PUBLICATION
Plasticin, a type III neuronal intermediate filament protein, assembles as an obligate heteropolymer: Implications for axonal flexibility
- Authors
- Asch, W.S. and Schechter, N.
- ID
- ZDB-PUB-001003-4
- Date
- 2000
- Source
- Journal of neurochemistry 75(4): 1475-1486 (Journal)
- Registered Authors
- Asch, William S., Schechter, Nisson
- Keywords
- neurofilament; zebrafish; cytoskeleton; axonogenesis
- MeSH Terms
-
- Amino Acid Substitution
- Animals
- Axons/metabolism*
- Biopolymers/metabolism
- Catalysis
- Cell Line
- Epidermolysis Bullosa Simplex/genetics
- Eye Proteins/genetics
- Eye Proteins/metabolism*
- Hemagglutinins/genetics
- Humans
- Immunohistochemistry
- Intermediate Filament Proteins/genetics*
- Intermediate Filament Proteins/metabolism*
- Intermediate Filaments/genetics
- Intermediate Filaments/metabolism
- Intermediate Filaments/ultrastructure
- Mutagenesis, Site-Directed
- Nerve Tissue Proteins/genetics
- Nerve Tissue Proteins/metabolism*
- Neurons/metabolism*
- Neurons/ultrastructure
- Phenotype
- Recombinant Fusion Proteins/genetics
- Recombinant Fusion Proteins/metabolism
- Temperature
- Transfection
- Vimentin/genetics
- Vimentin/metabolism
- Zebrafish
- PubMed
- 10987827 Full text @ J. Neurochem.
Citation
Asch, W.S. and Schechter, N. (2000) Plasticin, a type III neuronal intermediate filament protein, assembles as an obligate heteropolymer: Implications for axonal flexibility. Journal of neurochemistry. 75(4):1475-1486.
Abstract
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(-) cells but efficiently coassembles with vimentin in SW13c1.1Vim(-) cells. By cotransfecting plasticin and vimentin in SW13c1.1Vim(-) 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(+) cells, a point mutation in the first heptad of the alpha-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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping