Literature DB >> 8027175

Crowding-induced organization of cytoskeletal elements: II. Dissolution of spontaneously formed filament bundles by capping proteins.

T L Madden1, J Herzfeld.   

Abstract

Through calculations of molecular packing constraints in crowded solutions, we have previously shown that dispersions of filament forming proteins and soluble proteins can be unstable at physiological concentrations, such that tight bundles of filaments are formed spontaneously, in the absence of any accessory binding proteins. Here we consider the modulation of this phenomenon by capping proteins. The theory predicts that, by shortening the average filament length, capping alleviates the packing problem. As a result, the dispersed isotropic solution is stable over an expanded range of compositions.

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Year:  1994        PMID: 8027175      PMCID: PMC2120095          DOI: 10.1083/jcb.126.1.169

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


  10 in total

1.  Quantitation of liquid-crystalline ordering in F-actin solutions.

Authors:  C M Coppin; P C Leavis
Journal:  Biophys J       Date:  1992-09       Impact factor: 4.033

2.  The actin content of fibroblasts.

Authors:  D Bray; C Thomas
Journal:  Biochem J       Date:  1975-05       Impact factor: 3.857

3.  'Macromolecular crowding' is a primary factor in the organization of the cytoskeleton.

Authors:  P Cuneo; E Magri; A Verzola; E Grazi
Journal:  Biochem J       Date:  1992-01-15       Impact factor: 3.857

Review 4.  Actin-binding proteins.

Authors:  J H Hartwig; D J Kwiatkowski
Journal:  Curr Opin Cell Biol       Date:  1991-02       Impact factor: 8.382

5.  Microtubule solutions display nematic liquid crystalline structure.

Authors:  A L Hitt; A R Cross; R C Williams
Journal:  J Biol Chem       Date:  1990-01-25       Impact factor: 5.157

6.  Shape anisotropy and ordered phases in reversibly assembling lyotropic systems.

Authors: 
Journal:  Phys Rev A       Date:  1991-02-15       Impact factor: 3.140

7.  Theory of nematic order with aggregate dehydration for reversibly assembling proteins in concentrated solutions: Application to sickle-cell hemoglobin polymers.

Authors: 
Journal:  Phys Rev A       Date:  1991-06-15       Impact factor: 3.140

8.  Crowding-induced organization of cytoskeletal elements: I. Spontaneous demixing of cytosolic proteins and model filaments to form filament bundles.

Authors:  T L Madden; J Herzfeld
Journal:  Biophys J       Date:  1993-09       Impact factor: 4.033

9.  Radioimmunoassay for tubulin: a quantitative comparison of the tubulin content of different established tissue culture cells and tissues.

Authors:  G Hiller; K Weber
Journal:  Cell       Date:  1978-08       Impact factor: 41.582

10.  Osmoelastic coupling in biological structures: formation of parallel bundles of actin filaments in a crystalline-like structure caused by osmotic stress.

Authors:  A Suzuki; M Yamazaki; T Ito
Journal:  Biochemistry       Date:  1989-07-25       Impact factor: 3.162

  10 in total
  5 in total

1.  Nonideality and the nucleation of sickle hemoglobin.

Authors:  M Ivanova; R Jasuja; S Kwong; R W Briehl; F A Ferrone
Journal:  Biophys J       Date:  2000-08       Impact factor: 4.033

2.  Micro- and macrorheological properties of actin networks effectively cross-linked by depletion forces.

Authors:  R Tharmann; M M A E Claessens; A R Bausch
Journal:  Biophys J       Date:  2006-01-13       Impact factor: 4.033

3.  Tracer diffusion through F-actin: effect of filament length and cross-linking.

Authors:  J D Jones; K Luby-Phelps
Journal:  Biophys J       Date:  1996-11       Impact factor: 4.033

4.  The bundling of actin with polyethylene glycol 8000 in the presence and absence of gelsolin.

Authors:  J Goverman; L A Schick; J Newman
Journal:  Biophys J       Date:  1996-09       Impact factor: 4.033

5.  Flexible polymer-induced condensation and bundle formation of DNA and F-actin filaments.

Authors:  R de Vries
Journal:  Biophys J       Date:  2001-03       Impact factor: 4.033

  5 in total

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