PPP1R15B Antibody
- Known as:
- PPP1R15B Antibody
- Catalog number:
- GWB-MW030C
- Product Quantity:
- 50ug
- Category:
- -
- Supplier:
- GenWay
- Gene target:
- PPP1R15B Antibody
Related genes to: PPP1R15B Antibody
- Gene:
- PPP1R15B NIH gene
- Name:
- protein phosphatase 1 regulatory subunit 15B
- Previous symbol:
- -
- Synonyms:
- FLJ14744
- Chromosome:
- 1q32.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-29
- Date modifiied:
- 2015-11-18
Related products to: PPP1R15B Antibody
Related articles to: PPP1R15B Antibody
- Chondrodysplasia is a genetic disorder characterized by impaired cartilage development and bone growth. Dysregulation of the endoplasmic reticulum (ER) stress is associated with chondrodysplasia. Here, we demonstrate a critical role for the ER stress regulator PPP1R15B in chondrocyte development. PPP1R15B is a protein phosphatase that constitutively represses eIF2α phosphorylation to attenuate global protein translation in response to stress. Remarkably, deletion of in skeletal progenitors () impairs chondrogenesis, resulting in a disorganized growth plate, reduced trabecular bone, and shortened long bones in mice. Similarly, inducible deletion of in chondroprogenitors () leads to abnormal cartilage development and bone growth. Remarkably, no skeletal phenotype is observed in mice lacking in committed osteoprogenitors () and mature osteoblasts and osteocytes (), indicating that its role is limited to regulation of chondrogenesis, not osteogenic differentiation. Mechanistically, PPP1R15B deletion increases eIF2α phosphorylation, which in turn enhances lipogenic gene expression by suppressing leptin expression. This effect was reversed in mice by reconstitution with wild-type PPP1R15B, but not with a mutant form incapable of eIF2α dephosphorylation. Exogenous expression of leptin also reversed skeletal abnormalities in these mice. Collectively, these findings reveal a critical role for PPP1R15B in cartilage development through its regulation of lipid metabolism. - Source: PubMed
Publication date: 2026/06/01
John Aijaz AhmadYang Yeon-SukXie JunChaugule SachinXu XuLee Ann-HweeLee Kyoung-MiPark Kwang HwanGao GuangpingShim Jae-Hyuck - The integrated stress response (ISR) is essential for cellular homeostasis and cognitive function. We investigated how persistent ISR activation affects cognitive performance by studying the PPP1R15B genetic variant associated with intellectual disability. To model this condition, we generated a mouse line with the pathogenic allele inserted. This variant destabilized the PPP1R15B•PP1 phosphatase complex, causing persistent ISR activation, impaired protein synthesis, and long-term memory deficits. We demonstrated that the cognitive and synaptic impairments in mice arise directly from ISR activation. Furthermore, we characterized DP71L, a viral ortholog of PPP1R15B, which acted as a potent pan-ISR inhibitor. DP71L reversed the cognitive and synaptic deficits across mouse models of Down syndrome, Alzheimer's disease, and aging, and enhanced synaptic plasticity and memory in healthy mice. - Source: PubMed
Publication date: 2026/04/02
Reineke Lucas CZhu Ping JunDalwadi UditDooling Sean WLiu YuweiWang I-ChingYoung-Baird SaraOkoh JamesKuncha Santosh KumarZhou HongyiKannan AksharaPark HyekyungDebeaubien Nicolas ACroll TristanLee D JohnArthur ChristopherDever Thomas EWalter PeterChen JinFrost AdamCosta-Mattioli Mauro - Lenvatinib is a first-line therapy for advanced hepatocellular carcinoma (HCC), yet the emergence of lenvatinib-tolerant persister cells (LTPCs) contributes to therapeutic failure and tumor relapse. The molecular programs that sustain this tolerant state remain insufficiently defined. Here, we investigated the role of the PPP1R15B-ATF4 stress-response axis in mediating lenvatinib tolerance and ferroptosis resistance. - Source: PubMed
Publication date: 2026/01/08
Chen Ming-YaoLai Shiue-WeiCheng Yi-ChiaoYadav Vijesh KumarFong Iat-HangKuo Kuang-TaiLee Kuen-HaurCherng Yih-Giun - Secretory proteins are synthesized in the endoplasmic reticulum (ER) and begin their transport from specialized domains on the ER called ER exit sites (ERES), where COPII proteins assemble. We previously demonstrated that the interaction between TANGO1 and Sec16A is critical for ERES formation. In this study, we reveal that the phosphorylation of TANGO1 and Sec16A is regulated by a FAM83A/CK1α-mediated negative feedback loop. Conversely, their dephosphorylation is regulated in a spatially distinct manner by different phosphatase complexes: PPP6R3/PPP6C for Sec16A and PPP1R15B/PPP1C for TANGO1. Excessive phosphorylation of either TANGO1 or Sec16A leads to ERES disassembly, while excessive dephosphorylation impairs secretion. Our findings demonstrate that maintaining a balanced phosphorylation state of TANGO1 and Sec16A through autoregulation by FAM83A/CK1α and the phosphatases PP1 and PP6 is essential for sustaining proper secretory activity at the ERES. - Source: PubMed
Publication date: 2025/11/25
Maeda MiharuArakawa MasashiWakabayashi MasakiKomatsu YukieSaito Kota - Stress responses enable cells to detect, adapt to, and survive challenges. The benefit of these signaling pathways depends on their reversibility. The integrated stress response (ISR) is elicited by phosphorylation of eukaryotic translation initiation factor eIF2, which traps and inhibits rate-limiting translation factor eIF2B, thereby attenuating translation initiation. Termination of this pathway thus requires relieving eIF2B from P-eIF2 inhibition. Here, we found that eIF2 phosphatase subunits PPP1R15A and PPP1R15B (R15B) bound P-eIF2 in complex with eIF2B. Biochemical investigations guided by cryo-electron microscopy structures of native eIF2-eIF2B and P-eIF2-eIF2B complexes bound to R15B demonstrated that R15B enabled dephosphorylation of otherwise dephosphorylation-incompetent P-eIF2 on eIF2B. This sheds light on ISR termination, revealing that R15B rescues eIF2B from P-eIF2 inhibition, thereby safeguarding translation and cell fitness. - Source: PubMed
Publication date: 2026/02/19
De Miguel ClaudiaThorkelsson Sigurdur RFatalska AgnieszkaHodgson GeorgeDalglish MaximillianWang ChaoBertolotti Anne