Assembly of vimentin in vitro and its implications concerning the structure of intermediate filaments

Ip, Wallace; Hartzer, Michael K.; Pang, Yan; Robson, Richard M.

doi:10.1016/0022-2836(85)90007-5

Cited by 148 publications

(79 citation statements)

References 36 publications

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“…2B) at 25 or 250 g/ml (data not shown) in pH 8.0 buffer were assembled in the presence of 0.17 M NaCl, followed by cross-linking with 0.1 M DST. Irrespective of the protein concentration, in the absence of salt, vimentin formed primarily tetramers and some higher oligomers, as expected (16,19,22,53,54) (Fig. 2A).…”

Section: Assembly Of ␣-Internexin In If In Vitro and Copolymerizationsupporting

confidence: 66%

“…2 Such pH-dependent association phenomena have not been reported for vimentin (19,22,54). These data therefore allow the speculation that in living cells the state of assembly of an ␣-internexin-containing IF may be significantly affected by the microenvironment.…”

Section: Molecular Packing Of Coiled-coil Molecules In Type IV If Is mentioning

confidence: 94%

“…Vimentin assembly was done at 0.2-0.5 mg/ml in a similar triethanolamine HCl buffer but at pH 7.4 -8.0 (16,19). ␣-Internexin and vimentin co-assembly experiments were done in similar buffers at pH 7.0 -8.0.…”

Section: Methodsmentioning

confidence: 99%

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Molecular Parameters of Type IV α-Internexin and Type IV-Type III α-Internexin-Vimentin Copolymer Intermediate Filaments

Steinert

Marekov

Parry

1999

Journal of Biological Chemistry

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During neuronal development, a dynamic replacement mechanism occurs in which the type VI nestin and type III vimentin intermediate filament proteins are replaced by a series of type IV proteins beginning with ␣-internexin. We have explored molecular details of how the type III to type IV replacement process may occur. First, we have demonstrated by cross-linking experiments that bacterially expressed forms of ␣-internexin and vimentin form heterodimer molecules in vitro that assemble into copolymer intermediate filaments. We show using a urea disassembly assay that ␣-internexin molecules are likely to be more stable than those of vimentin. Second, by analyses of the induced cross-links, we have determined the axial lengths of ␣-internexin homodimer and ␣-internexin-vimentin heterodimer molecules and their modes of alignments in filaments. We report that these dimensions are the same as those reported earlier for vimentin homopolymer molecules and, by implication, are also the same for the other neuronal type IV proteins. These data suggest that during neuronal development, ␣-internexin molecules are readily assimilated onto the pre-existing vimentin cytoskeletal intermediate filament network because the axial lengths and axial alignments of their molecules are the same. Furthermore, the dynamic replacement process may be driven by a positive equilibrium due to the increased stability of the ␣-internexin network.

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Section: Assembly Of ␣-Internexin In If In Vitro and Copolymerizationsupporting

confidence: 66%

Section: Molecular Packing Of Coiled-coil Molecules In Type IV If Is mentioning

confidence: 94%

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Molecular Parameters of Type IV α-Internexin and Type IV-Type III α-Internexin-Vimentin Copolymer Intermediate Filaments

Steinert

Marekov

Parry

1999

Journal of Biological Chemistry

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“…By increasing the ionic strength of the solution, higher IF aggregates can be induced. At the level of tetramers, basically two alignments of the constituting dimers have been proposed: an antiparallel in-register configuration (forming a structure of approximately 45 nm length [2,3]) and an antiparallel staggered (approximately 65 nm long) configuration [4~7]. Recently, we studied the structure of vimentin (a type III IF protein) and T-vimentin (vimentin missing the first 70 amino acids) by transient electric birefringence (TEB) measurements [8,9].…”

Section: Introductionmentioning

confidence: 99%

The assembly state of the intermediate filament proteins desmin and glial fibrillary acidic protein at low ionic strength

Kooijman¹,

Amerongen²,

Traub

et al. 1995

FEBS Letters

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“…In the assembly of vimentins, Ip et a1. [23] also found 66nm long intermediate filament. They called it the "minimal length" IF, and deduced from it that IF are staggered in some way.…”

Section: Discussionmentioning

confidence: 80%

Assembly of lamins in vitro

et al. 1996

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After lamins A, B and C were isolated and purified from rat liver, their assembly properties were examined by electron microscopy and scanning tunneling microscopy using negative staining and the glycerol coating method, respectively. By varying the assembly time or the ionic conditions under which polymerization takes place, we have observed different stages of lamin assembly, which may provide clues on the structure of the 10 nm lamin filaments. At the first level of structural organization, two lamin polypeptides associate laterally into dimers with the two domains being parallel and in register. At the second level of structural organization, two dimers associate in a half-staggered and antiparallel fashion to form a tetramer 75 nm in length. At the third level of structural organization, 4-10 lamin tetramers associate laterally in register to form 75 nm long 10nm filaments, which in turn combine head to head into long, fully assembled lamin filaments. The assembled lamin filaments are nonpolar.

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Assembly of vimentin in vitro and its implications concerning the structure of intermediate filaments

Cited by 148 publications

References 36 publications

Molecular Parameters of Type IV α-Internexin and Type IV-Type III α-Internexin-Vimentin Copolymer Intermediate Filaments

Molecular Parameters of Type IV α-Internexin and Type IV-Type III α-Internexin-Vimentin Copolymer Intermediate Filaments

The assembly state of the intermediate filament proteins desmin and glial fibrillary acidic protein at low ionic strength

Assembly of lamins in vitro

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