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Volumn 10, Issue 1, 1998, Pages 45-51

Control of actin dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; COFILIN;

EID: 0032006817     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80085-9     Document Type: Article
Times cited : (179)

References (55)
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    • of special interest. Immunodepletion of actin-depolymerizing factor (ADF)/cofilin from Xenopus egg extracts causes an increase in the length of actin tails at the rear of Listeria. Immunodepletion of gelsolin does not affect movement of Listeria. Adding back ADF, but not the Ser3→Glu ADF mutant, restores the control tail length. The authors conclude that ADF, but not gelsolin, increases the rate of depolymerization of actin filaments in the actin tails.
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    • of special interest. This is the first report that capping protein (CP) has an essential function in a multicellular organism. Reduced levels of CP in viable transheterozygous adults lead to defects in the organization of actin bundles in the bristles, causing abnormal morphology. The apparent increased amount of actin assembled in bundles may be consistent with a relatively low concentration of stady-state ATP·G-actin which results from incomplete capping.
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    • of special interest. The kinetics of capping protein (CP) association with/dissociation from barbed actin filament ends in vitro are relatively slow. The interesting consequence is that the kinetics of association of CP with growing barbed ends may by themselves control the length of actin filaments in vivo. Phosphatidylinositol 4,5-bisophosphate efficiently and rapidly dissociates CP from barbed ends. Possible models for the regulation of capping/uncapping/nucleation in actin-based motility are discussed in this paper.
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    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • of outstanding interest. Actin-depolymerizing factor (ADF) increases the rate of treadmilling of actin filaments in vitro by 25-fold. It does this by increasing the rate of filament disassembly from the pointed end specifically. ADF consistently increases the rate of Listeria propulsion in platelet extracts. Barbed end growth, which also powers lamellipodium protusion or filopodium extension, results from the ADF-regulated treadmilling of actin filaments.
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    • of special interest. The function of cofilin in budding yeast is adressed by a genetic approach. Cofilin mutants display a slower rate of F-actin depolymerization by latrunculin-A, and harbor defects in endocytosis, while the motility of cortical actin patches is unaffected.
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    • of special interest. Cryoelectron microscopic observations and image reconstructions show that, in binding to F-actin in a 1:1 ratio, cofilin makes contacts with two F-actin subunits along the long pitch helix, thereby increasing the twist of the filament. Interestingly, the cofilin-binding site overlaps with interfaces of myosin, profilin and gelsolin with actin, although the resulting structural features of the complexes are different.
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    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • of outstanding interest. This mutagenesis study delineates the regions of ADF that interact with both G- and F-actin, and demonstrates the existence of other regions more specifically involved in F-actin binding. The amino-terminal region of ADF, which contains the phosphorylatable serine residue, plays a role in actin binding. Despite the similar folds in ADF and gelsolin segment-1, the two proteins bind actin differently, consistent with their different functions.
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    • of special interest. This is a very clear electron microscopic study of the organization of actin filaments in the actin tails of Listeria in cell protrusions. The study shows that long (over 2μm long) axial filaments forming the core of the tail are perpendicular to the bacterium surface, while peripheral shorter filaments (0.3 μm long) are arranged in randomly distributed oblique directions. A model more complex than the simple initial nucleation release model [55] needs to be elaborated to accommodate these new results.
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    • Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes
    • of special interest. These authors make the interesting point that deletion of residues 21-97 in the amino-terminal region of Act A produces bacteria moving with periodic oscillatory changes in rate. Consistently, actin tails display a periodic density of actin filaments. This behavior has important implications for the mechanism of movement.
    • Lasa I, Gouin E, Goethals M, Vancompernolle K, David V, Vandekerckhove J, Cossart P. Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes. of special interest EMBO J. 16:1997;1531-1540 These authors make the interesting point that deletion of residues 21-97 in the amino-terminal region of Act A produces bacteria moving with periodic oscillatory changes in rate. Consistently, actin tails display a periodic density of actin filaments. This behavior has important implications for the mechanism of movement.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.