[2] Use of latrunculin-A, an actin monomer-binding drug

Ayscough, Kathryn R.

doi:10.1016/s0076-6879(98)98004-1

Cited by 83 publications

(66 citation statements)

References 16 publications

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“…To examine this hypothesis, the role of actin bundles in the nucleocytoplasmic transport of gag mRNA was studied by using an actin monomerbinding compound, latrunculin-B (LAT-B; Fig. 5), which speci®cally disrupts actin ®lament formation (Ayscough 1998). The compound was added to HeLa cells at 16 h after transfection of pCRRE/DRev and pCG-HA-Rev, and the cells were incubated for another 16 h at 37 8C.…”

Section: Resultsmentioning

confidence: 99%

Rev‐dependent association of the intron‐containing HIV‐1 gag mRNA with the nuclear actin bundles and the inhibition of its nucleocytoplasmic transport by latrunculin‐B

Kimura¹,

Hashimoto²,

Yamamoto

et al. 2000

Genes to Cells

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Section: Resultsmentioning

confidence: 99%

Rev‐dependent association of the intron‐containing HIV‐1 gag mRNA with the nuclear actin bundles and the inhibition of its nucleocytoplasmic transport by latrunculin‐B

Kimura¹,

Hashimoto²,

Yamamoto

et al. 2000

Genes to Cells

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“…First, multiple distinct molecular mechanisms exist to support actin assembly in cells (33,34). Whereas EGFP-CA is predicted to target Arp2/3-mediated actin assembly, drugs, such as cytochalasins and latrunculin, that cap the barbed ends of filaments or sequester G-actin, respectively (35), likely inhibit all these processes indiscriminately. Drug inhibitor studies therefore establish the general requirement for actin integrity to support cadherin function but cannot define specific molecular mechanisms.…”

Section: Discussionmentioning

confidence: 99%

Arp2/3 Activity Is Necessary for Efficient Formation of E-cadherin Adhesive Contacts

Verma

Shewan

Scott

et al. 2004

Journal of Biological Chemistry

141

136

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Classical cadherin adhesion molecules are fundamental determinants of cell-cell recognition that function in cooperation with the actin cytoskeleton. Productive cadherin-based cell recognition is characterized by a distinct morphological process of contact zone extension, where limited initial points of adhesion are progressively expanded into broad zones of contact. We recently demonstrated that E-cadherin ligation recruits the Arp2/3 actin nucleator complex to the plasma membrane in regions where cell contacts are undergoing protrusion and extension. This suggested that Arp2/3 might generate the protrusive forces necessary for cell surfaces to extend upon one another during contact assembly. We tested this hypothesis in mammalian cells by exogenously expressing the CA region of N-WASP. This fragment, which potently inhibits Arp2/3-mediated actin assembly in vitro, also effectively reduced actin assembly at cadherin adhesive contacts. Blocking Arp2/3 activity by this strategy profoundly reduced the ability of cells to extend cadherin adhesive contacts but did not affect cell adhesiveness. These findings demonstrate that Arp2/3 activity is necessary for cells to efficiently extend and assemble cadherin-based adhesive contacts.

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“…Treatment of one-cell embryos with the actin depolymerizer latrunculin (Ayscough, 1998) caused apparently random localization of subunit A (Fig. 3G).…”

Section: H + -V-atpase Subunits Are Asymmetrically Localized In Xenopusmentioning

confidence: 95%

Early, H+-V-ATPase-dependent proton flux is necessary for consistent left-right patterning of non-mammalian vertebrates

Adams

Robinson

Fukumoto³

et al. 2006

Development

249

306

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Biased left-right asymmetry is a fascinating and medically important phenomenon. We provide molecular genetic and physiological characterization of a novel, conserved, early, biophysical event that is crucial for correct asymmetry: H + flux. A pharmacological screen implicated the H + -pump H + -V-ATPase in Xenopus asymmetry, where it acts upstream of early asymmetric markers. Immunohistochemistry revealed an actin-dependent asymmetry of H + -V-ATPase subunits during the first three cleavages. H + -flux across plasma membranes is also asymmetric at the four-and eight-cell stages, and this asymmetry requires H + -V-ATPase activity. Abolishing the asymmetry in H + flux, using a dominant-negative subunit of the H + -V-ATPase or an ectopic H + pump, randomized embryonic situs without causing any other defects. To understand the mechanism of action of H + -V-ATPase, we isolated its two physiological functions, cytoplasmic pH and membrane voltage (V mem ) regulation. Varying either pH or V mem , independently of direct manipulation of H + -V-ATPase, caused disruptions of normal asymmetry, suggesting roles for both functions. V-ATPase inhibition also abolished the normal early localization of serotonin, functionally linking these two early asymmetry pathways. The involvement of H + -V-ATPase in asymmetry is conserved to chick and zebrafish. Inhibition of the H + -V-ATPase induces heterotaxia in both species; in chick, H + -V-ATPase activity is upstream of Shh; in fish, it is upstream of Kupffer's vesicle and Spaw expression. Our data implicate H + -V-ATPase activity in patterning the LR axis of vertebrates and reveal mechanisms upstream and downstream of its activity. We propose a pH-and V mem -dependent model of the early physiology of LR patterning. Development 133, 1657Development 133, -1671Development 133, (2006 DEVELOPMENT 1658 necessary to characterize the endogenous behavior of the relevant pumps in embryos and to place their function in the context of known LR patterning mechanisms. Here, we explore the properties of H + -V-ATPase function in several vertebrate embryos. Through endogenous localization of the H + -V-ATPase and gain-and loss-offunction experiments in chick, frog and zebrafish, we identify the H + -V-ATPase as a novel, conserved, obligate component of LR patterning upstream of asymmetric gene expression. KEY WORDS: Left-right asymmetry, H + -V-ATPase, V-ATPase, Xenopus, Chick, Zebrafish, Axial patterning, Cytoplasmic pH, Membrane voltage MATERIALS AND METHODS Animal husbandryXenopus embryos were collected according to standard protocols (Sive et al., 2000) in 0.1ϫ Modified Marc's Ringers (MMR) pH 7.8 + 0.1% Gentamicin. Xenopus embryos were staged according to Nieuwkoop and Faber (Nieuwkoop and Faber, 1967). Chick embryos from Charles River Laboratories, maintained at 38°C, were staged according to Hamburger and Hamilton (Hamburger and Hamilton, 1992). Zebrafish embryos (Westerfield, 1995) were maintained at 28.5°C in water containing 1 drop per gallon Methyl Blue. Assaying organ situsXenopus e...

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[2] Use of latrunculin-A, an actin monomer-binding drug

Cited by 83 publications

References 16 publications

Rev‐dependent association of the intron‐containing HIV‐1 gag mRNA with the nuclear actin bundles and the inhibition of its nucleocytoplasmic transport by latrunculin‐B

Rev‐dependent association of the intron‐containing HIV‐1 gag mRNA with the nuclear actin bundles and the inhibition of its nucleocytoplasmic transport by latrunculin‐B

Arp2/3 Activity Is Necessary for Efficient Formation of E-cadherin Adhesive Contacts

Early, H+-V-ATPase-dependent proton flux is necessary for consistent left-right patterning of non-mammalian vertebrates

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