Barrier-to-autointegration factor – a BAFfling little protein

Margalit, Ayelet; Brachner, Andreas; Gotzmann, Josef; Foisner, Roland; Gruenbaum, Yosef

doi:10.1016/j.tcb.2007.02.004

Cited by 148 publications

(159 citation statements)

References 62 publications

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“…BAF is located in the nucleoplasm, cytoplasm and nuclear membrane and its intracellular distribution has been recently shown to vary according to the cell cycle, with nuclear localization during progression of S phase. [16][17][18] The regulation of BAF depends on its modification state and binding partners in the nucleus and nuclear membrane. 16,19,20 Recently, new BAF binding partners have been identified with chromatin-regulatory function.…”

Section: Resultsmentioning

confidence: 99%

“…[16][17][18] The regulation of BAF depends on its modification state and binding partners in the nucleus and nuclear membrane. 16,19,20 Recently, new BAF binding partners have been identified with chromatin-regulatory function. In particular, it has been reported that BAF and emerin dynamically interact with DNA damage response proteins of the CUL4-DDB-ROC1 complex.…”

Section: Resultsmentioning

confidence: 99%

“…16 It forms stable dimers and binds the dsDNA phosphate backbone without sequence specificity. 29 In addition BAF shows heterogeneous localization between the nucleus and cytoplasm, and becomes nucleo-specific when the cells are synchronized in S phase.…”

Section: Discussionmentioning

confidence: 99%

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Lamin A precursor induces barrier-to-autointegration factor nuclear localization

Capanni¹,

Cenni²,

Haraguchi

et al. 2010

Cell Cycle

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Lamin A, a protein component of the nuclear lamina, is synthesized as a precursor named prelamin A, whose multi-step maturation process involves different protein intermediates. As demonstrated in laminopathies such as familial partial lipodystrophy, mandibuloacral dysplasia, Werner syndrome, Hutchinson-Gilford progeria syndrome and restrictive dermopathy, failure of prelamin A processing results in the accumulation of lamin A protein precursors inside the nucleus which dominantly produces aberrant chromatin structure. To understand if nuclear lamina components may be involved in prelamin A chromatin remodeling effects, we investigated barrier-to-autointegration factor (BAF) localization and expression in prelamin A accumulating cells. BAF is a DNA-binding protein that interacts directly with histones, lamins and LEM-domain proteins and has roles in chromatin structure, mitosis and gene regulation. In this study, we show that the BAF heterogeneous localization between nucleus and cytoplasm observed in HEK293 cycling cells changes in response to prelamin A accumulation. In particular, we observed that the accumulation of lamin A, non-farnesylated prelamin A and farnesylated carboxymethylated lamin A precursors induce BAF nuclear translocation. Moreover, we show that the treatment of human fibroblasts with prelamin A interfering drugs results in similar changes. Finally, we report that the accumulation of progerin, a truncated form of farnesylated and carboxymethylated prelamin A identified in Hutchinson-Gilford progeria syndrome cells, induces BAF recruitment in the nucleus. These findings are supported by coimmunoprecipitation of prelamin A or progerin with BAF in vivo and suggest that BAF could mediate prelamin A-induced chromatin effects

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Lamin A precursor induces barrier-to-autointegration factor nuclear localization

Capanni¹,

Cenni²,

Haraguchi

et al. 2010

Cell Cycle

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“…Two small proteins that are likely to be important to chromatin folding are high-mobility-group (HMG) proteins, and the barrier-to-integration-factor (BAF-1) protein (Margalit et al 2007), which are present in mitotic chromosomes in numbers comparable to those of histones (Uchiyama et al 2005). HMG proteins are divided into three families with different functions (Hock et al 2007): HMGA proteins bind AT-rich DNA, HMGB proteins bend DNA (Thomas & Travers 2001), and HMGN proteins reorganize nucleosomes.…”

Section: Chromatin Fibrementioning

confidence: 99%

Micromechanical studies of mitotic chromosomes

2008

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Mitotic chromosomes respond elastically to forces in the nanonewton range, a property important to transduction of stresses used as mechanical regulatory signals during cell division. In addition to being important biologically, chromosome elasticity can be used as a tool for investigating the folding of chromatin. This paper reviews experiments studying stretching and bending stiffness of mitotic chromosomes, plus experiments where changes in chromosome elasticity resulting from chemical and enzyme treatments were used to analyse connectivity of chromatin inside chromosomes. Experiments with nucleases indicate that non-DNA elements constraining mitotic chromatin must be isolated from one another, leading to the conclusion that mitotic chromosomes have a chromatin Fnetwork_ or Fgel_ organization, with stretches of chromatin strung between Fcrosslinking_ points. The as-yet unresolved questions of the identities of the putative chromatin crosslinkers and their organization inside mitotic chromosomes are discussed.

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“…BAF directly cross-bridges and "loops" dsDNA in vitro (95)(96)(97), condenses chromatin (66), mediates chromatin attachment to the nuclear lamina (98,99), associates with telomeres and "core" regions of chromatin during mitosis (5, 6, 100), and protects chromatin from DNA damage (101). Our discovery that GFP-emerin and BAF associate only in the N S fraction, when both were also abundant in N E , provides a vital new tool for isolating endogenous BAF and testing its proposed role in linking chromatin to other major "lamina" components (emerin and lamins) in mammalian cells.…”

Section: Discussionmentioning

confidence: 99%

O-Linked β-N-Acetylglucosamine (O-GlcNAc) Regulates Emerin Binding to Barrier to Autointegration Factor (BAF) in a Chromatin- and Lamin B-enriched “Niche”

Berk

Maitra

Dawdy

et al. 2013

Journal of Biological Chemistry

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Background: Nuclear membrane protein emerin binding to nuclear intermediate filaments (lamins) and BAF contributes to forming a nuclear "lamina" structure. Results: Emerin is O-GlcNAc-modified at eight sites: two (Ser-53 and Ser-54) influence further O-GlcNAcylation, and one (Ser-173) regulates association with BAF in the chromatin/lamin B "niche." Conclusion: O-GlcNAc transferase, a nutrient-responsive enzyme, regulates emerin. Significance: Emerin hyper-O-GlcNAcylation may contribute to cardiomyopathy and other conditions.

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Barrier-to-autointegration factor – a BAFfling little protein

Cited by 148 publications

References 62 publications

Lamin A precursor induces barrier-to-autointegration factor nuclear localization

Lamin A precursor induces barrier-to-autointegration factor nuclear localization

Micromechanical studies of mitotic chromosomes

O-Linked β-N-Acetylglucosamine (O-GlcNAc) Regulates Emerin Binding to Barrier to Autointegration Factor (BAF) in a Chromatin- and Lamin B-enriched “Niche”

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