HIPK2 antibody
- Known as:
- HIPK2 (anti-)
- Catalog number:
- orb100602
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- HIPK2 antibody
Related genes to: HIPK2 antibody
- Gene:
- HIPK2 NIH gene
- Name:
- homeodomain interacting protein kinase 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 7q34
- Locus Type:
- gene with protein product
- Date approved:
- 2001-01-12
- Date modifiied:
- 2015-09-01
Related products to: HIPK2 antibody
Related articles to: HIPK2 antibody
- Spinal muscular atrophy (SMA) is caused by mutations in the Survival Motor Neuron 1 (SMN1) gene, leading to reduced SMN protein levels and widespread disruption in RNA metabolism. Despite of disease-modifying therapies, which remarkably improve patient outcomes, the long-term effects remain unknown. Dysregulated small non-coding RNAs, including microRNAs, have been reported in SMA, but their contribution to the disease remains unclear. We previously showed that flunarizine could improve the phenotype of an SMA mouse model; however its mode of action is incomplete. Here, we showed that flunarizine modulates the expression of numerous microRNAs. Using small-RNA sequencing of a flunarizine-treated SMA patient fibroblast cell line, we identified several microRNAs, which are also dysregulated in the brains and/or spinal cords of SMA mouse models at early disease stages and corrected with flunarizine. Transfection of the miR-128-3p inhibitor interferes with the flunarizine-induced neurite outgrowth in the murine neuronal NSC34 cells. Among the mRNAs modulated by flunarizine, homeodomain interacting protein kinase 2 (Hipk2) transcripts were revealed as novel miR-128-3p targets using either the mimic or its inhibitor. Our findings suggest that an early microRNA accumulation in spinal cords of SMA models can contribute to molecular dysfunctions and may represent an initiating event in pathogenesis. - Source: PubMed
Publication date: 2026/06/08
Bon EmelineDelers PerrineDumont FlorentSalman BadihSapaly DelphineLetourneur FranckArmand Anne-SophieLefebvre Suzie - Purinergic signaling is critical to myocardial inflammation and function. However, the underlying mechanisms are not well defined. Herein, we identified a protein kinase, homeodomain-interacting protein kinase 2 (HIPK2), as a novel regulator of purinergic signaling. Cardiomyocyte-specific HIPK2 knockout (CM-HIPK2-KO) hearts exhibited reduced expression of multiple key players of canonical purinergic signaling, including ectonucleases CD39 and CD73, and led to excessive inflammation and cardiac dysfunction. Multiple in vitro experiments with gain-of-function (adenovirus expressing HIPK2, Ad-HIPK2), and loss-of-function (Ad-sh-RNA-HIPK2) approaches were performed to establish that HIPK2-mediated regulation of purinergic signaling is a conserved mechanism in many cell types of diverse backgrounds. Mechanistically, we identified that the signaling circuit of HIPK2-ERK-CREB exerts its effects on purinergic signaling through transcriptional control on CD39 and CD73. Aberrant activation of purinergic signaling and inflammation was critical to cardiac pathologies because interventions with purinergic signaling inhibitor apyrase or NLRP3 inflammasome inhibitor CY09 largely rescued the detrimental cardiac phenotype of CM-HIPK2 KOs. Thus, herein, we identified HIPK2 as a novel regulator of purinergic signaling. Its deletion leads to excessive inflammation and cardiac dysfunction. Therefore, strategies to maintain HIPK2 are critical to sustaining cardiac health. - Source: PubMed
Publication date: 2026/05/11
Tousif SultanBhati Arvind SinghTitus Allen SamJaiswal AshishAnsari ImranHuque AmdadulUmbarkar PrachiSethi RohanToro Cora AngelicaChen YunxiHe JinDubey Praveen KZhang QinkunXie MinKrishnamurthy PrasannaLal Hind - Fusion genes have emerged as pivotal oncogenic drivers across diverse cancer types. The predominant mechanisms underlying fusion gene formation include chromosomal aberrations and intergenic mRNA trans-splicing. With advances in cancer genomics and transcriptomics, the identification, prevalence, and functional characterization of fusion genes have become major areas of investigation. In this study, we performed a comprehensive analysis of fusion events involving the family with sequence similarity 168B (FAM168B) and pleckstrin homology domain-containing B2 (PLEKHB2) in breast invasive carcinoma (BRCA). Integrated DNA and RNA sequencing analyses revealed that the chimeric PLEKHB2::FAM168B mRNA transcript is generated through an intergenic mRNA trans-splicing mechanism. This chimeric transcript leads to elevated FAM168B protein expression via long intergenic non-coding RNA 02228 (LINC02228)-mediated activation of DEAD-box helicase 3 X-linked (DDX3X). This, in turn, activates the DAZ-associated protein 2 (DAZAP2)/homeodomain-interacting protein kinase 2 (HIPK2)/tumor protein 53 (TP53) signaling cascade, resulting in enhanced cell cycle progression and increased BRCA cell proliferation. In summary, our findings suggest that chimeric PLEKHB2::FAM168B mRNA may serve as a potential biomarker in BRCA. - Source: PubMed
Publication date: 2026/05/05
Dash Sharma SidharthSensharma SreemoyeeKutzner ArneFuhrer ErwinPramanik GopalHeese KlausPramanik Subrata - Peutz-Jeghers syndrome (PJS) is a rare inherited cancer predisposing disorder associated with pathogenic variants of the Serine Threonine Kinase11 (STK11 / LKB1). Morbidity in children is driven by small intestinal obstruction from polyps. The molecular mechanisms driving polyp initiation and growth are poorly understood. We hypothesized that integrated phosphoproteomic analysis of pediatric Peutz-Jeghers polyps would reveal signaling networks driving polyp growth. - Source: PubMed
Publication date: 2026/05/04
Pushel IrinaRoy Badal CNolte Whitney MHarvey LisaBagherian AmberRekowski Michaella JClark Zachary DWashburn Michael PUmar ShahidAttard Thomas M - Both splicing and kinase signaling are biochemical processes that fundamentally determine and shape cell physiology. Although there has been some indication that there is an interaction between the two - splicing can alter the availability of exons encoding kinase targets and kinases can phosphorylate splicing factors - it has yet to be established the extent to which altering splicing factor expression impacts kinase signaling networks. In this work, we implemented a data-driven analysis using ENCODE RNA-sequencing data and prior work mapping post-translational modifications onto splice events to identify candidate splice factor perturbations that show extensive alterations to phosphorylation-encoding protein products. We then replicated the ENCODE knockdown experiments and performed global phosphoproteomics for two candidates, U2AF1 and SRSF3, complementing the transcription-level data. Both knockdowns showed extensive changes in phosphorylation and kinase activities, both basally and upon receptor tyrosine kinase stimulation. U2AF1 knockdown drove decreased JNK-associated cell death signaling but elevated chromosome regulation through CSNK2A1, PLK, and EIF2AK4 activity. SRSF3 knockdown, on the other hand, led to decreased cell cycle signaling through CDK and HIPK2 but increased cytoskeletal signaling through various PAKs. In addition, we found a striking enrichment of phosphorylated splicing regulators in both knockdowns that were linked to their splicing activity, such as HNRNPC, suggesting potential feedback and crosstalk between splice factors through signaling pathway activation. Importantly, comparison of differential phosphorylation measurements from this study to mRNA expression and splicing measurements from ENCODE revealed significant knockdown-dependent protein regulation, not captured by transcriptomic measurements alone, underscoring the value of phosphoproteomic profiling after splice factor perturbations. Combined, the transcriptomics and phosphoproteomics reveal deep interconnection between the two processes that are relevant to understanding cell signaling in health and disease. - Source: PubMed
Publication date: 2026/04/21
Crowl SamSingh SameekZhang TianNaegle Kristen M