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Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility: Implications for Axonal Flexibility
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| Zeitschriftentitel: | Journal of Neurochemistry |
|---|---|
| Personen und Körperschaften: | , |
| In: | Journal of Neurochemistry, 75, 2000, 4, S. 1475-1486 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Asch, William S. Schechter, Nisson Asch, William S. Schechter, Nisson |
|---|---|
| author |
Asch, William S. Schechter, Nisson |
| spellingShingle |
Asch, William S. Schechter, Nisson Journal of Neurochemistry Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility Cellular and Molecular Neuroscience Biochemistry |
| author_sort |
asch, william s. |
| spelling |
Asch, William S. Schechter, Nisson 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1046/j.1471-4159.2000.0751475.x <jats:p> <jats:bold>Abstract:</jats:bold> The assembly characteristics of the neuronal intermediate filament protein plasticin were studied in SW13 cells in the presence and absence of a cytoplasmic filament network. Full‐length plasticin cannot polymerize into homopolymers in filament‐less SW13c1.2Vim<jats:sup>‐</jats:sup> cells but efficiently coassembles with vimentin in SW13c1.1Vim<jats:sup>‐</jats:sup> cells. By cotransfecting plasticin and vimentin in SW13c1.1Vim<jats:sup>‐</jats:sup> cells, we show that plasticin assembly requires vimentin in noncatalytic amounts. Differing effects on assembly were seen with point mutations of plasticin monomers that were analogous to the keratin mutations that cause epidermolysis bullosa simplex (EBS). In particular, plasticin monomers with point mutations analogous to those in EBS do not uniformly inhibit neurofilament (NF) network formation. A point mutation in the helix termination sequence resulted in complete filament aggregation when coexpressed with vimentin but showed limited coassembly with low‐ and medium‐molecular‐weight NF proteins (NF‐L and NF‐M, respectively). In transfected SW13c1.1Vim<jats:sup>+</jats:sup> cells, a point mutation in the first heptad of the α‐helical coil region formed equal amounts of filaments, aggregates, and a mixture of filaments and aggregates. Furthermore, coexpression of this point mutation with NF‐L and NF‐M was associated with a shift toward increased numbers of aggregates. These results suggest that there are important structural differences in assembly properties between homologous fish and mammalian intermediate filament proteins. These structural differences may contribute to the distinctive growth characteristics of the teleost visual pathway.</jats:p> Implications for Axonal Flexibility Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility Journal of Neurochemistry |
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Journal of Neurochemistry |
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| title_sub |
Implications for Axonal Flexibility |
| title |
Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_unstemmed |
Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_full |
Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_fullStr |
Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_full_unstemmed |
Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_short |
Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_sort |
plasticin, a type iii neuronal intermediate filament protein, assembles as an obligate heteropolymer : implications for axonal flexibility |
| topic |
Cellular and Molecular Neuroscience Biochemistry |
| url |
http://dx.doi.org/10.1046/j.1471-4159.2000.0751475.x |
| publishDate |
2000 |
| physical |
1475-1486 |
| description |
<jats:p> <jats:bold>Abstract:</jats:bold> The assembly characteristics of the neuronal intermediate
filament protein plasticin were studied in SW13 cells in the presence and
absence of a cytoplasmic filament network. Full‐length plasticin cannot
polymerize into homopolymers in filament‐less SW13c1.2Vim<jats:sup>‐</jats:sup> cells
but efficiently coassembles with vimentin in SW13c1.1Vim<jats:sup>‐</jats:sup> cells. By
cotransfecting plasticin and vimentin in SW13c1.1Vim<jats:sup>‐</jats:sup> cells, we
show that plasticin assembly requires vimentin in noncatalytic amounts.
Differing effects on assembly were seen with point mutations of plasticin
monomers that were analogous to the keratin mutations that cause epidermolysis
bullosa simplex (EBS). In particular, plasticin monomers with point mutations
analogous to those in EBS do not uniformly inhibit neurofilament (NF) network
formation. A point mutation in the helix termination sequence resulted in
complete filament aggregation when coexpressed with vimentin but showed
limited coassembly with low‐ and medium‐molecular‐weight NF proteins (NF‐L and
NF‐M, respectively). In transfected SW13c1.1Vim<jats:sup>+</jats:sup> cells, a point mutation in the first heptad of the α‐helical coil region formed equal amounts of filaments, aggregates, and a mixture of filaments and aggregates. Furthermore, coexpression of this point mutation with NF‐L and NF‐M was associated with a shift toward increased numbers of aggregates. These results suggest that there are important structural differences in assembly properties between homologous fish and mammalian intermediate filament proteins. These structural differences may contribute to the distinctive growth characteristics of the teleost visual pathway.</jats:p> |
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| author | Asch, William S., Schechter, Nisson |
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| description | <jats:p> <jats:bold>Abstract:</jats:bold> The assembly characteristics of the neuronal intermediate filament protein plasticin were studied in SW13 cells in the presence and absence of a cytoplasmic filament network. Full‐length plasticin cannot polymerize into homopolymers in filament‐less SW13c1.2Vim<jats:sup>‐</jats:sup> cells but efficiently coassembles with vimentin in SW13c1.1Vim<jats:sup>‐</jats:sup> cells. By cotransfecting plasticin and vimentin in SW13c1.1Vim<jats:sup>‐</jats:sup> cells, we show that plasticin assembly requires vimentin in noncatalytic amounts. Differing effects on assembly were seen with point mutations of plasticin monomers that were analogous to the keratin mutations that cause epidermolysis bullosa simplex (EBS). In particular, plasticin monomers with point mutations analogous to those in EBS do not uniformly inhibit neurofilament (NF) network formation. A point mutation in the helix termination sequence resulted in complete filament aggregation when coexpressed with vimentin but showed limited coassembly with low‐ and medium‐molecular‐weight NF proteins (NF‐L and NF‐M, respectively). In transfected SW13c1.1Vim<jats:sup>+</jats:sup> cells, a point mutation in the first heptad of the α‐helical coil region formed equal amounts of filaments, aggregates, and a mixture of filaments and aggregates. Furthermore, coexpression of this point mutation with NF‐L and NF‐M was associated with a shift toward increased numbers of aggregates. These results suggest that there are important structural differences in assembly properties between homologous fish and mammalian intermediate filament proteins. These structural differences may contribute to the distinctive growth characteristics of the teleost visual pathway.</jats:p> |
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| spelling | Asch, William S. Schechter, Nisson 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1046/j.1471-4159.2000.0751475.x <jats:p> <jats:bold>Abstract:</jats:bold> The assembly characteristics of the neuronal intermediate filament protein plasticin were studied in SW13 cells in the presence and absence of a cytoplasmic filament network. Full‐length plasticin cannot polymerize into homopolymers in filament‐less SW13c1.2Vim<jats:sup>‐</jats:sup> cells but efficiently coassembles with vimentin in SW13c1.1Vim<jats:sup>‐</jats:sup> cells. By cotransfecting plasticin and vimentin in SW13c1.1Vim<jats:sup>‐</jats:sup> cells, we show that plasticin assembly requires vimentin in noncatalytic amounts. Differing effects on assembly were seen with point mutations of plasticin monomers that were analogous to the keratin mutations that cause epidermolysis bullosa simplex (EBS). In particular, plasticin monomers with point mutations analogous to those in EBS do not uniformly inhibit neurofilament (NF) network formation. A point mutation in the helix termination sequence resulted in complete filament aggregation when coexpressed with vimentin but showed limited coassembly with low‐ and medium‐molecular‐weight NF proteins (NF‐L and NF‐M, respectively). In transfected SW13c1.1Vim<jats:sup>+</jats:sup> cells, a point mutation in the first heptad of the α‐helical coil region formed equal amounts of filaments, aggregates, and a mixture of filaments and aggregates. Furthermore, coexpression of this point mutation with NF‐L and NF‐M was associated with a shift toward increased numbers of aggregates. These results suggest that there are important structural differences in assembly properties between homologous fish and mammalian intermediate filament proteins. These structural differences may contribute to the distinctive growth characteristics of the teleost visual pathway.</jats:p> Implications for Axonal Flexibility Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility Journal of Neurochemistry |
| spellingShingle | Asch, William S., Schechter, Nisson, Journal of Neurochemistry, Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility, Cellular and Molecular Neuroscience, Biochemistry |
| title | Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_full | Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_fullStr | Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_full_unstemmed | Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_short | Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| title_sort | plasticin, a type iii neuronal intermediate filament protein, assembles as an obligate heteropolymer : implications for axonal flexibility |
| title_sub | Implications for Axonal Flexibility |
| title_unstemmed | Plasticin, a Type III Neuronal Intermediate Filament Protein, Assembles as an Obligate Heteropolymer : Implications for Axonal Flexibility |
| topic | Cellular and Molecular Neuroscience, Biochemistry |
| url | http://dx.doi.org/10.1046/j.1471-4159.2000.0751475.x |