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Updated: Jul 11, 2026

Following the Dynamics of Structural Variants in Experimentally Evolved Populations
Published on: February 3, 2023
Molecular evolution of type VI intermediate filament proteins
Dominique Guérette1, Paul A Khan, Pierre E Savard
1CREFSIP and Département de médecine, Pavillon Charles-Eugène-Marchand, Université Laval, Québec, G1K 7P4, Canada. doguerette@gmail.com
Type VI intermediate filament (IF) proteins like tanabin, transitin, and nestin are evolutionarily related. Rapid C-terminal evolution drives their distinct functions, with avian transitin showing nucleotide hydrolysis activity not found in mammalian nestin.
Area of Science:
- Evolutionary biology
- Molecular biology
- Cell biology
Background:
- Tanabin, transitin, and nestin are developmentally regulated type VI intermediate filament (IF) proteins found in various species.
- These IF proteins share an alpha-helical core domain but possess distinct C-terminal tails with repeated motifs.
- The molecular evolution of type VI IF proteins is not well understood.
Purpose of the Study:
- To investigate the evolutionary history and relationships of type VI IF proteins.
- To identify orthologous proteins and understand their gene structure and conservation.
- To explore the functional implications of C-terminal tail variations.
Main Methods:
- Sequence comparisons and BLAST searches
- Synteny studies and phylogenetic analyses
- In silico and in vitro analyses of protein tail domains
Main Results:
- Tanabin, transitin, and nestin are confirmed as orthologous type VI IF proteins.
- Homologous genes share intron positions, sequence identities, and chromosomal context.
- Avian transitin possesses a nucleotide hydrolysis-active repeat domain in its tail, unlike mammalian nestin.
Conclusions:
- Type VI IFs represent a distinct evolutionary branch separate from NF proteins.
- Synemin and nestin orthologs constitute the major type VI IF proteins.
- Rapid C-terminal evolution likely accounts for the divergent functions of nestin orthologs.
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