or alter the amplitude or kinetics of excitatory postsynaptic currents (EPSCs). However, it slightly enhanced release during repetitive stimulation. While dispersal of presynaptic actin puncta with latrunculin-A failed to disperse synaptic vesicles or inhibit synaptic transmission, presynaptic phalloidin injection blocked exocytosis and reduced endocytosis measured by action potential-evoked FM1-43 staining. Furthermore, phalloidin stabilization of only cortical actin following pretreatment with latrunculin-A was sufficient to inhibit synaptic transmission. Conversely, treatment of axons with jasplakinolide, which induces F-actin accumulation but disrupts F-actin structures in vivo, resulted in increased synaptic transmission accompanied by a loss of phalloidin labeling of cortical actin but no loss of actin labeling within vesicle clusters. Marked synaptic deficits seen with phalloidin stabilization of cortical F-actin, in contrast to the minimal effects of disruption of a synaptic vesicle-associated F-actin, led us to conclude that two structurally and functionally distinct pools of actin exist at presynaptic sites.

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