Ultrastructure of the nuclear membrane of a Gregarine parasitic in grasshoppers

Beams, H. W.; Tahmisian, T. N.; Devine, R. L.; Anderson, Everett

doi:10.1016/0014-4827(57)90071-x

Cited by 64 publications

(26 citation statements)

References 20 publications

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“…The nuclear lamins are the major components of a filamentous layer, the nuclear lamina, that is closely associated with the inner nuclear membrane. This layer was originally described in ultrastructural studies of the protozoans Amoeba proteus (28,29) and Gregarina melanoplus (30), as well as in neurons of the leech Hirudo medicinalis (31,32), and often appeared to have a honeycomb structure. The first descriptions of a fibrous lamina in vertebrate cells came from EM observations of smooth muscle cells obtained from the guinea pig epididymis, intestinal epithelial cells from the Congo eel, and interstitial cells from the cat (33).…”

Section: Historical Overview Of Ifs Early Difficulties In the Recognimentioning

confidence: 92%

Introducing intermediate filaments: from discovery to disease

Eriksson

Dechat²,

Grin³

et al. 2009

J. Clin. Invest.

383

366

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It took more than 100 years before it was established that the proteins that form intermediate filaments (IFs) comprise a unified protein family, the members of which are ubiquitous in virtually all differentiated cells and present both in the cytoplasm and in the nucleus. However, during the past 2 decades, knowledge regarding the functions of these structures has been expanding rapidly. Many disease-related roles of IFs have been revealed. In some cases, the molecular mechanisms underlying these diseases reflect disturbances in the functions traditionally assigned to IFs, i.e., maintenance of structural and mechanical integrity of cells and tissues. However, many disease conditions seem to link to the nonmechanical functions of IFs, many of which have been defined only in the past few years.

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Section: Historical Overview Of Ifs Early Difficulties In the Recognimentioning

confidence: 92%

Introducing intermediate filaments: from discovery to disease

Eriksson

Dechat²,

Grin³

et al. 2009

J. Clin. Invest.

383

366

View full text Add to dashboard Cite

show abstract

“…A well organized lamina has been identified by TEM in several Protozoa species from diverse groups, including phylogenetically unrelated unicellular eukaryotes (Frajola et al, 1956; Pappas, 1956; Rudzinska, 1956; Beams et al, 1957; Lang and Loidl, 1993; Chen et al, 1994; Minguez et al, 1994), and it has also been isolated from Trypanosoma (Rout and Field, 2001; Figure 1 ). Except for that in Amoeba proteus and Gregarina melanopli (Frajola et al, 1956; Beams et al, 1957; Schmidt et al, 1995), the protozoan lamina resembles that of metazoans, particularly once isolated (Rout and Field, 2001). However, protozoa lack lamin orthologs and thus, their lamina is likely to be based on different proteins with similar functions.…”

Section: The Lamina In Non-metazoansmentioning

confidence: 99%

“…Although the first descriptions of the lamina in protozoa date from the 1950s (Pappas, 1956; Beams et al, 1957), it was not until it was described in mammalian cells that interest in the lamina became more widespread (Fawcett, 1966). Thin section TEM shows the lamina to be a thin fibrillar layer between the NE and the condensed chromatin masses (Pappas, 1956; Beams et al, 1957; Fawcett, 1966).…”

Section: The Metazoan Laminamentioning

confidence: 99%

“…Thin section TEM shows the lamina to be a thin fibrillar layer between the NE and the condensed chromatin masses (Pappas, 1956; Beams et al, 1957; Fawcett, 1966). The fibrous nature of the lamina was corroborated when its fibrils were seen to interconnect with the NPCs in NE fractions from amphibian oocytes (Scheer et al, 1976) and rat liver cells (Aaronson and Blobel, 1975; Dwyer and Blobel, 1976).…”

Section: The Metazoan Laminamentioning

confidence: 99%

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The intriguing plant nuclear lamina

Ciska

Espina

2014

Front. Plant Sci.

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The nuclear lamina is a complex protein mesh attached to the inner nuclear membrane (INM), which is also associated with nuclear pore complexes. It provides mechanical support to the nucleus and nuclear envelope, and as well as facilitating the connection of the nucleoskeleton to the cytoskeleton, it is also involved in chromatin organization, gene regulation, and signaling. In metazoans, the nuclear lamina consists of a polymeric layer of lamins and other interacting proteins responsible for its association with the INM and chromatin. In plants, field emission scanning electron microscopy of nuclei, and thin section transmission electron microscopy of isolated nucleoskeletons, reveals the lamina to have a similar structure to that of metazoans. Moreover, although plants lack lamin genes and the genes encoding most lamin-binding proteins, the main functions of the lamina are fulfilled in plants. Hence, it would appear that the plant lamina is not based on lamins and that other proteins substitute for lamins in plant cells. The nuclear matrix constituent proteins are the best characterized structural proteins in the plant lamina. Although these proteins do not display strong sequence similarity to lamins, their predicted secondary structure and sub-nuclear distribution, as well as their influence on nuclear size and shape, and on heterochromatin organization, suggest they could be functional lamin analogs. In this review we shall summarize what is currently known about the organization and composition of the plant nuclear lamina and its interacting complexes, and we will discuss the activity of this structure in the plant cell and its nucleus.

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“…The nuclear envelope consists of two lipid bilayers, the inner and outer nuclear membranes. [1][2][3][4][5][6][7][8][9] The isolation of a pore complex-lamina fraction from rat liver nuclei 10,11 and the immunohistochemical characterization of lamin proteins 12 established that lamins are the main components of the lamina. The nucleoplasmic side of the inner nuclear membrane of metazoans is closely associated with a fibrous protein network, the nuclear lamina.…”

Section: Introductionmentioning

confidence: 99%

Evolution of the lamin protein family

Peter

Stick

2012

Nucleus

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Lamins are the major components of the nuclear lamina, a filamentous layer found at the interphase between chromatin and the inner nuclear membrane. The lamina supports the nuclear envelope and provides anchorage sites for chromatin. Lamins and their associated proteins are required for most nuclear activities, mitosis, and for linking the nucleoskeleton to the network of cytoskeletal filaments. Mutations in lamins and their associated proteins give rise to a wide range of diseases, collectively called laminopathies. This review focuses on the evolution of the lamin protein family. Evolution from basal metazoans to man will be described on the basis of protein sequence comparisons and analyses of their gene structure. Lamins are the founding members of the family of intermediate filament proteins. How genes encoding cytoplasmic IF proteins could have arisen from the archetypal lamin gene progenitor, can be inferred from a comparison of the respective gene structures. The lamin/IF protein family seems to be restricted to the metazoans. In general, invertebrate genomes harbor only a single lamin gene encoding a B-type lamin. The archetypal lamin gene structure found in basal metazoans is conserved up to the vertebrate lineage. The completely different structure of lamin genes in Caenorhabditis and Drosophila are exceptions rather than the rule within their systematic groups. However, variation in the length of the coiled-coil forming central domain might be more common than previously anticipated. The increase in the number of lamin genes in vertebrates can be explained by two rounds of genome duplication. The origin of lamin A by exon shuffling might explain the processing of prelamin A to the mature non-isoprenylated form of lamin A. By alternative splicing the number of vertebrate lamin proteins has increased even further. Lamin C, an alternative splice form of the LMNA gene, is restricted to mammals. Amphibians and mammals express germline-specific lamins that differ in their protein structure from that of somatic lamins. Evidence is provided that there exist lamin-like proteins outside the metazoan lineage.

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Ultrastructure of the nuclear membrane of a Gregarine parasitic in grasshoppers

Cited by 64 publications

References 20 publications

Introducing intermediate filaments: from discovery to disease

Introducing intermediate filaments: from discovery to disease

The intriguing plant nuclear lamina

Evolution of the lamin protein family

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