The binding of cytochalasin D to monomeric actin

Goddette, Dean W.; Frieden, Carl

doi:10.1016/0006-291x(85)91051-4

Cited by 48 publications

(38 citation statements)

References 18 publications

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“…While this interaction may serve as a means to control the spatial distribution of ion channels in the apical membrane of epithelial cells, a requirement in polarized epithelia, the possibility also existed that the colocalization of actin filaments with the apical Na ϩ channels would serve a functional role. Modification of actin filament organization with cytochalasin D, an actin filament disrupter (41)(42)(43), induced apical Na ϩ channel activity in the A6 cell (15). Because DNase I, which inhibits actin polymerization, inhibited the cytochalasin D-induced Na ϩ channel activity, the data suggested that "short" actin filaments might be involved in effect- ing ion channel activation.…”

Section: Discussionmentioning

confidence: 97%

Regulation of Epithelial Sodium Channels by Short Actin Filaments

Berdiev

Prat

Cantiello

et al. 1996

Journal of Biological Chemistry

149

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Cytoskeletal elements play an important role in the regulation of ion transport in epithelia. We have studied the effects of actin filaments of different length on the ␣, ␤, ␥-rENaC (rat epithelial Na ؉ channel) in planar lipid bilayers. We found the following. 1) Short actin filaments caused a 2-fold decrease in unitary conductance and a 2-fold increase in open probability (P o ) of ␣,␤,␥-rENaC. 2) ␣,␤,␥-rENaC could be transiently activated by protein kinase A (PKA) plus ATP in the presence, but not in the absence, of actin. 3) ATP in the presence of actin was also able to induce a transitory activation of ␣,␤,␥-rENaC, although with a shortened time course and with a lower magnitude of change in P o . 4) DNase I, an agent known to prohibit elongation of actin filaments, prevented activation of ␣,␤,␥-rENaC by ATP or PKA plus ATP. 5) Cytochalasin D, added after rundown of ␣,␤,␥-rENaC activity following ATP or PKA plus ATP treatment, produced a second transient activation of ␣,␤,␥-rENaC. 6) Gelsolin, a protein that stabilizes polymerization of actin filaments at certain lengths, evoked a sustained activation of ␣,␤,␥-rENaC at actin/gelsolin ratios of <32:1, with a maximal effect at an actin/gelsolin ratio of 2:1. These results suggest that short actin filaments activate ␣,␤,␥-rENaC. PKA-mediated phosphorylation augments activation of this channel by decreasing the rate of elongation of actin filaments. These results are consistent with the hypothesis that cloned ␣,␤,␥-rENaCs form a core conduction unit of epithelial Na ؉ channels and that interaction of these channels with other associated proteins, such as short actin filaments, confers regulation to channel activity.Membrane transport protein-cytoskeleton interactions are thought to be important not only for restricting various transporters to specific membrane domains, especially in epithelia, but also for regulating transport activity (1, 2). Actin networks interact with the plasma membrane either by direct binding (3, 4) or through anchoring proteins, including actin-binding protein (filamin), spectrin (fodrin, the non-erythroid form of spectrin), and ankyrin (5-8). The actin cytoskeleton has been shown to interact with a variety of transmembrane proteins, including ion transport molecules such as the band 3 anion exchanger (9), the epithelial Na ϩ /K ϩ -ATPase (6, 10), rat brain voltage-sensitive Na ϩ channels (11, 12), the Na ϩ -K ϩ -Cl Ϫ cotransporter (13), and the Na ϩ -H ϩ exchanger (14). Recently, functional interactions between the actin cytoskeleton and ion channels have been demonstrated for Na ϩ channel activity in epithelial cells (15), N-methyl-D-aspartic acid-activated channels in neurons (16), the Na ϩ /K ϩ -ATPase (17), a renal K ϩ channel (18), and two epithelial anion channels (namely, a renal Cl Ϫ channel (19) and the cystic fibrosis transmembrane conductance regulator (20, 21)). Apically located, renal amiloride-sensitive Na ϩ channels have also been shown to be associated directly with the actin-based membrane cytoskeleton (15, 22). Moreov...

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Section: Discussionmentioning

confidence: 97%

Regulation of Epithelial Sodium Channels by Short Actin Filaments

Berdiev

Prat

Cantiello

et al. 1996

Journal of Biological Chemistry

149

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“…Cytochalasin D was used to prevent internalization of bacteria (29). Cells were treated with cytochalasin D (5 M) for 1 h followed by washing three times with PBS before infection with M. smegmatis.…”

Section: Methodsmentioning

confidence: 99%

Execution of Macrophage Apoptosis by PE_PGRS33 of Mycobacterium tuberculosis Is Mediated by Toll-like Receptor 2-dependent Release of Tumor Necrosis Factor-α

Basu

Pathak

Banerjee

et al. 2007

Journal of Biological Chemistry

195

213

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“…This motion is consistent with the formation of endocytic vesicles. To confirm that the disappearance of GFP-Ras from the membrane was a consequence of endocytic traffic, the cells were treated with cytochalasin D, which inhibits endocytosis by destabilizing actin filaments (11,27). As shown in Fig.…”

Section: Fig 1 Ras Is Present In Lipid Raftsmentioning

confidence: 99%