Restin _ CLIP1
- Known as:
- Restin _ CLIP1
- Catalog number:
- Y214156
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Restin _ CLIP1
Related genes to: Restin _ CLIP1
- Gene:
- CLIP1 NIH gene
- Name:
- CAP-Gly domain containing linker protein 1
- Previous symbol:
- RSN
- Synonyms:
- CYLN1, CLIP170, CLIP, CLIP-170
- Chromosome:
- 12q24.31
- Locus Type:
- gene with protein product
- Date approved:
- 1993-06-10
- Date modifiied:
- 2016-10-05
Related products to: Restin _ CLIP1
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- ALK and ROS1 fusions are key drivers of infant-type hemispheric gliomas (IHG). With diverse gene partners, the impact of ALK and ROS1 oncoprotein heterogeneity on glioma biology remains unknown. We developed an integrative phospho-proteomic and transcriptomic approach to discover biological functions regulated by five IHG-associated fusions: CCDC88A::ALK, PPP1CB::ALK, GOPC::ROS1, CLIP1::ROS1, and KIF21A::ROS1. Here, we report fusion-specific oncogenic functions conferred by the 5' gene partner, including increased cell motility driven by microtubule-interacting fusions CCDC88A::ALK and CLIP1::ROS1. All studied fusions converge on STAT3 activation. Using affinity purification mass spectrometry, we identified SHP2 in direct interaction with all three ROS1 oncoproteins but with none of the ALK oncoproteins, which in turn interact with SHC1/SHC3. ROS1 fusions phosphorylate SHP2 to a greater extent than ALK fusions, and analyses of downstream pathways suggest MAPK-independent, non-canonical SHP2-driven functions. Our findings reveal both common and fusion-specific dependencies, offering opportunities to optimize therapeutic strategies for pediatric gliomas. - Source: PubMed
Publication date: 2026/03/05
Postlmayr AndreasSanchez Bergman AstridTorrejon Diaz JacobCiraulo BernardYan ShenHofmann NinaCarbajal SamantaDobler RosalieMachaalani CharbelSchönholzer Marc TPriego Gonzalez LauraDe Micheli Andrea JBerenjeno-Correa ErnestoBaroncini LucaGrotzer Michael ATabori UriHawkins CynthiaAyrault OlivierZuckermann MarcBaumgartner MartinGuerreiro Stücklin Ana S - Cervical cancer (CC) remains a major cause of cancer-related mortality among women worldwide. Although screening and vaccination have reduced its incidence, advanced-stage cases still pose a serious clinical challenge. This study aimed to identify novel biomarkers and therapeutic targets for CC through integrated bioinformatics and experimental approaches. Analysis of multiple datasets (GSE63514, GSE67522, and TCGA-GTEx) revealed 426 consistently upregulated genes in CC, among which several kinesin family members, including kinesin family member 20 A (KIF20A), were significantly overexpressed. KIF20A mRNA and protein levels were markedly elevated in CC patient tissues ( = 306 tumors vs. 22 normal controls). Functional assays demonstrated that KIF20A knockdown strongly inhibited cell proliferation, migration, and tumor growth in vitro and in vivo. Mechanistically, KIF20A interacts with CAP Gly domain containing linker protein 1 (CLIP1) and enhances its protein stability. Rescue experiments confirmed that CLIP1 silencing reversed the oncogenic effects of KIF20A overexpression. These results unveil a previously unrecognized KIF20A-CLIP1 regulatory axis in CC progression and suggest its potential as both a biomarker and a therapeutic target. - Source: PubMed
Publication date: 2026/03/03
Ma XiaofengXu ZhongleiChen YueJiang FangJiao YuyingWang WenyanWang Enlin - Substrate type play a pivotal role in regulating the morphology, mechanical properties, and cytoskeletal organization of cancer cells. In this study, we examined the response of U2OS osteosarcoma cells to substrate stiffness, with a particular focus on cytoskeletal remodeling, cell elasticity, and microparticle internalization. To simulate environments of moderate and high stiffness, cells were cultured on polyacrylamide (PA) hydrogels with a stiffness of 40 kPa and on rigid glass substrates, respectively. Changes in cell morphology and cytoskeletal organization were assessed using fluorescence microscopy, while cell mechanical properties were measured using AFM. To investigate the relationship between substrate mechanics and endocytic activity, carboxylated fluorescent 2 µm latex microspheres were introduced to the cell culture system. U2OS cells cultured on glass exhibited a significantly larger surface area, more actin stress fibers, and a more organized, stretched cytoskeletal architecture compared to cells grown on 40 kPa PA gels. AFM measurements further demonstrated that cells on glass were mechanically stiffer than those on PA substrates. Microparticle uptake was also strongly influenced by substrate stiffness. Cells cultured on 40 kPa PA gels internalized a significantly greater number of fluorescent microspheres and notably, on 40 kPa PA gel formed "cup-like" structures around the beads, composed of microtubules. Three-dimensional image reconstructions revealed that these structures frequently encapsulate the particles in an asymmetrical manner, indicative of an active cytoskeletal remodeling. To better understand the molecular composition of microtubule-based structures, we analyzed the localization of selected microtubule-associated proteins (MAPs), including IQGAP1, CLIP1, and MARK2. Interestingly, only IQGAP1 was localized prominently to the microtubule cups on 40 kPa gels, often forming ring-like structures surrounding the beads. In some cases, these rings were observed independently of microtubules, suggesting the involvement of IQGAP1 in an active, possibly microtubule-initiated, endocytic process. In conclusion, our findings demonstrate that substrate type modulates multiple aspects of U2OS cell behavior, including morphology, cytoskeletal arrangement, mechanical properties, and microparticle uptake. These results underscore the mechanosensitive nature of osteosarcoma cells and highlight novel roles for microtubule cup-like structures and MAPs, particularly IQGAP1 in cellular uptake mechanisms. - Source: PubMed
Publication date: 2025/12/24
Rząca CarinaKubisiak AgataPanek DominikTargosz-Korecka MartaRajfur Zenon - Cellular senescence and necroptosis are two cell fates, which trigger an inflammatory response and increase with age, that have been proposed to play a role in inflammaging. In this study, we performed the first study to directly test the possible interaction between necroptosis and cellular senescence. Using a novel Mlkl-KI mouse model, we were able to specifically induce (~ 4-fold) the overexpression of MLKL, the necroptotic executioner, in hepatocytes (hMlkl-KI mice). The overexpression of MLKL led to increased necroptosis and cell damage/death in liver, as shown by increased levels of MLKL-oligomers, TUNEL staining, and Ki-67 staining in the livers, as well as increased ALT activity and HMGB1 levels in the plasma. The increase in necroptosis was paralleled by an increase in cellular senescence. We observed increased levels of p16 and p21 as well as SASP-factors. As expected, inflammation, as measured by the levels of proinflammatory factors and mononuclear cell clusters, was increased in the hMlkl-KI mice. Transcriptomic analysis revealed that MLKL overexpression altered the expression of genes involved in cellular senescence, inflammation, and drug metabolism. The increase in inflammation, necroptosis, and cellular senescence in the livers of 6-month-old hMlkl-KI mice was associated with an increase in liver fibrosis. The data from our study suggest that necroptosis has the potential of inducing inflammation through two pathways: (1) the initial inflammatory storm triggered by DAMPs released from necroptotic, dying cells and (2) SASP-factors produced by senescent cells that were induced by necroptosis. - Source: PubMed
Publication date: 2025/11/24
Selvarani RamasamyLee SunhoSaminathan ManiBoovalingam PuvarajanKurup KavithaPham KevinWolf Roman FFreeman Willard MUnnikrishnan ArchanaRichardson Arlan - Phloem-inhabiting unculturable bacterial pathogens are persistently transmitted by insect vectors. However, how they evade insect immune responses to ensure persistent transmission remains unknown. The important melanization immune response in insects is triggered by cleavage of prophenoloxidase (PPO) into active phenoloxidase (PO) via clip-domain serine proteases (CLIPs). Here, we demonstrate that infection of Liberibacter asiaticus (Las) in psyllid vectors activates the peptidoglycan recognition protein (PGRP)-CLIP1-CLIP4-PPO-PO signaling cascade to induce a mild melanization response, ensuring persistent Las infection without causing significant insect fitness costs to the insect. A Las-encoded secretory protein, SDE3230, directly interacts with PGRP and suppresses its activity in transducing this signaling cascade. CLIP4 cleaves PPO between arginine 125 and methionine 126 residues to active PO to induce melanization, and this cleavage pattern in psyllid is distinct from other insects. However, SDE3230 competitively binds to this cleavage site of PPO with CLIP4, thereby suppressing PPO effective cleavage. Collectively, these findings reveal the dual role of SDE3230 in facilitating the mild melanization response, benefitting persistent Las infection and insect fitness.IMPORTANCEPsyllid-borne huanglongbing is the most destructive citrus disease worldwide, causing billions of dollars in annual production losses and threatening the entire citrus industry. Currently, the mechanism by which the causal agent Liberibacter asiaticus (Las) antagonizes psyllid innate immune responses to facilitate its coexistence with psyllid vectors is still unknown. Here, we report that Las exploits the highly expressed secretory protein SDE3230 in psyllids to suppress the important melanization immune response in hemolymph via inhibiting the pattern recognition receptor PGRP activity and the cleavage of prophenoloxidase into active phenoloxidase by clip-domain serine proteases. The pattern of PPO cleavage is novel, and this process ultimately ensures persistent Las infection and insect fitness. Our findings provide insights into how Las has evolved novel strategies to evade the insect melanization response, thereby facilitating persistent Las transmission. - Source: PubMed
Publication date: 2025/08/29
Li YouDu YuRen DongshengBin YuChen QianWei Taiyun