A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes.

Barratt, Michael J.; Hazzalin, Catherine A.; Zhelev, N; Mahadevan, Louis C.

doi:10.1002/j.1460-2075.1994.tb06774.x

Cited by 47 publications

(42 citation statements)

References 107 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…3A). It has been reported that EGF-stimulated histone H3 phosphorylation is restricted to a small subset of nucleosomes that are associated with active gene transcription (4,5,17,18,20). Recently, it was found that in Drosophila salivary glands, heat shock significantly stimulated histone H3 phosphorylation at a few loci where the heat shock protein genes are located, while the global level of phosphorylated histone H3 decreased dramatically (47).…”

Section: Resultsmentioning

confidence: 99%

Transcriptional Induction of MKP-1 in Response to Stress Is Associated with Histone H3 Phosphorylation-Acetylation

Gorospe

Hutter

et al. 2001

Molecular and Cellular Biology

174

185

View full text Add to dashboard Cite

Mitogen-activated protein (MAP) kinase phosphatase 1 (MKP-1) has been shown to play a critical role in mediating the feedback control of MAP kinase cascades in a variety of cellular processes, including proliferation and stress responsiveness. Although MKP-1 expression is induced by a broad array of extracellular stimuli, the mechanisms mediating its induction remain poorly understood. Here we show that MKP-1 mRNA was potently induced by arsenite and ultraviolet light and modestly increased by heat shock and hydrogen peroxide. Interestingly, arsenite also dramatically induces phosphorylation-acetylation of histone H3 at a global level which precedes the induction of MKP-1 mRNA. The transcriptional induction of MKP-1, histone H3 modification, and elevation in MKP-1 mRNA in response to arsenite are all partially prevented by the p38 MAP kinase inhibitor SB203580, suggesting that the p38 pathway is involved in these processes. Finally, analysis of the DNA brought down by chromatin immunoprecipitation (ChIP) reveals that arsenite induces phosphorylation-acetylation of histone H3 associated with the MKP-1 gene and enhances binding of RNA polymerase II to MKP-1 chromatin. ChIP assays following exposure to other stress agents reveal various degrees of histone H3 modification at the MKP-1 chromatin. The differential contribution of p38 and ERK MAP kinases in mediating MKP-1 induction by different stress agents further illustrates the complexity and versatility of stress-induced MKP-1 expression. Our results strongly suggest that chromatin remodeling after stress contributes to the transcriptional induction of MKP-1.The mitogen-activated protein (MAP) kinases play a central role in orchestrating many short-and long-term changes in the cell in response to extracellular stimuli (50). To date, three major MAP kinase subfamilies have been well characterized in mammalian cells: the extracellular signal-regulated kinase (ERK), the c-Jun N-terminal kinases/stress-activated protein kinase (JNK/SAPK), and p38 (11,40,50). Thus far, numerous proteins with a wide spectrum of biological functions have been identified as the targets of MAP kinase cascades, including protein kinases, cytoskeletal components, phospholipase A2, stalhmin, and the Na ϩ /H ϩ antipump NHE1 (6,23,42). In addition to the proteins that function on the membrane or in the cytoplasm, MAP kinases also play a crucial role in regulating gene transcription. Upon activation, MAP kinases translocate from the cytoplasm to the nucleus, where they phosphorylate and activate a multitude of transcription factors, including c-Myc, c-Jun, c-Fos, Elk-1, and ATF-2, ultimately resulting in enhanced gene transcription (8,24,58). The fact that a broad variety of extracellular signals conscript MAP kinase cascades to convey their specific messages suggests that MAP kinase cascades serve a myriad of purposes and the cascades need to be tightly controlled.The activities of all MAP kinases are regulated through reversible phosphorylation of two different amino acid residues (threonine ...

show abstract

Section: Resultsmentioning

confidence: 99%

Transcriptional Induction of MKP-1 in Response to Stress Is Associated with Histone H3 Phosphorylation-Acetylation

Gorospe

Hutter

et al. 2001

Molecular and Cellular Biology

174

185

View full text Add to dashboard Cite

show abstract

“…Such a mode of access for HMG-14, in particular, is consistent with a potential role in the rapid regulation of gene expression in response to a variety of extracellular signals. As opposed to HMG-17, HMG-14 is specifically and rapidly phosphorylated in response to both mitogenic stimuli and thyroid-stimulating hormone (6,56) and is rapidly acetylated in response to estrogen (10,47).…”

Section: Discussionmentioning

confidence: 99%

Alleviation of Histone H1-Mediated Transcriptional Repression and Chromatin Compaction by the Acidic Activation Region in Chromosomal Protein HMG-14

Ding

Bustin

Hansen

1997

Molecular and Cellular Biology

114

View full text Add to dashboard Cite

Histone H1 promotes the generation of a condensed, transcriptionally inactive, higher-order chromatin structure. Consequently, histone H1 activity must be antagonized in order to convert chromatin to a transcriptionally competent, more extended structure. Using simian virus 40 minichromosomes as a model system, we now demonstrate that the nonhistone chromosomal protein HMG-14, which is known to preferentially associate with active chromatin, completely alleviates histone H1-mediated inhibition of transcription by RNA polymerase II. HMG-14 also partially disrupts histone H1-dependent compaction of chromatin. Both the transcriptional enhancement and chromatin-unfolding activities of HMG-14 are mediated through its acidic, C-terminal region. Strikingly, transcriptional and structural activities of HMG-14 are maintained upon replacement of the C-terminal fragment by acidic regions from either GAL4 or HMG-2. These data support the model that the acidic C terminus of HMG-14 is involved in unfolding higher-order chromatin structure to facilitate transcriptional activation of mammalian genes.In mammalian cells, genomic DNA is highly condensed, being organized in the nucleoprotein complex constituting chromatin (65,70). The packaging of genomic DNA into chromatin can inhibit gene expression in multiple ways: restricting the access of transcription factors to their promoter elements, blocking assembly and initiation by the general transcriptional machinery, and inhibiting elongation by the RNA polymerase. As a corollary, activation of transcription requires remodeling of the chromatin structure of the gene in order to relieve the repressive effects of chromatin on transcription (34,38,45,71,72).The building block of chromatin is the nucleosome, consisting of DNA wrapped twice around a histone octamer comprising the core histones H2A, H2B, H3, and H4. A linker histone, generally histone H1, interacts with DNA at several sites simultaneously (3, 51, 55, 58): (i) with DNA at or close to the entry and exit points of the nucleosome, (ii) with nucleosomal DNA over the dyad axis, after one wrap around the octamer, and (iii) with linker DNA between adjacent nucleosomal core particles. Within the interphase nucleus of higher eukaryotic cells, the linear array of nucleosomes is folded into a higherorder structure, called the 30-nm chromatin fiber (65, 70). Histone H1 plays a key role in the formation of such a higherorder chromatin structure (4, 37, 52, 59, 60).Biochemical and genetic studies have identified two distinct systems capable of remodeling the nucleosome structure for transcriptional activation. The multisubunit SWI/SNF complex, which is conserved from yeasts to humans (49, 69), can perturb the structure of a nucleosome in an ATP-dependent manner (15,29,35). This promotes the binding in vitro of either specific or general transcription factors, such as GAL4 and TBP, to their sites on nucleosomal DNA. A distinct nucleosome-remodeling factor (NURF), originally purified from Drosophila embryo extracts (63), is also capable ...

show abstract

“…The only known signalling responses activated in common by all three classes of stimuli are the activation of p70/85 S6k and phosphorylation of S6, the di erential activation of MAP kinase subtypes and the nucleosomal response i.e. the rapid phosphorylation of histone H3 Barratt et al, 1994a) and HMG-14 (Barratt et al, 1994b) on serine residues in their NH-termini . However, p70/85 S6k activation can be ablated with rapamycin with no consequence to nucleosomal or IE gene responses (Kardalinou et al, 1994), leaving the MAP kinases as the only signalling cascade currently indissociable from nucleosomal and gene induction events.…”

Section: Introductionmentioning

confidence: 99%

Effects of the inhibition of p38/RK MAP kinase on induction of five fos and jun genes by diverse stimuli

et al. 1997

View full text Add to dashboard Cite

The ERK, JNK/SAPK and p38/RK MAP kinase subtypes are di erentially activated by physiological, pharmacological and stress stimuli; all three subtypes are implicated in immediate-early (IE) gene induction by these agents. Here, we have asked whether inhibition of a single MAP kinase subtype under these conditions would generally alter induction of several IE genes in a similar way or whether this would di erentially up-and down-regulate particular IE genes, an issue which bears on the question of whether individual MAP kinases are strictly targeted to speci®c IE genes, or whether they might catalyse phosphorylation events that a ect several IE genes in the same way. SB 203580, an inhibitor of p38/RK, has been used to analyse the role of this kinase in the induction of ®ve IE genes (c-fos, fosB, c-jun, junB and junD) under diverse conditions of stimulation. In C3H 10T cells, p38/RK and its downstream kinase MAPKAP K-2 are activated by all stimuli used with the exception of TPA. The speci®city of SB 203580 as a p38/RK inhibitor in these cells is demonstrated; it does not a ect ERKs or JNK/SAPKs but does result in a small increase in the activity of the upstream kinase MKK6, the principal p38/RK activator in these cells. We ®nd that inhibition of p38/RK under these conditions produces general e ects on all ®ve IE genes as a group in three ways. First, induction of all ®ve genes in response to okadaic acid or tumour necrosis factor-a (TNF-a) is not signi®cantly altered by SB 203580. Second, in cells stimulated with anisomycin or U.V. radiation, SB 203580 potently inhibits all of the induced IE genes. Finally, SB 203580 enhances induction of all ®ve IE genes in EGF-treated cells; these enhanced mRNA levels are not due to stabilisation of labile mRNA transcripts. The signi®cance of these results to current thinking on the relationship between distinct MAP kinase subtypes and speci®c IE genes is discussed.

show abstract

A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes.

Cited by 47 publications

References 107 publications

Transcriptional Induction of MKP-1 in Response to Stress Is Associated with Histone H3 Phosphorylation-Acetylation

Transcriptional Induction of MKP-1 in Response to Stress Is Associated with Histone H3 Phosphorylation-Acetylation

Alleviation of Histone H1-Mediated Transcriptional Repression and Chromatin Compaction by the Acidic Activation Region in Chromosomal Protein HMG-14

Effects of the inhibition of p38/RK MAP kinase on induction of five fos and jun genes by diverse stimuli

Contact Info

Product

Resources

About