Evolutionary changes in lamin expression in the vertebrate lineage

Stick, Reimer; Peter, Annette

doi:10.1080/19491034.2017.1303592

Cited by 4 publications

(3 citation statements)

References 60 publications

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“…Instead, PKC sites are used for depolymerization of Ce-lamin filaments mediated by phosphorylation. Some invertebrates may have more than a single lamin gene [ 18 – 21 ].…”

Section: Laminsmentioning

confidence: 99%

“…The presence of two lamin genes coding for lamin Dm and lamin C, which respectively correspond to B-type lamin and A-type lamin of vertebrates, makes the fly system a useful tool for studies of laminopathies. Although the fly lamin C gene originated from duplicated ancestor gene for lamin Dm, lamin C evolved to gain structural and functional similarity to lamin A-type proteins of vertebrates [ 18 , 20 , 21 , 28 , 49 , 57 ].…”

Section: Drosophila Lamin Cmentioning

confidence: 99%

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Laminopathies: what can humans learn from fruit flies

et al. 2018

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Lamin proteins are type V intermediate filament proteins (IFs) located inside the cell nucleus. They are evolutionarily conserved and have similar domain organization and properties to cytoplasmic IFs. Lamins provide a skeletal network for chromatin, the nuclear envelope, nuclear pore complexes and the entire nucleus. They are also responsible for proper connections between the karyoskeleton and structural elements in the cytoplasm: actin and the microtubule and cytoplasmic IF networks. Lamins affect transcription and splicing either directly or indirectly. Translocation of active genes into the close proximity of nuclear lamina is thought to result in their transcriptional silencing. Mutations in genes coding for lamins and interacting proteins in humans result in various genetic disorders, called laminopathies. Human genes coding for A-type lamin (LMNA) are the most frequently mutated. The resulting phenotypes include muscle, cardiac, neuronal, lipodystrophic and metabolic pathologies, early aging phenotypes, and combined complex phenotypes. The Drosophila melanogaster genome codes for lamin B-type (lamin Dm), lamin A-type (lamin C), and for LEM-domain proteins, BAF, LINC-complex proteins and all typical nuclear proteins. The fruit fly system is simpler than the vertebrate one since in flies there is only single lamin B-type and single lamin A-type protein, as opposed to the complex system of B- and A-type lamins in Danio, Xenopus and Mus musculus. This offers a unique opportunity to study laminopathies. Applying genetic tools based on Gal4 and in vitro nuclear assembly system to the fruit fly model may successfully advance knowledge of laminopathies. Here, we review studies of the laminopathies in the fly model system.Electronic supplementary materialThe online version of this article (10.1186/s11658-018-0093-1) contains supplementary material, which is available to authorized users.

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“…Instead, PKC sites are used for depolymerization of Ce-lamin filaments mediated by phosphorylation. Some invertebrates may have more than a single lamin gene [ 18 – 21 ].…”

Section: Laminsmentioning

confidence: 99%

Section: Drosophila Lamin Cmentioning

confidence: 99%

Laminopathies: what can humans learn from fruit flies

et al. 2018

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“…2A). This may indicate that the NL is a dynamic structure that varies between species, cell types and during differentiation [50][51][52][53]. Additional studies using cryo-ET as the method of choice or complementary approaches are needed in order to characterize the structural heterogeneity of lamins and the NL at a close-to-native state and providing mechanistic and functional insights.…”

Section: Lamina Organizationmentioning

confidence: 99%

Scaffold, mechanics and functions of nuclear lamins

Buxboim,

Kronenberg‐Tenga,

Salajkova

et al. 2023

FEBS Letters

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Nuclear lamins are type‐V intermediate filaments that are involved in many nuclear processes. In mammals, A‐ and B‐type lamins assemble into separate physical meshwork underneath the inner nuclear membrane, the nuclear lamina, with some residual fraction localized within the nucleoplasm. Lamins are the major part of the nucleoskeleton, providing mechanical strength and flexibility to protect the genome and allow nuclear deformability, while also contributing to gene regulation via interactions with chromatin. While lamins are the evolutionary ancestors of all intermediate filament family proteins, their ultimate filamentous assembly is markedly different from their cytoplasmic counterparts. Interestingly, hundreds of genetic mutations in the lamina proteins have been causally linked with a broad range of human pathologies, termed laminopathies. These include muscular, neurological and metabolic disorders, as well as premature aging diseases. Recent technological advances have contributed to resolving the filamentous structure of lamins and the corresponding lamina organization. In this review, we revisit the multiscale lamin organization and discuss its implications on nuclear mechanics and chromatin organization within lamina‐associated domains.

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Evolution of the lamin protein family at the base of the vertebrate lineage

Stick

Peter

2019

Cell Tissue Res

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Evolutionary changes in lamin expression in the vertebrate lineage

Cited by 4 publications

References 60 publications

Laminopathies: what can humans learn from fruit flies

Laminopathies: what can humans learn from fruit flies

Scaffold, mechanics and functions of nuclear lamins

Evolution of the lamin protein family at the base of the vertebrate lineage

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