DVL2 Antibody
- Known as:
- DVL2 Antibody
- Catalog number:
- csb-pa007286esr1hu
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- DVL2 Antibody
Related genes to: DVL2 Antibody
- Gene:
- DVL2 NIH gene
- Name:
- dishevelled segment polarity protein 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1996-03-12
- Date modifiied:
- 2015-09-11
Related products to: DVL2 Antibody
Related articles to: DVL2 Antibody
- Exercise profoundly impacts cortical bones that are refractory to current drugs. However, the mechanisms underlying these changes remain unclear. Here we show that mechanosensitive primary cilia on myeloid-lineage preosteoclasts have a critical role in mediating exercise-induced periosteal-bone formation. We crossed Cx3cr1-Cre or Ctsk-Cre mice with Ift88 and/or Kif3a mice to create models that lack primary cilia on myeloid-lineage cells at various stages of osteoclastic differentiation. On exercise, all these mice displayed decreases in periosteal-bone formation and cortical-bone size. Mechanical stimulation of primary cilia on preosteoclasts activated Dvl2, suppressing cathepsin K production and preventing periostin degradation. The resulting elevation of periostin levels promoted periosteal-bone formation. Notably, cathepsin K inhibition overcame the effects of primary cilia deficiency in exercised Cx3cr1-Cre;Ift88 mice, restoring cortical-bone size, bone formation, and periosteal periostin levels to those observed in exercised Ift88 littermates. By uncovering the primary cilia-preosteoclast-Ctsk-periostin axis, this study provides a foundation for developing targeted therapies to enhance cortical-bone strength. - Source: PubMed
Publication date: 2026/07/01
Kim Jin-ManLee Young-SunKim Min JiKim YewonKim Ho KyoungMoon Sung-AhKim HanjunCho Han JinKim SunghoonLee Seung HunKim Min-SeonKim Young-BumKoh Jung-Min - Pathological cardiac hypertrophy drives heart failure progression, but the proteostatic mechanisms restraining maladaptive remodeling remain poorly defined. Here, we identify Zyg-11-related regulator 1 (ZER1) as a previously unrecognized Gly/N-degron proteostatic regulator of pressure overload-induced remodeling. Failing human hearts and mouse transverse aortic constriction (TAC) hearts show suppression of a CRL2/Gly-N-degron signature and reduced ZER1 abundance. Global and cardiomyocyte-specific Zer1 loss exacerbates TAC-induced hypertrophy, fibrosis, and systolic dysfunction. Mechanistically, ZER1 directly binds disheveled segment polarity protein 2 (DVL2) in an N-terminus-dependent manner and promotes its K48-linked polyubiquitination and proteasomal degradation, thereby limiting DVL2 accumulation and downstream CaMKII-HDAC4-MEF2C signaling. Cardiomyocyte-targeted Dvl2 knockdown abolishes the phenotypic differences between Zer1 and Zer1-cKO mice after TAC. WWP1 knockdown cannot rescue the phenotype induced by ZER1 deletion, demonstrating that ZER1 is required for Wwp1 knockdown-mediated protection against pressure overload-induced cardiac remodeling. Importantly, cardiomyocyte-selective AAV9-mediated restoration of ZER1 after TAC onset attenuates established remodeling and preserves cardiac function. Together, these findings define a ZER1-DVL2 proteostatic checkpoint that links Gly/N-degron-dependent protein quality control to pathological cardiac remodeling and highlights ZER1 as a potential therapeutic target for heart failure. - Source: PubMed
Publication date: 2026/06/29
Jiang MingchaoLin ZhehaoChen LuNi YingZhou JunZhang WenjuanWang HuilinYing PeifengLu XiuWang KaiKong QingranXu NaxinZhao DingshengLi JianweiZhong GuohuiMeng XingchenHamad SarkawtZheng JunmengFu YuanQin RongjiangChu XuranLi ShangxuanLi YouyouWu YiliWang YiSong WeihongLi YingxianLing Shukuan - Itch, an E3 ubiquitin ligase, is involved in various cellular functions by regulating ubiquitination and proteasomal degradation of target proteins. However, its roles are unknown in kidney fibrosis. In the present study, the decreased expression of Itch in the renal tubules of patients with chronic kidney disease (CKD) and mice induced by unilateral ureteral obstruction (UUO) or folic acid (FA) is demonstrated. Itch mice exhibited more severe fibrotic lesions and inflammation after obstruction or FA treatment compared with Itch control. Itch overexpression alleviated UUO- or FA-induced kidney fibrosis and inflammation in mice. In addition, Disheveled 2 (Dvl2) deficiency reduced kidney fibrosis and inflammation in UUO mice. In vitro, Itch overexpression inhibited transforming growth factor-beta 1(TGF-β1)-induced fibrotic response in HK-2 cells. Mechanistically, Itch promoted K48-linked ubiquitination of Dvl2 at lysine 343, facilitating its proteasomal degradation, followed by suppressing GSK-3β/β-catenin signaling pathway, finally leading to the alleviation of kidney fibrosis. Collectively, our studies uncover that Itch exerts a critical role in kidney fibrosis, and it may be an attractive therapeutic target to slow the progression of fibrotic kidney disease. - Source: PubMed
Publication date: 2026/05/22
Li YueZhang WeiXie YingqingWang DongyunLiu MengyuHan WeixiaLi XinranSong ShanMu LinLi GuiyingShi Yonghong - Planar cell polarity (PCP) in epithelia is characterized by the polarized distribution of two opposing, membrane-associated PCP complexes across cell junctions. Transmembrane components of the PCP complex bridge cell junctions and organize into punctate, intercellular assemblies that exhibit a high degree of stability. Here, we define the contributions of the cytoplasmic PCP protein, Dishevelled (Dvl), in the sub-micron scale organization and stability of PCP complexes. Using endogenously-tagged fluorescent PCP reporters in the embryonic mouse epidermis, we quantify PCP protein mobility and clustering during polarization. We find that as transmembrane proteins immobilize into puncta, Dishevelled (Dvl2/3) co-accumulates with its transmembrane partner Frizzled (Fz6) in a polarized manner and stabilizes clusters of PCP complexes. We identify a previously unknown function for the oligomerizing DIX domain of Dvl3, typically associated with Wnt signaling, in Dvl3 asymmetric localization. These observations underscore a role for Dvl oligomerization in assembly and stabilization of asymmetric PCP puncta. - Source: PubMed
Publication date: 2026/05/05
Sil ParijatTrejo BrandonLittle Katherine ADevenport Danelle - Bunge has been used traditionally for cardiovascular disorders, but its specific roles in stem cell cardiac differentiation remain unclear. In this study, we examined whether Bunge (SM) promotes cardiomyocyte differentiation from mouse embryonic stem cells (mESCs) and defined its underlying mechanism. To dynamically monitor cardiac differentiation, we established a -H2B-mCherry reporter mESC line that retained normal pluripotency and differentiation capacity. Using an embryoid body-based differentiation system, we found that SM exerted a distinct temporal effect on lineage progression: treatment during the early differentiation window inhibited pluripotency maintenance, proliferation, and mesodermal development, whereas administration during the cardiac precursor stage markedly enhanced cardiomyocyte formation, as indicated by increased beating embryoid bodies and upregulation of , , , , and . Mechanistically, transcriptomic and protein analyses showed that SM suppressed canonical Wnt/β-catenin signaling, including downregulation of , , , , and , while Wnt activation WAY262611 partially reversed these effects. Further compound screening identified tanshinone IIA (Tan IIA) as the principal active constituent of SM, which largely recapitulated the pro-cardiogenic and Wnt-inhibitory effects of the crude extract. Together, these findings identify SM and Tan IIA as stage-dependent regulators of mESC fate and support their potential utility in natural product-based strategies for improving stem cell-derived cardiomyocyte generation. - Source: PubMed
Publication date: 2026/04/26
Lu GuotaoSun QiRen WeiYang JihongYang Fan