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Open Access Open Badges Research article

Molecular evolution of type VI intermediate filament proteins

Dominique Guérette1, Paul A Khan2, Pierre E Savard3 and Michel Vincent1*

Author Affiliations

1 CREFSIP and Département de médecine, Pavillon Charles-Eugène-Marchand, Université Laval, Québec, G1K 7P4, Canada

2 Unité de recherche en pédiatrie, Centre de recherche du CHUL, Université Laval, Québec, G1V 4G2, Canada

3 Unité de recherche en Neurosciences, Centre de recherche du CHUL, Université Laval, Québec, G1V 4G2, Canada

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BMC Evolutionary Biology 2007, 7:164  doi:10.1186/1471-2148-7-164

Published: 13 September 2007



Tanabin, transitin and nestin are type VI intermediate filament (IF) proteins that are developmentally regulated in frogs, birds and mammals, respectively. Tanabin is expressed in the growth cones of embryonic vertebrate neurons, whereas transitin and nestin are found in myogenic and neurogenic cells. Another type VI IF protein, synemin, is expressed in undifferentiated and mature muscle cells of birds and mammals. In addition to an IF-typical α-helical core domain, type VI IF proteins are characterized by a long C-terminal tail often containing distinct repeated motifs. The molecular evolution of type VI IF proteins remains poorly studied.


To examine the evolutionary history of type VI IF proteins, sequence comparisons, BLAST searches, synteny studies and phylogenic analyses were performed. This study provides new evidence that tanabin, transitin and nestin are indeed orthologous type VI IF proteins. It demonstrates that tanabin, transitin and nestin genes share intron positions and sequence identities, have a similar chromosomal context and display closely related positions in phylogenic analyses. Despite this homology, fast evolution rates of their C-terminal extremity have caused the appearance of repeated motifs with distinct biological activities. In particular, our in silico and in vitro analyses of their tail domain have shown that (avian) transitin, but not (mammalian) nestin, contains a repeat domain displaying nucleotide hydrolysis activity.


These analyses of the evolutionary history of the IF proteins fit with a model in which type VI IFs form a branch distinct from NF proteins and are composed of two major proteins: synemin and nestin orthologs. Rapid evolution of the C-terminal extremity of nestin orthologs could be responsible for their divergent functions.