Characterization of cAMP-dependent proteolysis of GATA-6

Ishida, Akiko; Iijima, Ryoko; Kobayashi, Ayako; Maeda, Masatomo

doi:10.1016/j.bbrc.2005.05.042

Cited by 15 publications

(20 citation statements)

References 39 publications

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“…To see whether the above observation satisfies the properties of cAMP-dependent proteolysis (Ishida et al, 2005;Nakagawa et al, 1997), a proteasome inhibitor (MG115) or A-kinase inhibitor (H-89 or K-252a) together with dbcAMP was added and the amount of 140 kDa protein compared (Fig. 5).…”

Section: Response Of the Fusion Protein To Various Inhibitorsmentioning

confidence: 93%

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Cyclic AMP‐dependent proteolysis of GATA‐6 expressed on the intracellular membrane

Tsuge

Uetani

Sato

et al. 2008

Cell Biology International

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Cyclic AMP-dependent proteolysis of GATA-6 was characterized by fusing GATA-6 with the carboxyl-terminal membrane domain of SREBP-2. When the fusion protein was stably expressed in CHO-K1 cells, it was recovered in the ER membrane. This protein was processed in a similar manner to SREBP-2 upon cholesterol starvation, and the GATA-6 moiety moved into the nucleus. The GATA-6 moiety on the membrane became undetectable in the presence of dbcAMP or cholera toxin. However, H-89, K-252a, MG115 and lactacystin inhibited this decrease, suggesting that the cytoplasmic GATA-6 moiety of the fusion protein was degraded by proteasomes though A-kinase upon elevation of the cellular cAMP concentration.

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Section: Response Of the Fusion Protein To Various Inhibitorsmentioning

confidence: 93%

“…We have found that GATA-6 stably expressed in CHO-K1 cells is degraded by proteasomes in response to cAMP (Ishida et al, 2005;Nakagawa et al, 1997). Proteasomes are distributed in both the cytoplasm and nucleus (Wojcik and DeMartino, 2003).…”

Section: Introductionmentioning

confidence: 98%

Cyclic AMP‐dependent proteolysis of GATA‐6 expressed on the intracellular membrane

Tsuge

Uetani

Sato

et al. 2008

Cell Biology International

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“…Two (H-89 and 4-cyano-3-methylisoquinoline) are inhibitors of A-kinase, indicating that our previous observation [4] is reproducible since H-89 is again positive in the present study. Furthermore, KN93, PD98059, SB239063, and PP1 also showed negative effects [5].…”

Section: Discussionmentioning

confidence: 96%

“…However, component molecules communicating between A-kinase and proteasomes have not been identified. To address the cross-talk between Akinase and other protein kinases [4,5], we examined the effects of kinase inhibitors (SCADS inhibitor kit III) [11] on cAMP-dependent proteolysis of GATA-6 using tc1-17a cells that is a CHO-K1 clone stably expressing GATA-6. Among 95 kinase inhibitors [11], H-89 [15] (A-kinase inhibitor) exhibited an inhibitory effect as we previously reported, and another A-kinase inhibitor 4-cyano-3-methylisoquinoline [16] also inhibited the proteolysis.…”

Section: Effects Of Kinase Inhibitors On Camp-dependent Proteolysis Omentioning

confidence: 99%

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Inhibitors of protein kinases affecting cAMP-dependent proteolysis of GATA-6

Ushijima¹,

Maeda²

2012

ABC

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We screened 95 kinase inhibitors whether they affect cAMP-dependent proteolysis of GATA-6 or not. Among them 7 inhibitors inhibited the proteolysis at the concentration range of μM around their IC50. They are inhibitors for protein kinase A (H-89 and 4-cyano-3-methylisoquinoline), c-Jun N-terminal kinase (SP600125), phosphatidylinositol 3-kinase (Wortmannin and LY-294002), casein kinase II (TBB) and cyclin dependent kinase (Cdk1/2 inhibitor III). It is of interest how these kinases play roles in the degradation process of GATA-6 since this transcription factor is essential for development and tissue-specific gene expression of mammals. Inhibitors identified in this study would be helpful to study molecular mechanisms of phenomena in which GATA-6 participates.

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The expression of the nuclear receptors NR5A1 and NR5A2 and transcription factor GATA6 correlates with steroidogenic gene expression in the bovine corpus luteum

Taniguchi¹,

Komiyama²,

Viger³

et al. 2009

Molecular Reproduction Devel

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The corpus luteum (CL) is the major site of progesterone (P4) production during the luteal phase of the estrous cycle in cattle. To better understand the molecular mechanisms underlying P4 production, we compared the mRNA and protein expression profiles of key components of the steroidogenic pathway (StAR, CYP11A, and 3beta-HSD) during the bovine CL luteal phase with that of several transcription factors (NR5A1, NR5A2, GATA4, GATA6) known for their roles in the control of steroidogenic gene expression. In the bovine CL, StAR, CYP11A, and 3beta-HSD mRNA and protein levels remained constant at the mid and late luteal phases but markedly declined at the regressed luteal stage. NR5A1 and NR5A2 exhibited a similar pattern with a significant decrease in expression at the regressed luteal stage. Both GATA4 and GATA6 mRNA and proteins could be detected in bovine CL; GATA6 levels, however, were generally higher. Although GATA4 expression did not change during the luteal phase, GATA6 showed a marked decrease at the regressed luteal stage, like NR5A1, NR5A2, and the other steroidogenic markers. Thus, we suggest that NR5A1, NR5A2, and GATA6, but not GATA4, contribute to the transcriptional regulation of steroidogenic gene expression, and hence P4 production, in the bovine CL. Furthermore, we have demonstrated the association of NR5A1 and NR5A2 with the bovine StAR promoter in the mid-luteal CL using chromatin immunoprecipitation, suggesting that these factors have definitive roles in the regulation of StAR gene transcription in vivo.

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Characterization of cAMP-dependent proteolysis of GATA-6

Cited by 15 publications

References 39 publications

Cyclic AMP‐dependent proteolysis of GATA‐6 expressed on the intracellular membrane

Cyclic AMP‐dependent proteolysis of GATA‐6 expressed on the intracellular membrane

Inhibitors of protein kinases affecting cAMP-dependent proteolysis of GATA-6

The expression of the nuclear receptors NR5A1 and NR5A2 and transcription factor GATA6 correlates with steroidogenic gene expression in the bovine corpus luteum

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