Ask about this productRelated genes to: GNB2L1 antibody
- Gene:
- RACK1 NIH gene
- Name:
- receptor for activated C kinase 1
- Previous symbol:
- GNB2L1
- Synonyms:
- Gnb2-rs1, H12.3
- Chromosome:
- 5q35.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-10-19
- Date modifiied:
- 2019-02-01
Related products to: GNB2L1 antibody
Related articles to: GNB2L1 antibody
- Osteoclast overactivation is a central driver of bone metabolic disorders such as osteoporosis, and novel drug targets for these diseases continue to be actively explored. Scaffold proteins, which enhance the specificity of deubiquitinase (DUB)-substrate interactions, have emerged as promising therapeutic targets for the sustained management of chronic diseases. Intraflagellar transport (IFT) proteins, recognized for their scaffolding roles in cellular signaling, are increasingly implicated in bone remodeling. However, their therapeutic potential for bone metabolic disorders remains to be fully elucidated. - Source: PubMed
Publication date: 2026/04/02
Gao YuanLai BowenYan RanHe JinnanLu TingweiYang ShiyuanChen JunGao RuiJiang HengZhou Xuhui - RACK1 (receptor for activated C kinase 1) is a highly conserved WD40 repeat family scaffold protein. As a central signaling hub, it regulates cell proliferation, migration, apoptosis, and stress responses by binding key molecules like protein kinase C, Src kinases, and integrin β-subunits. Additionally, RACK1 acts as a ribosomal protein, associating with the 40S subunit to modulate translational stalling and ubiquitination, influencing ribosome function and protein synthesis. RACK1 shows significantly down- or up-regulated in different tumors, highlighting its complex bidirectional signaling role. These effects are mediated through regulation of oncogenic pathways, apoptosis induction, metastasis inhibition, and modulation of metabolic and immune microenvironments. Therefore, the enthusiasm for RACK1-targeted therapeutic strategy is growing and placed RACK1 under the spotlight of oncology. This manuscript, to our knowledge, is the first review to summarize the role of RACK1 in pan-cancers via analysis of comprehensive gene information, and targeted inhibitors. Specifically, we introduce the structure of RACK1 and discuss the current understanding of its mechanism as a central signaling hub that coordinates diverse pathways to regulate cell proliferation, migration, apoptosis, and stress responses. This review outlines the potential therapeutic applications for targeting RACK1 and may contribute to the development of effective RACK1 inhibitors within the strategy of structure-based drug discovery of cancer therapy. - Source: PubMed
Publication date: 2026/04/11
Yang Jing-ChengDu Ya-YaZuo Wei-QiongYao Jing-YueMa KeLiang YingZhao Ming-GaoLi Zhi-Mei - Autophagy is an evolutionarily conserved catabolic process. In a process requiring a cascade of over 35 autophagy-related genes (Atg), a cupped phagophore membrane expands to surround cytoplasmic material, and seals itself to form an autophagosome, which finally fuses with lysosomes. Large numbers of autophagosomes form during stress responses, while simultaneously cells drastically reduce translation to conserve energy. Here, using proximity-labeling and Fluorescence in situ Hybridization we demonstrate that multiple mRNAs encoding proteins required for autophagy preferentially localize in proximity to forming autophagosomes. Polysome fractionation and proteomics of nascent proteins in proximity to forming autophagosomes provides evidence for the local translation of these mRNAs. Translation and the ribosome-binding protein RACK1 were required for the localization of these mRNAs to forming autophagosomes. Inhibition of translation or knockdown of RACK1 caused depletion of several proteins required for autophagy and a reduction in the number of autophagosomes. Local translation may enable a rapid, energy-efficient supply of proteins for autophagy to enable cells to massively induce autophagy while conserving energy during cell stress. - Source: PubMed
Publication date: 2026/04/10
Xue YunpingO'Connor KaelaNalbach KarstenSavard AlexandreKing Karyn ERussell Ryan CBehrends ChristianGibbings Derrick - Despite the widespread success of combination antiretroviral therapy (cART) in suppressing plasma viremia to undetectable levels, people living with HIV-1 (PLWH) continue to face a significantly elevated risk of chronic inflammation and Serious Non-AIDS Events (SNAEs). In this narrative review, we bridge the critical gap between molecular virology, immunometabolism, and clinical pathology by examining the complex interface of intrinsic immunity and viral persistence. We analyzed the evolutionary "arms race" between conserved host restriction factors, including TRIM5α, APOBEC3G, SAMHD1, BST-2, MX2, and SERINC, and the sophisticated viral evasion mechanisms that facilitate reservoir establishment. We further examined the role of bacterial translocation and gut barrier dysfunction in perpetuating systemic inflammation, emphasizing how HIV-1-mediated depletion of mucosal Th17 cells and disruption of tight junction proteins create a "leaky gut" that permits microbial product translocation despite suppressive therapy. Among viral proteins that may contribute to residual pathology during suppressive cART, we focused on the HIV-1 matrix protein p17, which has been proposed to function as a secreted "viral cytokine" from latent reservoirs, acting through CXCR1/CXCR2 receptors and the RACK1-JAK1-STAT1 pathway. Although primarily characterized in in vitro and ex vivo models, emerging data suggested that p17 may sustain systemic immune activation and metabolic reprogramming; however, its relative contribution compared with other viral proteins (Tat, Nef, gp120) in virologically suppressed patients remains to be fully delineated in human studies. Furthermore, we examined how HIV-1 hijacks cellular bioenergetics by shifting host cells from oxidative phosphorylation to aerobic glycolysis. We present an integrative model that connects restriction factor biology, p17-mediated chronic inflammation, immunometabolic dysregulation, and gut barrier dysfunction into a unified pathogenic framework, distinguishing established mechanisms from working hypotheses. Last, we assessed emerging therapeutic strategies, including CRISPR/Cas9-mediated enhancement of restriction factors, modulation of the mTOR pathway, and novel "Shock and Kill" approaches, stratified by development stage and demonstrated endpoints, offering potential pathways toward a functional cure. - Source: PubMed
Publication date: 2026/03/10
Nitsotolis ThomasAssimakopoulos Stelios FKouriannidi ElliLagadinou MariaPapalexandrou AlexiaIoannou PetrosMarangos MarkosMilionis HaralamposChristaki Eirini - Fibrinogen-like protein 2 (Fgl2) is a critical immunoregulatory factor, yet its precise roles in B-cell biology and mucosal immunity remain largely undefined. In this study, utilizing -knockout (KO) mice, we identified novel B cell subsets in the spleen (SPL), predominantly characterized by IGHA clonal dominance. Employing an intestinal () infection model and samples from patients exhibiting mucosal immune responses (the early stage of COVID-19 infection), we investigated the function of Fgl2 in mucosal immunity. We demonstrate that Fgl2 directly interacts with Receptor for activated C-kinase 1 (Rack1), thereby attenuating B cell receptor (BCR) signaling and metabolic activity by inhibiting AKT phosphorylation. Furthermore, the Fgl2 deficiency-induced expansion of marginal zone (MZ) B cells, germinal center (GC) B cells, and IgA+ plasma cells was effectively counteracted by in vivo Rack1 inhibition. Consistently, a Rack1 inhibitor also abrogated the enhanced activation of Fgl2-deficient B cells in vitro. Fgl2 deficiency also augmented early B cell activation, including B cell spreading, clustering, and signalosome recruitment, through upregulation of the DOCK8-WASP-actin axis. Our research uncovers an intrinsic role for Fgl2 in regulating BCR signaling, B cell differentiation, and mucosal immunity, elucidating a key underlying molecular mechanism. - Source: PubMed
Publication date: 2026/03/24
Chang JiangHuang DaYuan WeiTang JianingYang JingzhiChen YuyingYuan ZhizeWu YizhiWu DiYan WeimingNing Qin