GNB2L1 Blocking Peptide
- Known as:
- GNB2L1 Blocking Peptide
- Catalog number:
- 33r-4897
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- GNB2L1 Blocking Peptide
Related genes to: GNB2L1 Blocking Peptide
- 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 Blocking Peptide
Related articles to: GNB2L1 Blocking Peptide
- Autism Spectrum Disorder (ASD) has been linked to disturbance of the coordinated transcriptional mechanisms that govern neurogenesis, neuronal differentiation, and synaptic maturation in human cortical development. Nevertheless, the regulatory networks and cellular heterogeneity that underlie these processes are still poorly understood. Using an in vitro human cortical development dataset (GSE210960), single-cell RNA sequencing (scRNA-seq) and systems biology techniques were used to examine neurodevelopmental pathways associated with ASD. Different cellular populations representing neural progenitors and differentiated neuronal states were resolved by Seurat-based preprocessing and clustering, and developmental progressions from progenitor cells towards adult neuronal lineages were recreated using trajectory inference. Key biological processes linked to RNA splicing, energy consumption, and the formation of neural projections were found by differential expression and gene set enrichment analysis. Highly connected hub genes, such as RACK1 and NRXN1, which are essential for synaptic signalling and neuronal development and have been linked to an increased risk of ASD, were given priority in protein-protein interaction network analysis. Stable binding of tretinoin (all-trans-retinoic acid) to RACK1 was discovered by virtual drug screening, molecular docking, and molecular dynamics simulations. This was corroborated by favourable docking scores and persistent conformational stability across a 100 ns simulation. All things considered, these results offer a systems-level single-cell transcriptomic framework for locating potential molecular targets and neurodevelopmental pathways related to ASD. - Source: PubMed
Publication date: 2026/06/19
Akela Mohamed ATahir Ul Qamar MuhammadAlamri Mubarak A - Previous studies showed that a T. spiralis serine proteinase (TsSPc) was identified in intestinal infective larvae (IIL) surface and excretory-secretory (ES) proteins. The in vitro experiments revealed that rTsSPc bound to intestinal epithelial cells and promoted larval invasion, but the in vivo role of rTsSPc in T. spiralis infection remains unclear. The purpose of this study was to investigate the TsSPc's function and mechanism in T. spiralis infection in mice. Immunofluorescence assay (IFA), qPCR, and Western blotting showed that rTsSPc specifically bound and co-localized with RACK1 receptor in intestinal mucosal epithelium, activated the ERK1/2 pathway, decreased the expression of the tight junctions (E-cad, Occludin, and Claudin-1), increased intestinal permeability, impaired intestinal epithelial integrity and barrier function, thereby promoted T. spiralis invasion of intestinal mucosa. The H&E and PAS staining showed that rTsSPc also caused intestinal mucosal inflammation reactions; the number and size of goblet cells in the rTsSPc group were distinctly increased, and the expression levels of inflammatory cytokines (TNF-α, IL-1β, TGF-β, and IL-10) and mucins (Muc2 and Muc5ac) were significantly elevated. These findings further verified that the in vivo binding of TsSPc to RACK1 disrupted gut epithelial integrity and mediated T. spiralis invasion of intestinal mucosa, and TsSPc may be regarded as a potential vaccine target to block T. spiralis infection. - Source: PubMed
Wu Jin YiZhang Xin ZhuoZhang YaoZhang RuZhang XiLiu Ruo DanLong Shao RongWang Zhong QuanCui Jing - Lung adenocarcinoma (LUAD) remains a lethal malignancy plagued by therapy resistance and metabolic adaptability. This study identifies the scaffold protein RACK1 as a central regulator of LUAD pathogenesis and metabolic reprogramming. RACK1 is frequently upregulated in LUAD, where its expression correlates with advanced stage and poor prognosis. Mechanistically, RACK1 co-activates two pivotal metabolic pathways: it stabilizes LDHA by competing with its E3 ligase TRIM21, thereby enhancing glycolysis, and it scaffolds c-Src to phosphorylate and activate G6PD, fueling the pentose phosphate pathway. This dual metabolic switch promotes biomass production, redox balance, and drives aggressive tumor phenotypes. Crucially, combined targeting of RACK1 with c-Src or LDHA inhibition yielded synergistic anti-tumor effects in vivo, significantly surpassing monotherapies. Our findings establish RACK1 as a master metabolic regulator and propose a promising combinatorial therapeutic strategy for LUAD. - Source: PubMed
Publication date: 2026/05/29
Wan HuiminLi ChaoXia MengqianDong LinLin TingtingGuo WeiweiJiao FangleiLu JingjingGuo Zhongliang - Despite a growing interest in the ribotoxic stress response (RSR), it remains unknown how the upstream p38- and JNK-activating MAP3 kinase ZAKα senses translational impairment. Combining AlphaFold3 prediction and RNA crosslinking and immunoprecipitation (CLIP), we uncover that ZAKα dynamically monitors the mRNA exit channel of elongating ribosomes. This is accomplished by ZAKα via direct interactions with the ribosomal proteins RACK1 and RPS27 as well as 18S rRNA helix-26. In this conformation, the RNA-binding S (sensing) and C-terminal domain of ZAKα span across the mRNA exit channel. Loss of ribosome processivity and mRNA stasis stabilizes the interaction allowing for kinase activation. Prolonged binding of ZAKα to stalled and collided ribosomes is associated with sequestration of the sterile alpha-motif (SAM) domain on RACK1, which allows for transient ZAKα dimerization, activation loop trans-autophosphorylation, and RSR activation. Our findings highlight how ZAKα senses both stalled and collided ribosomes in human cells through overlapping mechanisms. - Source: PubMed
Publication date: 2026/05/29
Vind Anna ConstanceMartínez José FranciscoWu ZhenzhenBugai AndriiMordente KellyAbis GiancarloChamois SébastienRamalho SofiaPechincha CatarinaRyder LauraChen QiuyanRasmussen MadsShi XinyaoHe DandanSvejstrup Jesper QHaahr PeterGatfield DavidConte Maria RJensen Torben HeickBlasius MelanieBekker-Jensen Simon - Reactive Oxygen Species (ROS) signaling is a conserved biological process with parallel functions in all evolutionary branches of life. Here, we identify Receptor for Activated C Kinase 1 (RACK1) as a conserved redox-regulated hub that integrates ROS signals to coordinate cellular stress responses. Using cysteine reactivity profiling in intestinal epithelial cells, we demonstrate that RACK1 undergoes NOX1-dependent oxidation at multiple residues, with C286 serving as a key regulatory site. Functional studies reveal that RACK1 negatively regulates NFκB signaling through redox-dependent interactions with upstream signaling complexes. Upon stress stimulation, RACK1 dynamically redistributes into membrane-less condensates that act as redox-privileged microenvironments enriched for hydrogen peroxide. We find that oxidized RACK1 condensates are conserved through evolution with analogous stress response behavior in bacteria and yeast indicating a ubiquitous and ancient stress sensor-effector system. Functionally, redox-dependent RACK1 activity links environmental stress to translational control, with oxidation promoting inhibition of protein synthesis. Furthermore, RACK1 mediates responses to diverse pathogen-associated stimuli, including viral and bacterial infection, highlighting its role in epithelial innate immune responses. Collectively, these findings establish RACK1 as a cellular node for redox signaling, operating within condensate-based microdomains to spatially encode oxidative signals and regulate environmental stress pathways in cells. - Source: PubMed
Publication date: 2026/05/15
Ngwa ElsyChen XiSchmieder StefanieMaurais AaronSvistunov VictorPeng QianniMoore IanLencer Wayne IWeerapana EranthieRaghunathan KrishnanThiagarajah Jay R