ARPC2 Antibody
- Known as:
- ARPC2 Antibody
- Catalog number:
- AF1109a
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- ARPC2 Antibody
Related genes to: ARPC2 Antibody
- Gene:
- ARPC2 NIH gene
- Name:
- actin related protein 2/3 complex subunit 2
- Previous symbol:
- -
- Synonyms:
- p34-Arc, ARC34
- Chromosome:
- 2q35
- Locus Type:
- gene with protein product
- Date approved:
- 1999-08-06
- Date modifiied:
- 2016-10-05
Related products to: ARPC2 Antibody
Related articles to: ARPC2 Antibody
- WNT2B is canonically characterized as a secreted WNT-family ligand, which is transported to the extracellular space via the endoplasmic reticulum (ER)-Golgi pathway and binds to cell surface FZDs (frizzled class receptors) to trigger downstream signaling cascades. Here, we identify a previously unrecognized non-secretory intracellular function of WNT2B in impairing endosomal trafficking to inhibit macroautophagy/autophagy, as well as a non-canonical LC3B-II-dependent autophagic secretion mechanism for WNT2B. Specifically, the non-secretory intracellular pool of WNT2B via its conserved middle domain (MD) binds to the spectrin repeat domain (SRD) of WASHC5, competitively displacing WASHC1 and thereby disrupting WASH complex assembly and inhibiting WASHC1-mediated actin polymerization on early endosomes. This disruption impairs endosomal cargo trafficking, including the core autophagy protein ATG9A, leading to defective autophagy initiation and subsequent accumulation of pro-inflammatory and pro-fibrotic factors in fibroblasts. We validated this mechanism in vivo using a TNBS-induced mouse model of chronic colitis. Fibroblast-specific deletion restores autophagy, reduces pro-inflammatory cytokine secretion, and ameliorates intestinal fibrosis. Consistently, in Crohn disease (CD) patient tissues, elevated WNT2B in fibrotic regions negatively correlates with autophagy activity, and positively correlates with pro-fibrotic phenotypes, and clinical disease severity. Moreover, we identify a novel LC3B-II-dependent autophagic secretion pathway for WNT2B, which is distinct from the conventional ER-to-Golgi-dependent protein secretion. Collectively, our study delineates a novel non-canonical WNT2B-WASH complex-ATG9A regulatory axis through which WNT2B impairs endosomal trafficking and disrupts autophagy, ultimately amplifying inflammation and fibrosis. This study suggests that WNT2B may serve as a promising therapeutic target for CD and autophagy-associated fibrotic disorders.: 3-MA: 3-methyladenine; AAV: adeno-associated virus; ACTA2: actin alpha 2, smooth muscle; ARPC2: actin related protein 2/3 complex subunit 2; ATG: autophagy related; CCN3: cellular communication network factor 3; CD: Crohn disease; CK666: 2-fluoro-N-[2-(2-methyl-1H-indol-3-yl)ethyl]benzamide; COL1A1: collagen type I alpha 1 chain; Co-IP: co-immunoprecipitation; CTNNB1: catenin beta 1; DBcAMP: dibutyryl cyclic adenosine monophosphate; DPT: dermatopontin; EEA1: early endosome antigen 1; EGFR: epidermal growth factor receptor; ELISA: enzyme-linked immunosorbent assay; ER: endoplasmic reticulum; ESCRT: endosomal sorting complexes required for transport; EV: extracellular vesicle; FRAP: fluorescence recovery after photobleaching; FL: full length; FZD: frizzled class receptor; GST: glutathione S-transferase; HIF: human intestinal fibroblast; HMGB1: high mobility group box 1; IKBKB: inhibitor of nuclear factor kappa B kinase subunit beta; IL6: interleukin 6; LDELS: LC3-dependent EV loading and secretion; LPS: lipopolysaccharide; MAP1LC3B/LC3B: microtubule associated protein 1 light chain 3 beta; MD: middle domain; MEFs: mouse embryonic fibroblasts; MTOR: mechanistic target of rapamycin kinase; MVB: multivesicular body; NFKB: nuclear factor kappa B; NFKBIA: NFKB inhibitor alpha; PDCD6IP: programmed cell death 6 interacting protein; PLA: proximity ligation assay; RELA/p65: RELA proto-oncogene, NF-kB subunit; SAFB: scaffold attachment factor B; SES-CD: Simple Endoscopic Score for Crohn disease; SIM: super-resolution structured illumination microscopy; SMAD3: SMAD family member 3; SQSTM1/p62: sequestosome 1; SRD: spectrin repeat domain; TEM: transmission electron microscopy; TFRC: transferrin receptor; TGFB1: transforming growth factor beta 1; TGOLN2: trans-golgi network protein 2; TNBS: 2,4,6-trinitrobenzenesulfonic acid; TNF: tumor necrosis factor; VCA: Verprolin homology, Central and Acidic; WASHC: WASH complex subunit; WLS: Wnt ligand secretion mediator; WCL: whole cell lysates; WNT: Wnt family member; WT, wild type. - Source: PubMed
Publication date: 2026/06/03
Liu DanqiongCheng YanlingHuang ChuxiangXie KangJie JiananZhang QingqingLan LinChen PeiyuXie JingWang HongliRen LuLi HuiwenGeng LanlanGong SitangZhu YunCheng Yang - Cell migration depends on coordinating cell shape changes with force generation, yet how these processes are integrated remains unclear. Here, we combine live-cell imaging with traction force microscopy and computational analysis to quantify cell morphology, motility and force generation in migrating fibroblasts. We find that traction force magnitudes display a multimodal distribution, suggesting discrete migratory regimes. Using a Hidden Markov Model, we identify distinct force states that exhibit differences in shape and motion metrics, and show that individual cells transition between force states over time. To test the role of cytoskeletal organization in establishing the identified states, we analyzed cells lacking Arpc2, which disrupts branched actin assembly. Despite reduced forces and altered morphology, these cells also exhibit three migratory states. State transitions occur more frequently in cells lacking Arpc2 and unlike normal cells their protrusion geometry is force dependent. Together, our findings show that cell migration is organized into discrete mechanical states that couple morphology, motility and force generation. - Source: PubMed
Publication date: 2026/05/31
Davis Elizabeth MHockenberry Max AButler Mitchell TTruscott Harrison HShaul Noah JBear James EElston Timothy C - Macroautophagy/autophagy is a critical cellular process that maintains the cellular homeostasis by degrading and recycling cytotoxic material. Despite its importance, the intricate mechanisms governing this process remain partially elusive. Here, we designed and performed a genome-wide loss-of-function screen on a mouse haploid ESC mutant library and identified the actin-binding protein CORO1C (coronin 1C) as a previously unrecognized regulator of mammalian autophagy. Interactions between CORO1C and the ACTR2/ARP2 (actin related protein 2)-ACTR3/ARP3 complex are essential for branched actin network assembly, SQSTM1/p62 body formation, and maintaining autophagosome structural integrity. Unlike CORO1A and CORO1B, CORO1C possesses a unique second actin-binding site involved in regulating the branched actin network and autophagic process. Notably, newborn mice died earlier in starvation than wild-type littermates and multiple tissues showed autophagy-deficient phenotypes. Moreover, the adult -deficient mice exhibit severe spatial learning memory impairment. Collectively, our research uncovered the surprising role of CORO1C in promoting the formation of branched actin network and its central role in the assembly of structures vital to autophagy.: ACTR2/ARP2: actin related protein 2; ACTR3/ARP3: actin related protein 3; ARPC2: actin related protein 2/3 complex, subunit 2; ATG: autophagy related; ATG5: autophagy related 5; BafA1: bafilomycin A; CQ: chloroquine; FACS: fluorescence-activated cell sorting; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; haESC: haploid embryonic stem cell; HML: haploid-mutant library; IF: immunofluorescence; KO: knockout; MAP1LC3B/LC3: microtubule-associated protein 1 light chain 3B; RB1CC1/FIP200: RB1-inducible coiled-coil 1; SQSTM1/p62: sequestosome 1; STX17: syntaxin 17; TEM: transmission electron microscopy; WB: western blotting; WT: wild type. - Source: PubMed
Publication date: 2026/04/20
Zhang GuozhongYu NingqingSun YiLi XiaowenSun LihongLiu GuangHuang Yue - Idiopathic pulmonary fibrosis (IPF) is a chronic, progressive lung disease characterized by the pathological accumulation of collagen-rich extracellular matrix, resulting in irreversible lung remodeling and respiratory failure. The incomplete understanding of IPF pathogenesis has hindered the development of effective therapeutics. Here, we investigate the mechanism by which the actin-related protein 2/3 complex subunit 2 (ARPC2) contributes to the fibrotic response in lung fibroblasts. Modulating of ARPC2 expression levels altered the expression of profibrotic genes, including α-smooth muscle actin (), in TGF-β1-treated MRC-5 cells at the transcriptional level. We further show that ARPC2 regulates the TGF-β1-mediated nuclear translocation of myocardin-related transcription factor-A (MRTFA), a central driver of fibrotic gene induction. Our data indicate that ARPC2 plays a distinct role in profibrotic gene expression and MRTFA nuclear localization, distinguishing its function from other components of the actin-related protein 2/3 (ARP2/3) complex. Furthermore, ARPC2 appears to modulate the TGF-β1-dependent formation of MRTFA/G-actin complexes. Finally, transcriptomic analysis of cells depleted of ARPC2, ACTR2, or MRTFA revealed that ARPC2 and MRTFA co-regulate a specific repertoire of fibrotic genes. These observations support a profibrotic function for ARPC2 during fibroblast-to-myofibroblast transition (FMT), highlighting it as a potential therapeutic target for IPF. - Source: PubMed
Publication date: 2026/03/17
Du Eun JoKim HyunseongBae Seo-GyeongAn SihyeonRyoo Kanghyun - invasion of host respiratory epithelial cells is a critical mechanism driving acute exacerbations of chronic obstructive pulmonary disease (AECOPD). Although previous studies have extensively demonstrated that dynamic changes in the actin cytoskeleton are central to the invasion of host cells by , the detailed mechanisms underlying the specific upstream signaling pathways and key regulators driving this process remain incompletely understood. Our study identifies and validates the essential roles of key Rho GTPase regulators (CDC42, Rac1, ArpC2, ArpC4) in actin polymerization during infection, thereby elucidating a more comprehensive and specific molecular mechanism. Invasion assays and Transmission electron microscopy (TEM) showed that the Rho GTPase signaling pathway modulates bacterial load in A549 cells by regulating macropinosome volume. Further experiments used strains 73-OR and ATCC 25238 to invade wild-type A549 cells, CDC42 A549 cells, Rac1 A549 cells, ArpC2 A549 cells and ArpC4A549 cells respectively. Invasion assays and TEM were performed to quantify internalized bacteria, macropinosome volume changes, and bacterial distribution; Western blot analyses and cellular immunofluorescence were used to measure F-actin/G-actin ratios and microfilament fluorescence intensity. These results indicate that Rho GTPase signaling pathway modulates invasion by regulating actin polymerization dynamics. Specifically, CDC42 and Rac1 are essential for actin polymerization and bacterial internalization. ArpC4 contributes to actin remodeling without influencing invasion, while ArpC2 is uninvolved in both processes. These findings provide a theoretical basis for targeting innate immunity to prevent and treat -induced AECOPD. - Source: PubMed
Publication date: 2026/02/17
Ma RuiruiCheng GuixueWu YunChen JiaweiLu RongqiLiu Yali