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Barrier to autointegration factor 1

BAF, barrier-to-autointegration factor
The protein encoded by this gene was first identified by its ability to protect retroviruses from intramolecular integration and therefore promote intermolecular integration into the host cell genome. The protein forms a homodimer which localizes to both the nucleus and cytoplasm and is specifically associated with chromosomes during mitosis. This protein binds to double stranded DNA in a non-specific manner and also binds to LEM-domain containing proteins of the nuclear envelope. This protein is thought to facilitate nuclear reassembly by binding with both DNA and inner nuclear membrane proteins and thereby recruit chromatin to the nuclear periphery. Alternative splicing results in multiple transcript variants encoding the same protein.[provided by RefSeq, Jan 2009] (from NCBI)
Top mentioned proteins: CAN, SWI, BRG1, ATPase, PrP
Papers using BAF antibodies
Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1
Hetzer Martin W. et al., In The Journal of Cell Biology, 1995
... Antibodies against V5 (mouse [Invitrogen] and rabbit [Novus Biologicals]), BAF (Novus Biologicals), Sun1 (Abcam), tubulin (Sigma-Aldrich), ...
Papers on BAF
Sidt2 is involved in the NAADP-mediated release of calcium from insulin secretory granules.
Zhang et al., Shanghai, China. In J Mol Endocrinol, Feb 2016
Extraordinarily, pretreatment with bafilomycin A1(Baf-A1) led to a comparable [Ca2+]i increase pattern between these two groups, suggesting that calcium traffic from the intracellular acidic compartment is defective in Sidt2-/- β-cells.
(1)H, (13)C and (15)N backbone resonance assignment of the intrinsically disordered region of the nuclear envelope protein emerin.
Zinn-Justin et al., Gif-sur-Yvette, France. In Biomol Nmr Assign, Feb 2016
The three-dimensional structure of this LEM domain in complex with the chromatin BAF protein was solved from NMR data.
Simple Separation of Functionally Distinct Populations of Lamin-Binding Proteins.
Wilson et al., Baltimore, United States. In Methods Enzymol, Dec 2015
This protocol was developed for emerin, an inner nuclear membrane protein that binds lamins and barrier-to-autointegration factor (BANF1) as a component of nuclear lamina structure, and has diverse roles in nuclear assembly, signaling, and gene regulation.
Purification and Structural Analysis of LEM-Domain Proteins.
Zinn-Justin et al., Paris, France. In Methods Enzymol, Dec 2015
The LEM domain binds to BAF (barrier-to-autointegration factor; BANF1), which interacts with DNA and tethers chromatin to the nuclear envelope.
Selective targeting of the BRG/PB1 bromodomains impairs embryonic and trophoblast stem cell maintenance.
Müller et al., Oxford, United Kingdom. In Sci Adv, Nov 2015
BAF complexes contain an ATP (adenosine 5'-triphosphate)-driven remodeling enzyme (either BRG1 or BRM) and multiple protein interaction domains including bromodomains, an evolutionary conserved acetyl lysine-dependent protein interaction motif that recruits transcriptional regulators to acetylated chromatin.
Linker histones in hormonal gene regulation.
Beato et al., Spain. In Biochim Biophys Acta, Nov 2015
Similarly, during hormone-dependent gene repression a dedicated enzymatic mechanism controls H1 deposition at promoters by a complex containing HP1γ, LSD1 and BRG1, the ATPase of the BAF complex.
SMARCA4 inactivation defines a group of undifferentiated thoracic malignancies transcriptionally related to BAF-deficient sarcomas.
Tirode et al., Lyon, France. In Nat Genet, Oct 2015
While investigating cohorts of unclassified sarcomas by RNA sequencing, we identified 19 cases with inactivation of SMARCA4, which encodes an ATPase subunit of BAF chromatin-remodeling complexes.
Barrier to Autointegration Factor (BANF1): interwoven roles in nuclear structure, genome integrity, innate immunity, stress responses and progeria.
Wiebe et al., Lincoln, United States. In Curr Opin Cell Biol, Jun 2015
The Barrier to Autointegration Factor (BAF or BANF1) is an abundant, highly conserved DNA binding protein.
[Structure and biological functions of mammalian LEM-domain proteins].
Zhengmao et al., Tianjin, China. In Yi Chuan, Feb 2015
Recent studies demonstrated that LEM-domain protein family mediates interactions among inner nuclear membrane, nuclear lamina protein and chromatin by interacting with barrier-to-autointegration-factor (BAF).
Toward understanding the role of the neuron-specific BAF chromatin remodeling complex in memory formation.
Han et al., Taejŏn, South Korea. In Exp Mol Med, 2014
A few recent studies have implicated the Brm/Brg-associated factor (BAF) chromatin-remodeling complex, a mammalian homolog of the yeast Swi/Snf complex, in neuronal structural/functional plasticity and memory formation.
S1P signaling: new therapies and opportunities.
Rosen et al., Los Angeles, United States. In F1000prime Rep, 2013
Proof-of-concept studies across validated animal models with S1P receptor modulators highly selective for S1P1, such as BAF-312 (Siponimod), KRP-203, ONO-4641 (Ceralifimod), ponesimod and RPC-1063, and emerging clinical trials for safety and efficacy in humans, particularly in MS, ulcerative colitis (UC) and psoriasis, have set the stage for us to consider additional testing in various other autoimmune diseases.
The BAF complex interacts with Pax6 in adult neural progenitors to establish a neurogenic cross-regulatory transcriptional network.
Götz et al., München, Germany. In Cell Stem Cell, 2013
Here, we report that the transcription factor Pax6 directly interacts with the Brg1-containing BAF complex in adult neural progenitors.
BAF complexes facilitate decatenation of DNA by topoisomerase IIα.
Crabtree et al., Stanford, United States. In Nature, 2013
Recent exon-sequencing studies of human tumours have revealed that subunits of BAF (mammalian SWI/SNF) complexes are mutated in more than 20% of all human malignancies, but the mechanisms involved in tumour suppression are unclear.
Synovial sarcoma mechanisms: a series of unfortunate events.
Svejstrup, London, United Kingdom. In Cell, 2013
Kadoch and Crabtree now show that the resulting cellular transformation stems from disruption of the normal architecture and function of the human SWI/SNF (BAF) complex.
Reversible disruption of mSWI/SNF (BAF) complexes by the SS18-SSX oncogenic fusion in synovial sarcoma.
Crabtree et al., Stanford, United States. In Cell, 2013
Recent exon sequencing studies have revealed that over 20% of human tumors have mutations in subunits of mSWI/SNF (BAF) complexes.
Molecular characterization of the host defense activity of the barrier to autointegration factor against vaccinia virus.
Wiebe et al., Lincoln, United States. In J Virol, 2011
The authors demonstrate that the DNA binding and dimerization capabilities of BAF are essential for its function as an antipoxviral effector, while the presence of emerin is not required.
Néstor-Guillermo progeria syndrome: a novel premature aging condition with early onset and chronic development caused by BANF1 mutations.
López-Otín et al., Spain. In Am J Med Genet A, 2011
A single copy of normal BANF1 is sufficient to avoid the development of Nestor-Guillermo progeria syndrome.
Barrier-to-Autointegration Factor influences specific histone modifications.
Wilson et al., Baltimore, United States. In Nucleus, 2011
BAF associated in vivo with SET/I2PP2A (protein phosphatase 2A inhibitor; blocks H3 dephosphorylation) and G9a (H3-K9 methyltransferase), but showed no detectable association with HDAC1 or HATs.
Banf1 is required to maintain the self-renewal of both mouse and human embryonic stem cells.
Rizzino et al., Omaha, United States. In J Cell Sci, 2011
Data determined that the knockdown of Banf1 alters the cell cycle distribution of both human and mouse ESCs by causing an uncharacteristic increase in the proportion of cells in the G2-M phase of the cell cycle.
No interaction of barrier-to-autointegration factor (BAF) with HIV-1 MA, cone-rod homeobox (Crx) or MAN1-C in absence of DNA.
Craigie et al., Bethesda, United States. In Plos One, 2010
The absence of direct binding of BAF to MAN1-C eliminates disruption of this interaction as the cause of the premature aging phenotype.
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