Transcriptional activity and Sp 1/3 transcription factor binding to the P1 promoter sequences of the human AβH‐J‐J locus

Feriotto, Giordana; Finotti, Alessia; Breveglieri, Giulia; Treves, Susan; Zorzato, Francesco; Gambari, Roberto

doi:10.1111/j.1742-4658.2007.05976.x

Cited by 14 publications

(29 citation statements)

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“…The results obtained indicate that the P1 promoter directs transcription in all the cell lines analysed and is more active in HeLa cells (Figure 2 , column e). These data confirm and further extend the concept that P1 promoter, unlike the tissue-specific P2 promoter, directs transcription in cells of different tissues, as recently reported by our research group [ 15 , 16 ].…”

Section: Resultssupporting

confidence: 92%

“…In order to identify putative regulatory regions located within AβH-J-J P1 promoter, HeLa cells were transiently transfected with sequentially deleted reporter constructs, containing different regions of the -661/+81 P1 nucleotide sequence cloned into pGL3-basic reporter vector [ 16 ].…”

Section: Resultsmentioning

confidence: 99%

“…In additon, we have recently reported the role of Sp factors in upregulating the P1-directed transcription of the AβH-J-J locus [ 16 ]. This was the first study about the role of the P1 promoter.…”

Section: Introductionmentioning

confidence: 99%

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Upstream stimulatory factors are involved in the P1 promoter directed transcription of the AbetaH-J-J locus

et al. 2008

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Background: Alternative splicing of the locus AβH-J-J generates functionally distinct proteins: the enzyme aspartyl (asparaginyl) β-hydroxylase (AAH), truncated homologs of AAH with a role in calcium homeostasis humbug and junctate and a structural protein of the sarcoplasmic reticulum membranes junctin. AAH and humbug are over expressed in a broad range of malignant neoplasms. We have previously reported that this locus contains two promoters, P1 and P2. While AAH and humbug are expressed in most tissues under the regulation of the P1 promoter, AAH, junctin and junctate are predominantly expressed in excitable tissues under the control of the P2 promoter. We previously demonstrated that Sp transcription factors positively regulate the P1 promoter.

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 99%

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Upstream stimulatory factors are involved in the P1 promoter directed transcription of the AbetaH-J-J locus

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“…In addition, the N-terminal fragment of ASPH could remain attached to the ER membrane where it may serve a similar function as Humbug, i.e. regulating Ca 2 + flux needed for actin filament polymerization and de-polymerization [21,33,35,36]. …”

Section: Introductionmentioning

confidence: 99%

Phosphorylation Modulates Aspartyl-(Asparaginyl)-β- Hydroxylase Protein Expression, Catalytic Activity and Migration in Human Immature Neuronal Cerebellar Cells

2017

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Background Abundant aspartyl-asparaginyl-β-hydroxylase (ASPH) expression supports robust neuronal migration during development, and reduced ASPH expression and function, as occur in fetal alcohol spectrum disorder, impair cerebellar neuron migration. ASPH mediates its effects on cell migration via hydroxylation-dependent activation of Notch signaling networks. Insulin and Insulin-like growth factor (IGF-1) stimulate ASPH mRNA transcription and enhance ASPH protein expression by inhibiting Glycogen Synthase Kinase–3β (GSK-3β). This study examines the role of direct GSK-3β phosphorylation as a modulator of ASPH protein expression and function in human cerebellar-derived PNET2 cells. Methods Predicted phosphorylation sites encoded by human ASPH were ablated by S/T→A site-directed mutagenesis of an N-Myc-tagged wildtype (WT) cDNA regulated by a CMV promoter. Phenotypic and functional features were assessed in transiently transfected PNET2 cells. Results Cells transfected with WT ASPH had increased ASPH protein expression, directional motility, Notch-1 and Jagged-1 expression, and catalytic activity relative to control. Although most single- and multi-point ASPH mutants also had increased ASPH protein expression, their effects on Notch and Jagged expression, directional motility and adhesion, and catalytic activity varied such that only a few of the cDNA constructs conferred functional advantages over WT. Immunofluorescence studies showed that ASPH phosphorylation site deletions can alter the subcellular distribution of ASPH and therefore its potential interactions with Notch/Jagged at the cell surface. Conclusions Inhibition of ASPH phosphorylation enhances ASPH protein expression, but attendant alterations in intra-cellular trafficking may govern the functional consequences in relation to neuronal migration, adhesion and Notch activated signaling.

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“…Transcripts starting from exon 1 (green box in Fig. 3), which is under the control of the P1 promoter, are expressed in most tissues and share their NH 2 terminus with aspartyl‐β‐hydroxylase (Treves et al 2000; Dinchuk et al 2000; Feriotto et al 2007). Exon 1a (blue box in Fig.…”

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confidence: 99%

Minor sarcoplasmic reticulum membrane components that modulate excitation–contraction coupling in striated muscles

Treves

Vukcevic

Maj

et al. 2009

The Journal of Physiology

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In striated muscle, activation of contraction is initiated by membrane depolarisation caused by an action potential, which triggers the release of Ca 2+ stored in the sarcoplasmic reticulum by a process called excitation-contraction coupling. Excitation-contraction coupling occurs via a highly sophisticated supramolecular signalling complex at the junction between the sarcoplasmic reticulum and the transverse tubules. It is generally accepted that the core components of the excitation-contraction coupling machinery are the dihydropyridine receptors, ryanodine receptors and calsequestrin, which serve as voltage sensor, Ca 2+ release channel, and Ca 2+ storage protein, respectively. Nevertheless, a number of additional proteins have been shown to be essential both for the structural formation of the machinery involved in excitation-contraction coupling and for its fine tuning. In this review we discuss the functional role of minor sarcoplasmic reticulum protein components. The definition of their roles in excitation-contraction coupling is important in order to understand how mutations in genes involved in Ca 2+ signalling cause neuromuscular disorders.

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Transcriptional activity and Sp 1/3 transcription factor binding to the P1 promoter sequences of the human AβH‐J‐J locus

Cited by 14 publications

References 47 publications

Upstream stimulatory factors are involved in the P1 promoter directed transcription of the AbetaH-J-J locus

Upstream stimulatory factors are involved in the P1 promoter directed transcription of the AbetaH-J-J locus

Phosphorylation Modulates Aspartyl-(Asparaginyl)-β- Hydroxylase Protein Expression, Catalytic Activity and Migration in Human Immature Neuronal Cerebellar Cells

Minor sarcoplasmic reticulum membrane components that modulate excitation–contraction coupling in striated muscles

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