2018
DOI: 10.1093/nar/gky736
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Structural analysis of the ternary complex between lamin A/C, BAF and emerin identifies an interface disrupted in autosomal recessive progeroid diseases

Abstract: Lamins are the main components of the nucleoskeleton. Whereas their 3D organization was recently described using cryoelectron tomography, no structural data highlights how they interact with their partners at the interface between the inner nuclear envelope and chromatin. A large number of mutations causing rare genetic disorders called laminopathies were identified in the C-terminal globular Igfold domain of lamins A and C. We here present a first structural description of the interaction between the lamin A/… Show more

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Cited by 57 publications
(110 citation statements)
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References 67 publications
(92 reference statements)
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“…BAF directly binds to the LEM domain of the inner nuclear transmembrane proteins emerin [84] and LAP2ß [85], as well as to the Igfold of lamin A/C. Analysis of the 3D structure of the lamin A/C-BAF complex reveals that one Igfold domain binds to one BAF dimer [81]. Furthermore, almost all of the lamin A/C residues mutated in homozygous APS are on the surface binding to BAF (Fig.…”
Section: Recessive Mutations Causing Aps Disrupt the Lamin A/c-baf Inmentioning
confidence: 96%
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“…BAF directly binds to the LEM domain of the inner nuclear transmembrane proteins emerin [84] and LAP2ß [85], as well as to the Igfold of lamin A/C. Analysis of the 3D structure of the lamin A/C-BAF complex reveals that one Igfold domain binds to one BAF dimer [81]. Furthermore, almost all of the lamin A/C residues mutated in homozygous APS are on the surface binding to BAF (Fig.…”
Section: Recessive Mutations Causing Aps Disrupt the Lamin A/c-baf Inmentioning
confidence: 96%
“…The highly evolutionarily conserved protein BAF directly interacts with lamin A/C [80,81]. BAF is a small, 89-amino acid protein that forms obligate dimers, each subunit of which binds to doublestranded DNA (dsDNA) allowing BAF to bridge two strands of dsDNA [82,83].…”
Section: Recessive Mutations Causing Aps Disrupt the Lamin A/c-baf Inmentioning
confidence: 99%
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“…Recent findings have shown that deleting components of the LINC complex abolished control of endoreplication in myofibers nuclei by affecting the chromatin regulator BAF leading to an increase DNA content 36 . Mutations in nesprin-1 have been shown to reduce levels of Lamin A/C 37 , a known partner of BAF 38 , leading to changes in chromatin structure and aberrant expression of genes involved in differentiation 39 . We also observed a loss of Lamin C in CBs upon MSP-300 loss of function (data not shown).…”
Section: Cap and Msp-300 Are Required For Coordinated Cbs Migrationmentioning
confidence: 99%