Literature DB >> 1736897

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

P Cuneo1, E Magri, A Verzola, E Grazi.   

Abstract

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 tropomyosin-decorated actin is faster than that promoted by the addition of tropomyosin.

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Year:  1992        PMID: 1736897      PMCID: PMC1130714          DOI: 10.1042/bj2810507

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  30 in total

1.  THE INTERACTION BETWEEN POLYSACCHARIDES AND OTHER MACROMOLECULES. 4. THE OSMOTIC PRESSURE OF MIXTURES OF SERUM ALBUMIN AND HYALURONIC ACID.

Authors:  T C LAURENT; A G OGSTON
Journal:  Biochem J       Date:  1963-11       Impact factor: 3.857

2.  The extrapolation of light-scattering data to zero concentration.

Authors:  S N TIMASHEFF; M J KRONMAN
Journal:  Arch Biochem Biophys       Date:  1959-07       Impact factor: 4.013

3.  The influence of molecular crowding on the binding of glycolytic enzymes to cytoskeletal structure.

Authors:  K Shearwin; C Nanhua; C Masters
Journal:  Biochem Int       Date:  1989-10

Review 4.  Hydration of proteins and polypeptides.

Authors:  I D Kuntz; W Kauzmann
Journal:  Adv Protein Chem       Date:  1974

5.  Effect of thermodynamic nonideality on the subcellular distribution of enzymes: adsorption of aldolase to muscle myofibrils.

Authors:  S J Harris; D J Winzor
Journal:  Arch Biochem Biophys       Date:  1985-12       Impact factor: 4.013

6.  Caldesmon. Molecular weight and subunit composition by analytical ultracentrifugation.

Authors:  P Graceffa; C L Wang; W F Stafford
Journal:  J Biol Chem       Date:  1988-10-05       Impact factor: 5.157

7.  Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties.

Authors:  A Bretscher
Journal:  J Biol Chem       Date:  1984-10-25       Impact factor: 5.157

8.  Bundling of actin filaments by aorta caldesmon is not related to its regulatory function.

Authors:  C J Moody; S B Marston; C W Smith
Journal:  FEBS Lett       Date:  1985-10-21       Impact factor: 4.124

9.  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.  Mechanism of poly(ethylene glycol) interaction with proteins.

Authors:  T Arakawa; S N Timasheff
Journal:  Biochemistry       Date:  1985-11-19       Impact factor: 3.162

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  15 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.  The control of cellular shape and motility. Mg2+ and tropomyosin regulate the formation and the dissociation of microfilament bundles.

Authors:  E Grazi; P Cuneo; A Cataldi
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

3.  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

4.  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

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

6.  Phase behavior of mixtures of rods (tobacco mosaic virus) and spheres (polyethylene oxide, bovine serum albumin).

Authors:  M Adams; S Fraden
Journal:  Biophys J       Date:  1998-01       Impact factor: 4.033

7.  Filamin and gelsolin influence Ca(2+)-sensitivity of smooth muscle thin filaments.

Authors:  N B Gusev; K Pritchard; J L Hodgkinson; S B Marston
Journal:  J Muscle Res Cell Motil       Date:  1994-12       Impact factor: 2.698

8.  Molecular crowding of collagen: a pathway to produce highly-organized collagenous structures.

Authors:  Nima Saeidi; Kathryn P Karmelek; Jeffrey A Paten; Ramin Zareian; Elaine DiMasi; Jeffrey W Ruberti
Journal:  Biomaterials       Date:  2012-07-29       Impact factor: 12.479

Review 9.  Caldesmon and the regulation of cytoskeletal functions.

Authors:  C L Albert Wang
Journal:  Adv Exp Med Biol       Date:  2008       Impact factor: 2.622

10.  Isolation of cell nuclei using inert macromolecules to mimic the crowded cytoplasm.

Authors:  Ronald Hancock; Yasmina Hadj-Sahraoui
Journal:  PLoS One       Date:  2009-10-23       Impact factor: 3.240

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