An electron microscope study of the interaction between fructose diphosphate aldolase and actin-containing filaments.

Morton, Don; Clarke, Frank M.; Masters, C.J.

doi:10.1083/jcb.74.3.1016

Cited by 45 publications

(19 citation statements)

References 26 publications

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“…The results obtained with aldolase were qualitatively similar to those with actophorin and a-actinin. We realize that aldolase alone can bundle but this requires much higher aldolase ratios to actin than we used here (Morton et al, 1977) . The binding of aldolase to actin is probably relevant physiologically, since aldolase is known to be associated with the solid phase of cell cytoplasm, probably actin filaments (Pagliaro and Taylor, 1988).…”

Section: Discussionmentioning

confidence: 99%

The actin filament severing protein actophorin promotes the formation of rigid bundles of actin filaments crosslinked with alpha-actinin.

Maciver

Wachsstock

Schwarz

et al. 1991

The Journal of Cell Biology

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Abstract. The actin filament severing protein, Acanthamoeba actophorin, decreases the viscosity of actin filaments, but increases the stiffness and viscosity of mixtures of actin filaments and the crosslinking protein a-actinin . The explanation of this paradox is that in the presence of both the severing protein and crosslinker the actin filaments aggregate into an interlocking meshwork of bundles large enough to be visualized by light microscopy. The size of these bundles depends on the size of the containing vessel . The actin filaments in these bundles are tightly packed in some areas while in others they are more disperse. The bundles form a continuous reticulum that fills the container, since the filaments from a particular bundle S NCE the first descriptions of ameboid locomotion a century and a half ago, the concept of a reversible transformation between "sol" and "gel" has been central to hypothesis attempting to explain the phenomenon. Although it was proposed that the protoplasm is a contractile three-dimensional reticulum as early as 1873 (De Bruyn, 1947), only in comparatively recent times has this reticulum been shown to be mainly an actin-based system (Pollard and Ito, 1970) . Subsequent research has revealed that cytoplasmic actin filaments are associated with myosin (reviewed by Korn and Hammer, 1988) and a number of other proteins that regulate actin filament assembly and crosslinking (reviewed by Stossel et al., 1985, andPollard and . Because there are multiple crosslinking proteins in these cytoplasmic actin gels, the physiological function of the individual crosslinking proteins by mutation or gene disruption is difficult to demonstrate (Wallraff et al ., 1986;Schleicher et al., 1988). Consequently most of our knowledge about cytoplasmic actin gels has come from in vitro reconstitution with actin and purified individual crosslinkers such as a-actinin.Alpha-actinin is a major actin crosslinking protein in skeletal muscle and nonmuscle cells . Skeletal muscle a-actinins are calcium-insensitive crosslinking proteins. Some, but not all, a-actinins from smooth muscle and nonmuscle cells are inhibited by calcium . Acanthamoeba a-actinin is calcium insensitive but is otherwise a typical a-actinin (Pollard, 1981;

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Section: Discussionmentioning

confidence: 99%

The actin filament severing protein actophorin promotes the formation of rigid bundles of actin filaments crosslinked with alpha-actinin.

Maciver

Wachsstock

Schwarz

et al. 1991

The Journal of Cell Biology

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“…Aldolase and glyceraldehyde phosphate dehydrogenase undergo adventitious binding to microfilaments [29] and act as actin-bundling proteins [30,31]. Furthermore, their interaction with F-actin is regulated by physiological concentrations of their substrates [29,32].…”

Section: Discussionmentioning

confidence: 99%

“…The thermodynamic properties of these ternary systems were discussed by Ogston [31,Timasheff & Kronman [4], Kuntz & Kautzmann [5], Arakawa & Timasheff [6,71. As a result of these studies it became clear that phenomena similar to those described by Ogston & Phelps [1] were of general occurrence in the cytoplasmic matrix, where the association and dissociation of macromolecules is influenced by other macromolecules present in solution.…”

Section: Introductionmentioning

confidence: 99%

‘Macromolecular crowding’ is a primary factor in the organization of the cytoskeleton

Cuneo

Magri

Verzola

et al. 1992

Biochemical Journal

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We propose that, in the cell, the reversible conversion of actin filaments into actin bundles is controlled by the concentration of the macromolecules [we have employed poly(ethylene glycol) 6000 to mimic the macromolecules of the cell] as well as by the nature of the ancillary cytoskeletal proteins that decorate actin filaments. The proposal is based on the following evidence. (1) Under our experimental conditions the transition from filaments into bundles occurs at increasing concentrations of poly(ethylene glycol), with the following sequence: caldesmon-actin, 3 %; filamin-actin, 4-5 %; caldesmon-tropomyosin-actin, 5-7 %; actin, 6-7 %; tropomyosin-actin, 9-10 %. (2) Under conditions of low osmoelastic stress [3 % poly(ethylene glycol)], preformed caldesmon-actin bundles are dissociated by the addition of either tropomyosin or tropomyosin-decorated actin. The dissociation of the bundles promoted by the addition of tropomyosindecorated actin is faster than that promoted by the addition of tropomyosin.

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“…The glycolytic enzyme aldolase can induce the parallel alignment of actin filaments in vitro when present at high molar ratios to actin (Clarke & Morton 1976Morton et al 1977). Although some bundling of filaments occurs when aldolase is added to F -actin alone, a more ordered lattice structure showing transverse bands every 38 nm forms when aldolase is added to actin filaments that contain tropomyosin and troponin.…”

Section: Actin Filament Bundling Proteinsmentioning

confidence: 99%

Nonmuscle Actin-Binding Proteins

Stossel¹,

Chaponnier²,

Ezzell³

et al. 1985

Annu. Rev. Cell. Biol.

557

135

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An electron microscope study of the interaction between fructose diphosphate aldolase and actin-containing filaments.

Cited by 45 publications

References 26 publications

The actin filament severing protein actophorin promotes the formation of rigid bundles of actin filaments crosslinked with alpha-actinin.

The actin filament severing protein actophorin promotes the formation of rigid bundles of actin filaments crosslinked with alpha-actinin.

‘Macromolecular crowding’ is a primary factor in the organization of the cytoskeleton

Nonmuscle Actin-Binding Proteins

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