The sequence of a cytoplasmic intermediate filament (IF) protein from theannelid <i>Lumbricus terrestris</i> emphasizes a distinctive feature of protostomic IF proteins

Bovenschulte, Marc; Riemer, Dieter; Weber, Klaus

doi:10.1016/0014-5793(95)00108-l

Cited by 13 publications

(2 citation statements)

References 20 publications

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“…There are many types of IF protein in vertebrates, most of which can be grouped into five classes: (1) type I (acidic) keratins; (2) type II (basic) keratins; (3) vimentin and desmin; (4) α-internexin and neurofilament proteins; and (5) lamins (Fuchs and Weber, 1994). Lamins are also present in protosomes, suggesting that all IF protein families are derived from a single lamin-like sequence in the common metazoan ancestor (Weber et al, 1989; Dodemont et al, 1994; Bovenschulte et al, 1995). Significantly, however, eukaryotic IF proteins have only been found unambiguously in animals and their relatives (Erber et al, 1998), suggesting that they are an innovation specific to this lineage and not present in the last eukaryotic common ancestor (LECA; see Fig.…”

Section: Filaments Iii: Intermediate Filamentsmentioning

confidence: 99%

The evolution of the cytoskeleton

Wickstead

Gull

2011

Journal of Cell Biology

273

216

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The cytoskeleton is a system of intracellular filaments crucial for cell shape, division, and function in all three domains of life. The simple cytoskeletons of prokaryotes show surprising plasticity in composition, with none of the core filament-forming proteins conserved in all lineages. In contrast, eukaryotic cytoskeletal function has been hugely elaborated by the addition of accessory proteins and extensive gene duplication and specialization. Much of this complexity evolved before the last common ancestor of eukaryotes. The distribution of cytoskeletal filaments puts constraints on the likely prokaryotic line that made this leap of eukaryogenesis.

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Section: Filaments Iii: Intermediate Filamentsmentioning

confidence: 99%

The evolution of the cytoskeleton

Wickstead

Gull

2011

Journal of Cell Biology

273

216

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“…In contrast to vertebrates, protostomic phyla display cytoplasmic IF proteins which have an extra 42 residues in their coil 1b domain and in most cases harbor a lamin homology segment of 120 residues in their tail domain. This was originally documented for molluscs, nematodes and annelids (Weber et al, 1988(Weber et al, , 1989Dodemont et al, 1990Dodemont et al, , 1994Szaro et al, 1991;Way et al, 1992;Tomarev et al, 1993 Bovenschulte et al, 1995;Johansen and Johansen, 1995) and more recently the long coil 1b version has also been found in eight further protostomic phyla (D.R., K.W., A. Erber and M. Bovenschulte, unpublished results). Parallel work showed that the short coil 1b version present in all vertebrate IF proteins also holds for the eight cytoplasmic IF proteins established for the cephalochordate Branchiostoma (Riemer et al, 1992(Riemer et al, , 1998.…”

Section: Introductionmentioning

confidence: 57%

Common and variant properties of intermediate filament proteins from lower chordates and vertebrates; two proteins from the tunicate Styela and the identification of a type III homologue

Riemer

Weber²

1998

Journal of Cell Science

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The chordates combine the vertebrates and the invertebrate phyla of the cephalo- and urochordates (tunicates). Two cytoplasmic intermediate filament (IF) proteins of the urochordate Styela plicata are characterized by cDNA cloning, gene organization, tissue specific expression patterns in the adult animal and the self assembly properties of the recombinant proteins. In line with metazoan phylogeny St-A and St-B have the short length version of the coil 1b domain found in all vertebrate and cephalochordate IF proteins while protostomic IF proteins have the longer length version with an extra 42 residues. St-A is the first IF protein from a lower chordate which can be unambiguously related to a particular vertebrate IF subfamily. St-A shares 46% sequence identity with desmin, displays the N-terminal motif necessary for filament assembly of type III proteins and forms normal homopolymeric 10 nm filaments in vitro. St-A but not St-B is present in smooth muscle cells of the body wall musculature. St-A and St-B are found as separate networks in some interior epithelia. St-B shares 30 to 35% identity with keratin 8, St-A and desmin and does not form IF under in vitro assembly conditions. Its relation to a particular vertebrate IF type or to the eight currently known IF proteins from the cephalochordate Branchiostoma remains unresolved. The striking relation between St-A and desmin predicts that the common progenitor of the urochordate (tunicate) and the cephalochordate/vertebrate lineages already possessed a type III homologue. Unlike in vertebrates intron patterns cannot be used to classify the tunicate IF genes. Although St-A is a type III homologue its gene shows an intron position which in vertebrates is restricted to keratin type II genes.

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Gliarin and macrolin, two novel intermediate filament proteins specifically expressed in sets and subsets of glial cells in leech central nervous system

Bolton

Zipser

et al. 1999

J. Neurobiol.

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Using monoclonal antibodies, we have identified two novel intermediate filament (IF) proteins, Gliarin and Macrolin, which are specifically expressed in the central nervous system of an invertebrate. The two proteins both contain the coiled‐coil rod domain typical of the superfamily of IF proteins flanked by unique N‐ and C‐terminal domains. Gliarin was found in all glial cells including macro‐ and microglial cells, whereas Macrolin was expressed in only a single pair of giant connective glial cells. The identification of Macrolin and Gliarin together with the characterization of the strictly neuronal IF protein Filarin in leech central nervous system demonstrate that multiple neuron‐ and glial‐specific IFs are not unique to the vertebrate nervous system but are also found in invertebrates. Interestingly, phylogenetic analysis based on maximum parsimony indicated that the presence of neuron‐ and glial cell–specific IFs in coelomate protostomes as well as in vertebrates is not of monophyletic origin, but rather represents convergent evolution and appears to have arisen independently. © 1999 John Wiley & Sons, Inc. J Neurobiol 40: 244–253, 1999

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The sequence of a cytoplasmic intermediate filament (IF) protein from theannelid Lumbricus terrestris emphasizes a distinctive feature of protostomic IF proteins

Abstract: Materials and methods

Cited by 13 publications

References 20 publications

The evolution of the cytoskeleton

The evolution of the cytoskeleton

Common and variant properties of intermediate filament proteins from lower chordates and vertebrates; two proteins from the tunicate Styela and the identification of a type III homologue

Gliarin and macrolin, two novel intermediate filament proteins specifically expressed in sets and subsets of glial cells in leech central nervous system

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