Abstract
The major constituents of mammalian neurofilaments are the three triplet proteins of molecular weight 200,000 (200K), 145K and 68K, which also co-migrate in slow axonal transport1–5. Partial amino acid sequence data6 and chemical cleavage patterns7,8 indicate that various cell-specific non-neuronal intermediate filament proteins having molecular weights between 40,000 and 70,000 are structurally related, consistent with a common filament morphology. Here we extend this principle to the neurofilament 68K triplet protein, NF68. We show that NF68, muscle-specific desmin (52K) and mesenchymally derived vimentin (55K) are related proteins. Direct amino acid sequence analysis of a uniquely positioned marker peptide (5K) shows that in this region, NF68 shows ∼42% sequence identity with vimentin and desmin, which have ∼70% identity. These results are discussed with respect to neurofilament organization.
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Geisler, N., Plessmann, U. & Weber, K. Related amino acid sequences in neurofilaments and non-neuronal intermediate filaments. Nature 296, 448–450 (1982). https://doi.org/10.1038/296448a0
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DOI: https://doi.org/10.1038/296448a0
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