Akap8
- Known as:
- Akap8
- Catalog number:
- 060502A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Akap8
Related genes to: Akap8
- Gene:
- AKAP8 NIH gene
- Name:
- A-kinase anchoring protein 8
- Previous symbol:
- -
- Synonyms:
- AKAP95, DKFZp586B1222
- Chromosome:
- 19p13.12
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-16
- Date modifiied:
- 2015-11-17
Related products to: Akap8
Related articles to: Akap8
- RNA binding proteins could regulate transcription through modulating RNA polymerase II involved transcriptional condensates with the aid of nascent RNA. However, whether this mechanism also contributes to tumorigenesis is still unknown. Here, we show the RBP AKAP95 is required for MLL rearranged leukemogenesis. Phase separation and RNA binding properties of AKAP95 modulate Pol II recruitment into condensates at genome-wide target sites. AKAP95 interact with MLL1 translocated fragment and their partial co-condensation leads to stronger AKAP95 binding towards MLL-AF9 target genes. Loss of AKAP95 significantly downregulates expression of MLL-AF9 targets and impairs MLL-AF9 driven leukemogenesis. AKAP95 is not essential for normal and regenerative hematopoiesis, rendering it an ideal target for leukemia therapeutics. As an endeavor for modifying condensates, we design a peptide JD-PI95 bridging AKAP95 to protein quality surveillance component HSP70. The peptide successfully impairs AKAP95 phase separation, attenuates gene transcription and inhibits MLLr leukemia cells proliferation. Our work demonstrates an important role of RBP condensates in tumorigenesis through regulation of transcription and a new method to perturb specific condensates for tumor inhibition. - Source: PubMed
Publication date: 2026/01/07
Yan XiangLuan YongkunZhu YiCai YouYe FanghuaYang LiangchunZhu KaiboHu JingLuo ShuangziLin JiazhengWang YixiuHuang YuluSun PingYang ZhenhuaShi BiJiang HaoLi Wei - Regulatory enzymes fulfill critical roles within specific subcellular compartments. Scaffolding proteins orchestrate enzyme activity and signal transduction by confining these processes to distinct spatial locations, thereby forming functional microdomains or signaling islands. The A kinase anchoring protein (AKAP) family represents a unique class of scaffolding proteins. AKAPs bind to protein kinase A (PKA) and its substrates to spatiotemporally regulate phosphorylation processes within these microdomains. Dysregulation of AKAPs in humans has been implicated in diverse pathologies. Moreover, AKAPs are emerging as platforms for precision drug therapy because of their compartmentalized signaling capabilities. AKAP95 (also termed AKAP8), a nuclear protein belonging to the AKAP family, has functions that extend beyond PKA signaling, including participation in liquid-liquid phase separation (LLPS) and transcriptional regulation. Additionally, it plays critical roles in cellular development and disease pathogenesis. Despite its importance, no comprehensive review has yet emphasized its molecular mechanisms, biological functions, and disease associations. This article delineates the regulatory roles of AKAP95 both within and beyond the PKA pathway through the conformation of nonmembrane compartments and microdomains, highlights its contributions to viral life cycles and oncogenesis, and reviews its potential as a therapeutic target in precision medicine. - Source: PubMed
Publication date: 2025/08/20
Wang XuHe JinlianMa GangyuanZhou FengChen LiqingLiu Liang - A-kinase anchoring protein 95 (AKAP95) functions as a scaffold for protein kinase A. Prior work by our group has shown that AKAP95, in coordination with Connexin 43 (Cx43), modulates the expression of cyclin D and E proteins, thus affecting the cell cycle progression in lung cancer cells. In the current study, we confirmed that AKAP95 forms a complex with Cx43. Moreover, it associates with cyclins D1 and E1 during the G1 phase, leading to the formation of protein complexes that subsequently translocate to the nucleus. These findings indicate that AKAP95 might facilitate the nuclear transport of cyclins D1 and E1. Throughout this process, AKAP95 and Cx43 collectively regulate the expression of cyclin D, phosphorylate cyclin E1 proteins, and target their specific ubiquitin ligases, ultimately impacting cell cycle progression. - Source: PubMed
Publication date: 2024/06/24
Deng ZifengDou LiangdingLuo ZhenLiu RongZhang JinwenWang JingWang DaiGuo DongBeiAn RanYao YouliangQiu GuihuaZhang Yongxing - Ovarian cancer (OC) is the highest worldwide cancer mortality cause among gynecologic tumors, but its underlying molecular mechanism remains largely unknown. Here, we report that the RNA binding protein A-kinase anchoring protein 8 (AKAP8) is highly expressed in ovarian cancer and predicts poor prognosis for ovarian cancer patients. AKAP8 promotes ovarian cancer progression through regulating cell proliferation and metastasis. Mechanically, AKAP8 is enriched at chromatin and regulates the transcription of the specific hnRNPUL1 isoform. Moreover, AKAP8 phase separation modulates the hnRNPUL1 short isoform transcription. Ectopic expression of the hnRNPUL1 short isoform could partially rescue the growth inhibition effect of AKAP8-knockdown in ovarian cancer cells. In addition, AKAP8 modulates PARP1 expression through hnRNPUL1, and AKAP8 inhibition enhances PAPR inhibitor cytotoxicity in ovarian cancer. Together, our study uncovers the crucial function of AKAP8 condensation-mediated transcription regulation, and targeting AKAP8 could be potential for improvement of ovarian cancer therapy. - Source: PubMed
Publication date: 2024/04/16
Mobet YouchaouWang HaochengWei QinglvLiu XiaoyiYang DanZhao HongyanYang YuNgono Ngane Rosalie AnneSouopgui JacobXu JingLiu TaoYi Ping - The RNA-dependent RNA polymerase (RdRp) is a crucial element in the replication and transcription of RNA viruses. Although the RdRps of lethal human coronaviruses severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), SARS-CoV, and Middle East respiratory syndrome coronavirus (MERS-CoV) have been extensively studied, the molecular mechanism of the catalytic subunit NSP12, which is involved in pathogenesis, remains unclear. In this study, the biochemical and cell biological results demonstrate the interactions between SARS-CoV-2 NSP12 and seven host proteins, including three splicing factors (SLU7, PPIL3, and AKAP8). The entry efficacy of SARS-CoV-2 considerably decreased when SLU7 or PPIL3 was knocked out, indicating that abnormal splicing of the host genome was responsible for this occurrence. Furthermore, the polymerase activity and stability of SARS-CoV-2 RdRp were affected by the three splicing factors to varying degrees. In addition, NSP12 and its homologues from SARS-CoV and MERS-CoV suppressed the alternative splicing of cellular genes, which were influenced by the three splicing factors. Overall, our research illustrates that SARS-CoV-2 NSP12 can engage with various splicing factors, thereby impacting virus entry, replication, and gene splicing. This not only improves our understanding of how viruses cause diseases but also lays the foundation for the development of antiviral therapies. - Source: PubMed
Yang LiZeng Xiao-TaoLuo Rong-HuaRen Si-XueLiang Lin-LinHuang Qiu-XiaTang YingFan HongRen Hai-YanZhang Wan-JiangZheng Yong-TangCheng Wei