Cyclic AMP Stimulates SF-1-Dependent CYP11A1 Expression through Homeodomain-Interacting Protein Kinase 3-Mediated Jun N-Terminal Kinase and c-Jun Phosphorylation

Lan, Hsin Chieh; Li, Hua Jung; Lin, Guang; Lai, Pao Yen; Chung, Bon Chu

doi:10.1128/mcb.02253-06

Cited by 67 publications

(35 citation statements)

References 57 publications

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“…Although dependent on cAMP, c-Jun phosphorylation was not mediated through the PKA/PI3K 3 ERK pathway. A potential candidate is the homeodomain-interacting protein kinase 3 (HIPK3) shown to be involved in cAMP-induced stimulation of JNK in the adrenal gland (49).…”

Section: Discussionmentioning

confidence: 99%

Prostaglandin E2 Induces Matrix Metalloproteinase 9 Expression in Dendritic Cells through Two Independent Signaling Pathways Leading to Activator Protein 1 (AP-1) Activation

Yen

Kocieda

Jing

et al. 2011

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Prostaglandin E2 Induces Matrix Metalloproteinase 9 Expression in Dendritic Cells through Two Independent Signaling Pathways Leading to Activator Protein 1 (AP-1) Activation

Yen

Kocieda

Jing

et al. 2011

Journal of Biological Chemistry

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“…Several studies have revealed important roles of HIPK3 in the regulation of transcription and phosphorylation in cultured cells [32][33][34][35][36]. HIPK3 overproduction has been reported to enhance androgen receptor-dependent transcription in various cell lines [32].…”

Section: Introductionmentioning

confidence: 99%

Depletion of homeodomain-interacting protein kinase 3 impairs insulin secretion and glucose tolerance in mice

et al. 2012

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Aims/hypothesis Insufficient insulin secretion and reduced pancreatic beta cell mass are hallmarks of type 2 diabetes. Here, we focused on a family of serine-threonine kinases known as homeodomain-interacting protein kinases (HIPKs). HIPKs are implicated in the modulation of Wnt signalling, which plays a crucial role in transcriptional activity, and in pancreas development and maintenance. The aim of the present study was to characterise the role of HIPKs in glucose metabolism. Methods We used RNA interference to characterise the role of HIPKs in regulating insulin secretion and transcription activity. We conducted RT-PCR and western blot analyses to analyse the expression and abundance of HIPK genes and proteins in the islets of high-fat diet-fed mice. Glucoseinduced insulin secretion and beta cell proliferation were measured in islets from Hipk3 −/− mice, which have impaired glucose tolerance owing to an insulin secretion deficiency. The abundance of pancreatic duodenal homeobox (PDX)-1 and glycogen synthase kinase (GSK)-3β phosphorylation in Hipk3 −/− islets was determined by immunohistology and western blot analyses.Results We found that HIPKs regulate insulin secretion and transcription activity. Hipk3 expression was most significantly increased in the islets of high-fat diet-fed mice. Furthermore, glucose-induced insulin secretion and beta cell proliferation were decreased in the islets of Hipk3 −/− mice.Levels of PDX1 and GSK-3β phosphorylation were significantly decreased in Hipk3 −/− islets. Conclusions/interpretation Depletion of HIPK3 impairs insulin secretion and glucose tolerance. Decreased levels of HIPK3 may play a substantial role in the pathogenesis of type 2 diabetes.

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“…One of the factors suggested to have a role in activating JNK is the homeodomain-interacting protein kinases (Hipks) Lan et al, 2007;Li et al, 2005). Hipks are a family of serine/threonine kinases that are initially identified as the regulators of transcriptional co-repressors Kim et al, 1998;Sung et al, 2005;Zhang et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Drosophila Smt3 negatively regulates JNK signaling through sequestering Hipk in the nucleus

Huang

Chen

et al. 2011

Development

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SUMMARYPost-translational modification by the small ubiquitin-related modifier (SUMO) is important for a variety of cellular and developmental processes. However, the precise mechanism(s) that connects sumoylation to specific developmental signaling pathways remains relatively less clear. Here, we show that Smt3 knockdown in Drosophila wing discs causes phenotypes resembling JNK gain of function, including ectopic apoptosis and apoptosis-induced compensatory growth. Smt3 depletion leads to an increased expression of JNK target genes Mmp1 and puckered. We show that, although knockdown of the homeodomaininteracting protein kinase (Hipk) suppresses Smt3 depletion-induced activation of JNK, Hipk overexpression synergistically enhances this type of JNK activation. We further demonstrate that Hipk is sumolylated in vivo, and its nuclear localization is dependent on the sumoylation pathway. Our results thus establish a mechanistic connection between the sumoylation pathway and the JNK pathway through the action of Hipk. We propose that the sumoylation-controlled balance between cytoplasmic and nuclear Hipk plays a crucial role in regulating JNK signaling.

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Cyclic AMP Stimulates SF-1-Dependent CYP11A1 Expression through Homeodomain-Interacting Protein Kinase 3-Mediated Jun N-Terminal Kinase and c-Jun Phosphorylation

Cited by 67 publications

References 57 publications

Prostaglandin E2 Induces Matrix Metalloproteinase 9 Expression in Dendritic Cells through Two Independent Signaling Pathways Leading to Activator Protein 1 (AP-1) Activation

Prostaglandin E2 Induces Matrix Metalloproteinase 9 Expression in Dendritic Cells through Two Independent Signaling Pathways Leading to Activator Protein 1 (AP-1) Activation

Depletion of homeodomain-interacting protein kinase 3 impairs insulin secretion and glucose tolerance in mice

Drosophila Smt3 negatively regulates JNK signaling through sequestering Hipk in the nucleus

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