Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1

Ruan, Jianbin; Xu, Chao; Bian, Chuanbing; Lam, Robert; Wang, Jia-Pey; Kania, Joanna; Min, Jinrong; Zang, Jianye

doi:10.1016/j.febslet.2012.01.007

Cited by 34 publications

(25 citation statements)

References 19 publications

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“…Due to the challenge of crystallizing filamentous proteins, crystallographic analysis has been restricted to smaller lamin fragments, including the coil 2B of lamin A/C [53] and lamin B1 [54], along with the lamin A/C globular tail [55]. Combined with in vitro assembly experiments using lamin mutations and partial deletions, these studies indicate that the supramolecular assembly of lamins largely depends on interactions within the lamin rod domains and the N-terminal head domain [52].…”

Section: Broken Nuclei Lead To Broken Hearts (And Muscle) – the Effecmentioning

confidence: 99%

Broken nuclei – lamins, nuclear mechanics, and disease

Davidson

Lammerding

2014

Trends in Cell Biology

250

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Mutations in lamins, which are ubiquitous nuclear intermediate filaments, lead to a variety of disorders, including muscular dystrophy and dilated cardiomyopathy. Lamins provide nuclear stability, help connect the nucleus to the cytoskeleton, and can modulate chromatin organization and gene expression. Nonetheless, the diverse functions of lamins remain incompletely understood. Here, we focus on the role of lamins on nuclear mechanics and its implication in human diseases. Recent findings suggest that lamin mutations can decrease nuclear stability, increase nuclear fragility, and disturb mechanotransduction signaling, possibly explaining the muscle-specific defects in many laminopathies. At the same time, altered lamin expression has been reported in many cancers, where the resulting increased nuclear deformability could enhance the ability of cells to transit tight interstitial spaces, promoting metastasis.

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Section: Broken Nuclei Lead To Broken Hearts (And Muscle) – the Effecmentioning

confidence: 99%

Broken nuclei – lamins, nuclear mechanics, and disease

Davidson

Lammerding

2014

Trends in Cell Biology

250

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“…Arrow indicates the Zmpste24 cleavage site in pre-lamin A (plamA cleavage). Underlined residues in (B) comprise the lamin Ig-fold domain (Dhe-Paganon et al 2002; Krimm et al 2002; Ruan et al 2012). …”

Section: Figurementioning

confidence: 99%

Partners and post-translational modifications of nuclear lamins

2013

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Nuclear intermediate filament networks formed by A- and B-type lamins are major components of the nucleoskeleton that are required for nuclear structure and function, with many links to human physiology. Mutations in lamins cause diverse human diseases (‘laminopathies’). At least fifty-four partners interact with human A-type lamins directly or indirectly. The less studied human lamins B1 and B2 have twenty-three and seven reported partners, respectively. These interactions are likely to be regulated at least in part by lamin post-translational modifications. This review summarizes the binding partners and post-translational modifications of human lamins and discusses their known or potential implications for lamin function.

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“…The first atomic structure of a lamin fragment was obtained from the globular tail domain (amino acids 436-552) of human lamin A/C, showing that this fragment formed a sandwich of two b-sheets, a structure which is referred to as an Ig domain (Dhe-Paganon et al 2002). Later, the crystal structure of the lamin B1 Ig domain was determined, and as expected, given the high sequence similarity between the two proteins, the overall structure of the lamin A and B1 globular tail domain is very similar (Ruan et al 2012). X-ray crystallography was successfully applied to determine the atomic structure of lamin A coil 2B (amino acids 305-387), which represents the last part of the central coiled-coil domain.…”

Section: Structural Determination Of Lamin Proteinsmentioning

confidence: 66%

From lamins to lamina: a structural perspective

Zwerger

Medalia

2013

Histochem Cell Biol

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Lamin proteins are the major constituents of the nuclear lamina, a proteinaceous network that lines the inner nuclear membrane. Primarily, the nuclear lamina provides structural support for the nucleus and the nuclear envelope; however, lamins and their associated proteins are also involved in most of the nuclear processes, including DNA replication and repair, regulation of gene expression, and signaling. Mutations in human lamin A and associated proteins were found to cause a large number of diseases, termed 'laminopathies.' These diseases include muscular dystrophies, lipodystrophies, neuropathies, and premature aging syndromes. Despite the growing number of studies on lamins and their associated proteins, the molecular organization of lamins in health and disease is still elusive. Likewise, there is no comprehensive view how mutations in lamins result in a plethora of diseases, selectively affecting different tissues. Here, we discuss some of the structural aspects of lamins and the nuclear lamina organization, in light of recent results.

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Crystal structures of the coil 2B fragment and the globular tail domain of human lamin B1

Cited by 34 publications

References 19 publications

Broken nuclei – lamins, nuclear mechanics, and disease

Broken nuclei – lamins, nuclear mechanics, and disease

Partners and post-translational modifications of nuclear lamins

From lamins to lamina: a structural perspective

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