Phosphodiesterases link the aryl hydrocarbon receptor complex to cyclic nucleotide signaling

Oliveira, Simone Kobe de; Smolenski, Albert

doi:10.1016/j.bcp.2008.08.027

Cited by 21 publications

(13 citation statements)

References 101 publications

(127 reference statements)

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“…Naturally occurring AIP-truncating mutations completely abolish the interaction with PDE4A5 (Bolger et al 2003, Leontiou et al 2008, Igreja et al 2010, Trivellin & Korbonits 2011. Another PDE isoform, PDE2A, expressed in human pituitary (Lennox et al 2011), has also been reported to bind to the C-terminal region of AIP and it has been shown that AIP has the opposite effect on PDE4A5 and PDE2A functions (de Oliveira et al 2007, de Oliveira & Smolenski 2009 Recently it has been shown that in GH3 cells AIP regulates cAMP signaling and GH secretion independently of the AIP-PDE interaction (Formosa et al 2013). The overexpression of the WT AIP, but not of a truncated mutant, reduces intracellular cAMP levels, the expression of cAMP target genes, and forskolin-induced GH secretion.…”

Section: Cross Talk Between Camp and Calcium Signaling Pathwaysmentioning

confidence: 99%

cAMP in the pituitary: an old messenger for multiple signals

Peverelli¹,

Mantovani²,

Lania³

et al. 2013

Journal of Molecular Endocrinology

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The cyclic nucleotide cAMP is a universal regulator of a variety of cell functions in response to activated G-protein coupled receptors. In particular, cAMP exerts positive or negative effects on cell proliferation in different cell types. As demonstrated by several in vitro studies, in somatotrophs and in other endocrine cells, cAMP is a mitogenic factor. In agreement with this notion, it has been found that the mutations of genes coding for proteins that contribute to increases in the cAMP signaling cascade may cause endocrine tumor development. This review will discuss the central role of cAMP signaling in the pituitary, focusing on the cAMP pathway alterations involved in pituitary tumorigenesis, as well as on poorly investigated the aspects of cAMP cascade, such as crosstalk with the ERK signaling pathway and new cAMP effectors.

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Section: Cross Talk Between Camp and Calcium Signaling Pathwaysmentioning

confidence: 99%

cAMP in the pituitary: an old messenger for multiple signals

Peverelli¹,

Mantovani²,

Lania³

et al. 2013

Journal of Molecular Endocrinology

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“…Although the majority of studies regarding AIP have so far focused mainly on the AhR pathway, lots of interactions with functionally different proteins have also been reported, indicating that AIP is involved in various cellular pathways. The role of AIP in all these pathways needs to be further investigated as well as the possible links between them, as it is beginning to unravel, for instance, between the AhR-cAMP-PDE and AhR-EGFR pathways (HaarmannStemmann et al 2009, Oesch-Bartlomowicz & Oesch 2009, de Oliveira & Smolenski 2009.…”

Section: Discussionmentioning

confidence: 99%

“…PDE4s can be distinguished from other PDE subfamilies by sequence identity in the catalytic region and by the presence of specific regions, located at the N-terminal portion of the proteins, called upstream conserved regions 1 and 2 (UCR1 and UCR2; Bolger et al 2003, de Oliveira & Smolenski 2009). At least 35 splice variants are encoded by four genes (PDE4A-D; Lugnier 2006).…”

Section: Pde4a5mentioning

confidence: 99%

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AIP and its interacting partners

Trivellin¹,

Korbonits²

2011

Journal of Endocrinology

124

104

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Germline mutations in the aryl hydrocarbon receptorinteracting protein gene (AIP) predispose to young-onset pituitary tumours, most often to GH-or prolactin-secreting adenomas, and most of these patients belong to familial isolated pituitary adenoma families. The molecular pathway initiated by the loss-of-function AIP mutations leading to pituitary tumour formation is unknown. AIP, a co-chaperone of heat-shock protein 90 and various nuclear receptors, belongs to the family of tetratricopeptide repeat (TPR)-containing proteins. It has three antiparallel a-helix motifs (TPR domains) that mediate the interaction of AIP with most of its partners. In this review, we summarise the known interactions of AIP described so far. The identification of AIP partners and the understanding of how AIP interacts with these proteins might help to explain the specific phenotype of the families with heterozygous AIP mutations, to gain deeper insight into the pathological process of pituitary tumour formation and to identify novel drug targets.

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“…On the other hand, AIP has been shown to interact with some phosphodiesterases (PDEs), which inactivate cyclic nucleotides, and this may modulate cAMP concentration and/or AhR nuclear translocation and transcriptional activity. Such mechanisms have been recently reviewed by de Oliveira and Smolenski ( 2009 ) . Brie fl y, a direct interaction of AIP with the isoforms PDE4A5 and PDE2 has been demonstrated, which is mediated by its TPR domains.…”

Section: Aip Ahr and The Modulation Of The Camp Pathwaymentioning

confidence: 99%