Evolution of homologous domains of cytoplasmic intermediate filament proteins and lamins.
The earliest gene duplications in the evolution of the intermediate filament proteins created the ancestors of acidic keratins, basic keratins, nonepithelial intermediate filament proteins, and lamins. Biochemistry and function of cytoplasmic intermediate filaments differ greatly from those of lamins. Cytoplasmic intermediate filament proteins have a different cellular location than lamins, form different types of supramolecular structures, and are missing a protein segment found in lamins; but the data presented here indicate that the cytoplasmic intermediate filaments do not have a common ancestor separate from the ancestor of lamins. In the non-epithelial intermediate filament branch, the ancestor of neurofilament proteins and the common ancestor of desmin, vimentin, and glial fibrillary acidic protein (GFAP) diverged first. By evolutionary criteria, the intermediate filament protein recently discovered in neuronal cells does not belong to the neurofilament family but is more closely related to desmin, vimentin, and GFAP. Sequences of different sub-domains yield different evolutionary trees, possibly indicating existence of sub-domain-specific functions.
Blumenberg
M
M
Department of Dermatology, New York University Medical Center, New York 10016.
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D006801:Humans; D007381:Intermediate Filament Proteins / Q000235:genetics*; D034882:Lamins; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000235:genetics*; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
D007381:Intermediate Filament Proteins; D034882:Lamins; D009687:Nuclear Proteins