Nuclear actin is involved in the regulation of CSF1 gene transcription in a chromatin required, BRG1 independent manner

2007 ◽  
Vol 102 (2) ◽  
pp. 403-411 ◽  
Author(s):  
Zhaoxia Song ◽  
Min Wang ◽  
Xiaoguang Wang ◽  
Xuefang Pan ◽  
Wenguang Liu ◽  
...  
Keyword(s):  
Gene Transcription ◽  
Nuclear Actin ◽  
Independent Manner

scholarly journals DNA Damage Induces Dynamic Associations of BRD4/P-TEFb With Chromatin and Modulates Gene Transcription in a BRD4-Dependent and -Independent Manner

2020 ◽  
Vol 7 ◽  
Author(s):  
Yawei Song ◽  
Gongcheng Hu ◽  
Jinping Jia ◽  
Mingze Yao ◽  
Xiaoshan Wang ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Gene Transcription ◽  
Map Kinases ◽  
Transcriptional Elongation ◽  
Dependent Manner ◽  
Rna Seq ◽  
Mitotic Chromosomes ◽  
Uv Treatment ◽  
Independent Manner ◽  
Uv Stress

The bromodomain-containing protein BRD4 has been thought to transmit epigenetic information across cell divisions by binding to both mitotic chromosomes and interphase chromatin. UV-released BRD4 mediates the recruitment of active P-TEFb to the promoter, which enhances transcriptional elongation. However, the dynamic associations between BRD4 and P-TEFb and BRD4-mediated gene regulation after UV stress are largely unknown. In this study, we found that BRD4 dissociates from chromatin within 30 min after UV treatment and thereafter recruits chromatin. However, P-TEFb binds tightly to chromatin right after UV treatment, suggesting that no interactions occur between BRD4 and P-TEFb within 30 min after UV stress. BRD4 knockdown changes the distribution of P-TEFb among nuclear soluble and chromatin and downregulates the elongation activity of RNA polymerase II. Inhibition of JNK kinase but not other MAP kinases impedes the interactions between BRD4 and P-TEFb. RNA-seq and ChIP assays indicate that BRD4 both positively and negatively regulates gene transcription in cells treated with UV stress. These results reveal previously unrecognized dynamics of BRD4 and P-TEFb after UV stress and regulation of gene transcription by BRD4 acting as either activator or repressor in a context-dependent manner.

scholarly journals A Cytosolic STIM2 Preprotein Created by Signal Peptide Inefficiency Activates ORAI1 in a Store-independent Manner

2011 ◽  
Vol 286 (18) ◽  
pp. 16174-16185 ◽  
Author(s):  
Sarah J. L. Graham ◽  
Marie A. Dziadek ◽  
Lorna S. Johnstone
Keyword(s):  
Plasma Membrane ◽  
Gene Transcription ◽  
Signal Peptide ◽  
Independent Manner ◽  
Methionine Residue ◽  
Store Depletion ◽  
Amino Acid Signal Peptide ◽  
Er Targeting ◽  
Amino Acid Signal ◽  
Er Membrane

Calcium (Ca2+) influx through the plasma membrane store-operated Ca2+ channel ORAI1 is controlled by Ca2+ sensors of the stromal interaction molecule (STIM) family. STIM1 responds to endoplasmic reticulum (ER) Ca2+ store depletion by redistributing and activating ORAI1 from regions of the ER juxtaposed to the plasma membrane. Unlike STIM1, STIM2 can regulate ORAI1 in a store-dependent and store-independent manner, but the mechanism by which this is achieved is unknown. Here we find that STIM2 is translated from a highly conserved methionine residue and is directed to the ER by an incredibly long 101-amino acid signal peptide. We find that although the majority of the total STIM2 population resides on the ER membrane, a second population escapes ER targeting to accumulate as a full-length preprotein in the cytosol, signal peptide intact. Unlike STIM2, preSTIM2 localizes to the inner leaflet of the plasma membrane where it interacts with ORAI1 to regulate basal Ca2+ concentration and Ca2+-dependent gene transcription in a store-independent manner. Furthermore, a third protein comprising a fragment of the STIM2 signal peptide is released from the ER membrane into the cytosol where it regulates gene transcription in a Ca2+-independent manner. This study establishes a new model for STIM2-mediated regulation of ORAI1 in which two distinct proteins, STIM2 and preSTIM2, control store-dependent and store-independent modes of ORAI1 activation.

Unpolymerized nuclear actin is involved in the activation of CSF-1 gene transcription

2004 ◽  
Vol 28 (7) ◽  
pp. 511-516 ◽  
Author(s):  
Z SONG
Keyword(s):  
Gene Transcription ◽  
Nuclear Actin

scholarly journals Nuclear Actin-Binding Proteins as Modulators of Gene Transcription

Traffic ◽  
2005 ◽  
Vol 6 (10) ◽  
pp. 847-857 ◽  
Author(s):  
Jan Gettemans ◽  
Katrien Van Impe ◽  
Veerle Delanote ◽  
Thomas Hubert ◽  
Joël Vandekerckhove ◽  
...  
Keyword(s):  
Gene Transcription ◽  
Binding Proteins ◽  
Actin Binding ◽  
Nuclear Actin ◽  
Actin Binding Proteins

scholarly journals Nuclear Actin Extends, with No Contraction in Sight

2005 ◽  
Vol 16 (11) ◽  
pp. 5055-5060 ◽  
Author(s):  
Thoru Pederson ◽  
Ueli Aebi
Keyword(s):  
Gene Transcription ◽  
Nuclear Periphery ◽  
Structural Basis ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Nuclear Actin ◽  
The Past ◽  
Eukaryotic Gene ◽  
The One ◽  
Pore Complexes

Within the past two years, actin has been implicated in eukaryotic gene transcription by all three classes of RNA polymerase. Moreover, within just the past year, actin has been identified as a constituent of filaments attached to the nuclear pore complexes and extending into the nucleus. This review summarizes these and other very recent advances in the nuclear actin field and emphasizes the key present issues. On the one hand, we are confronted with a body of evidence for a role of actin in gene transcription but with no known structural basis; on the other hand, there is now evidence for polymeric actin—not likely in the classical F-actin conformation—in the nuclear periphery with no known function. In addition, numerous proteins that interact with either G- or F-actin are increasingly being detected in the nucleus, suggesting that both monomeric and oligomeric or polymeric forms of actin are at play and raising the possibility that the equilibrium between them, perhaps differentially regulated at various intranuclear sites, may be a major determinant of nuclear function.

scholarly journals A Nuclear Actin Function Regulates Neuronal Motility by Serum Response Factor-Dependent Gene Transcription

2009 ◽  
Vol 29 (14) ◽  
pp. 4512-4518 ◽  
Author(s):  
S. Stern ◽  
E. Debre ◽  
C. Stritt ◽  
J. Berger ◽  
G. Posern ◽  
...  
Keyword(s):  
Gene Transcription ◽  
Serum Response Factor ◽  
Response Factor ◽  
Nuclear Actin ◽  
Serum Response

scholarly journals Transcriptional Activity of Androgen Receptor Is Modulated by Two RNA Splicing Factors, PSF and p54nrb

2007 ◽  
Vol 27 (13) ◽  
pp. 4863-4875 ◽  
Author(s):  
Xuesen Dong ◽  
Joan Sweet ◽  
John R. G. Challis ◽  
Theodore Brown ◽  
Stephen J. Lye
Keyword(s):  
Androgen Receptor ◽  
Nuclear Receptors ◽  
Gene Transcription ◽  
Rna Splicing ◽  
Transcription Initiation ◽  
Transcriptional Activity ◽  
Protein Complexes ◽  
Gene Activation ◽  
Splicing Factors ◽  
Independent Manner

ABSTRACT Nuclear receptors regulate gene activation or repression through dynamic interactions with coregulators. The interactions between nuclear receptors and RNA splicing factors link gene transcription initiation with pre-mRNA splicing, providing a coordinated control of the products of gene transcription. Here we report that two RNA splicing factors, PTB-associated splicing factor (PSF) and p54nrb, synergistically form protein complexes with the androgen receptor (AR) in a ligand-independent manner and inhibit its transcriptional activity. PSF does not affect AR protein stability, as in the case of the progesterone receptor, but impedes the interaction of AR with the androgen response element. Both splicing factors interact directly with mSin3A and attract mSin3A to the AR complex in a synergistic manner. The suppression of AR transcriptional activity by PSF and p54nrb is reversed by the inhibition of histone deacetylase activity. These data demonstrated that PSF and p54nrb complex with AR and play a key role in modulating AR-mediated gene transcription.

scholarly journals A DNA Damage Response-Independent Mechanism for Telomere Shortening-Elicited Age-Related Pathologies

2020 ◽  
Vol 4 (Supplement_1) ◽  
pp. 885-885
Author(s):  
Amanda Stock ◽  
Kun Wang ◽  
Chongkui Sun ◽  
Chengyu Liu ◽  
Yi Gong ◽  
...  
Keyword(s):  
Dna Damage ◽  
Gene Transcription ◽  
Dna Damage Response ◽  
Cell Fractionation ◽  
Telomeric Dna ◽  
Independent Manner ◽  
Telomere Shortening ◽  
Telomere Attrition ◽  
Age Related ◽  
Damage Response

Abstract Telomere attrition is associated with telomeropathies and age-related pathologies. In telomeropathies, telomere uncapping induces a DNA damage response (DDR) that drives apoptosis or senescence. However, a defined mechanism by which telomere attrition contributes to other age-related pathologies has not been determined. Telomere integrity is maintained by shelterin, a six-protein complex. Rap1 is the only shelterin member that is not essential for telomere capping but engages non-telomeric DNA and regulates gene transcription. We hypothesized that non-telomeric Rap1 accumulation could contribute to age-related pathologies in a DDR-independent manner. To test this, we used CRISPR/Cas9 editing to generate a Rap1 mutant mouse model in which Rap1 at telomeres is prevented, leaving only non-telomeric Rap1. Indirect immunostaining showed no differences in telomere dysfunction-induced DDR foci in Rap1 mutant compared to wild-type primary fibroblasts. Cell fractionation/western blotting of fibroblasts from Rap1 mutants demonstrated decreased Rap1 expression and Rap1 re-localization off telomeres, which mimics the same alteration of Rap1 in human cells with telomere attrition. Rap1 mutant mice exhibited increased body weight and altered metabolic and immune-response transcripts in various tissues, indicating that altered transcription could account for some of the observed phenotypes related to telomere attrition. In conclusion, telomere shortening may facilitate non-telomeric Rap1, which alters gene transcription and drives metabolic and immune dysfunction in a DDR-independent manner.

Activator protein-1 is necessary for angiotensin-II stimulation of human adrenocorticotropin receptor gene transcription

2001 ◽  
Vol 268 (6) ◽  
pp. 1802-1810
Author(s):  
Danielle Naville ◽  
Estelle Bordet ◽  
Marie-Claude Berthelon ◽  
Philippe Durand ◽  
Martine Begeot
Keyword(s):  
Angiotensin Ii ◽  
Gene Transcription ◽  
Receptor Gene ◽  
Activator Protein 1 ◽  
Activator Protein ◽  
Stimulation Of
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