Regulation of assembly-disassembly of intermediate filaments in vitro.

Inagaki, Masaki; Gonda, Y; Ando, Shoji; Kitamura, Shinobu; Nishi, Yoshimi; Sato, Chikara

doi:10.1247/csf.14.279

Cited by 30 publications

(20 citation statements)

References 37 publications

(12 reference statements)

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“…The persistence length of native actin filaments (without phalloidin) under our experimental conditions is 9.8 ±0.1 µm (Table1); comparable to a previously reported value of 9.0±0.5 µm measured under slightly different buffer conditions, 19 and the value predicted from molecular dynamics simulations. [20][21][22] 23 and vimentin 24,25 ).…”

Section: Resultsmentioning

confidence: 99%

Cofilin Increases the Bending Flexibility of Actin Filaments: Implications for Severing and Cell Mechanics

McCullough

Blanchoin

Martiel

et al. 2008

Journal of Molecular Biology

203

254

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We determined the flexural (bending) rigidities of actin and cofilactin filaments from a cosine correlation function analysis of their thermally driven, two-dimensional fluctuations in shape. The persistence length of actin filaments is 9.8 µm, corresponding to a flexural rigidity of 0.040 pN µm 2 . Cofilin binding lowers the persistence length ∼5-fold to a value of 2.2 µm and the filament flexural rigidity to 0.0091 pN µm 2 . That cofilin-decorated filaments are more flexible than native filaments despite an increased mass indicates that cofilin binding weakens and redistributes stabilizing subunit interactions of filaments. We favor a mechanism in which the increased flexibility of cofilin-decorated filaments results from the linked dissociation of filament-stabilizing ions and reorganization of actin subdomain 2 and as a consequence promotes severing due to a mechanical asymmetry. Knowledge of the effects of cofilin on actin filament bending mechanics, together with our previous analysis of torsional stiffness, provide a quantitative measure of the mechanical changes in actin filaments associated with cofilin binding, and suggest that the overall mechanical and forceproducing properties of cells can be modulated by cofilin activity.

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Section: Resultsmentioning

confidence: 99%

Cofilin Increases the Bending Flexibility of Actin Filaments: Implications for Severing and Cell Mechanics

McCullough

Blanchoin

Martiel

et al. 2008

Journal of Molecular Biology

203

254

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“…These alterations in podocyte structure were accompanied by a change in the distribution of vimentin, a major intermediate filament of the podocyte. Vimentin polymerization is regulated through phosphorylation of serine/threonine, as well as tyrosine residues, and tyrosine kinases can modify vimentin organization in cells (25,26). Therefore, potential mechanisms to explain the observed effect might involve regulation of the podocyte cytoskeletal proteins in some manner, including the possibility of direct or indirect interactions between the GLEPP1 phosphatase and vimentin.…”

Section: Discussionmentioning

confidence: 99%

Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate

Wharram¹,

Goyal²,

Gillespie³

et al. 2000

J. Clin. Invest.

144

107

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“…Each of these polypeptides has structural features characteristic of the family of intermediate filament proteins: (1) a central a-helical rod domain that interacts with other rod domains to form tetrameric subunits, (2) an Nterminal head domain that is important for polymerization, and (3) a C-terminal tail region of variable length that is thought to extend from the filament and interact with the surrounding environment ( Fig. 1; for reviews, see Steinert and Roop, 1988;Inagaki et al, 1989). After they are synthesized in the cell bodies of neurons, all 3 neurofilament polypeptides are phosphorylated, but to different extents: 3, 6, and 13 mol phosphate/m01 polypeptide for NF-L, NF-M, and NF-H, respectively in rat (Julien and Mushynski, 1982; the reported values have been corrected to reflect more recent determinations of the molecular weights of the subunits).…”

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confidence: 99%

Identification of serine 473 as a major phosphorylation site in the neurofilament polypeptide NF-L

Liu

Willard

1990

J. Neurosci.

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Neurofilaments are composed of 3 polypeptides designated NF-H, NF-M, and NF-L, all of which are subject to posttranslational phosphorylation. It has been suggested that phosphorylation of the NF-L polypeptide can influence the assembly of NF-L into filaments, but the sites at which NF-L is phosphorylated are unknown. To locate these phosphorylation sites, we have identified phosphopeptides of NF-L by labeling them with 32P both in vitro and in cultured neurons and also by observing their change in chromatographic behavior after they have been treated with phosphatase. We report here that serine 473, in the carboxy-terminal tail domain of NF-L, is a major substrate in vitro for protein kinases endogenous to a crude cytoskeleton-containing fraction. Moreover, serine 473 is a major phosphorylation site in vivo; in neurofilaments isolated from rat spinal cord, approximately 73% of serine 473 was phosphorylated, and accounted for at least one-third of the total phosphate associated with NF-L. The identification of this phosphorylation site in NF-L provides a criterion for identifying the protein kinase that phosphorylates NF-L and raises the question of its function.

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Regulation of assembly-disassembly of intermediate filaments in vitro.

Cited by 30 publications

References 37 publications

Cofilin Increases the Bending Flexibility of Actin Filaments: Implications for Severing and Cell Mechanics

Cofilin Increases the Bending Flexibility of Actin Filaments: Implications for Severing and Cell Mechanics

Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate

Identification of serine 473 as a major phosphorylation site in the neurofilament polypeptide NF-L

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