Ask about this productRelated genes to: TMOD1 antibody
- Gene:
- TMOD1 NIH gene
- Name:
- tropomodulin 1
- Previous symbol:
- D9S57E, TMOD
- Synonyms:
- ETMOD
- Chromosome:
- 9q22.33
- Locus Type:
- gene with protein product
- Date approved:
- 1991-05-21
- Date modifiied:
- 2016-10-05
Related products to: TMOD1 antibody
Related articles to: TMOD1 antibody
- Jinfeng pills (JFP), a well-known traditional Chinese medicine (TCM) consisted of 9 herbs, benefit Qi, nourish the blood, effectively regulate the menstrual cycle, promote ovulation and improve endometrial thickness and blood flow. Previous studies have shown that JFP has certain effect on premature ovarian insufficiency (POI). In this prospective cohort study, the effect and mechanisms of JFP on the outcomes of in vitro fertilization and embryo transfer (IVF-ET) in poor ovarian response(POR) was investigated. - Source: PubMed
Publication date: 2026/07/18
Kong XumeiLuo QianwenHuang TianhongChen FuruiZhang YananXiong DongshengQiu YuLai WeiYan XiaoyanLong FangyiGong Yan - Cyclase-associated protein 2 (CAP2) is a conserved actin-binding protein that promotes actin filament (F-actin) turnover by disassembling ADF/cofilin-decorated filaments, supporting F-actin remodeling in differentiating cells and tissues. In the ocular lens, the actin cytoskeleton is crucial for maintaining tissue biomechanical properties during fiber cell maturation. To assess the role of CAP2 in the lens, we examined lens-specific CAP2 knockout (CAP2cKO) mice at cellular and tissue levels. CAP2cKO lenses were normal in size, shape and transparency but exhibited increased stiffness under compression and enhanced recovery after load removal. Although total actin and F-actin levels were unchanged, immunofluorescence revealed higher levels for tropomodulin 1 (Tmod1, F-actin pointed-end capping), tropomyosin isoform 3.5 (Tpm3.5, F-actin stabilizing) and T-plastin (also known as PLS3; F-actin bundling) in F-actin-rich membrane protrusions of mature fibers, whereas that for α-actinin-1 (F-actin cross-linking) was reduced. These findings suggest that CAP2 loss disrupts F-actin remodeling, indirectly promoting filament stabilization through Tpm3.5 binding, Tmod1 capping and T-plastin bundling. Consequently, F-actin networks become stiffer and more resilient, altering lens biomechanics. This study provides the first evidence that CAP2 maintains cell biomechanical properties in a non-muscle tissue through influencing the composition of actin cytoskeleton networks. - Source: PubMed
Publication date: 2026/05/26
Cheheltani SepidehCoffin MeganFowler Velia M - Cyclase-associated actin cytoskeleton regulatory protein 2 (CAP2) is a conserved actin-binding protein that promotes actin filament (F-actin) turnover by disassembling ADF/cofilin-decorated filaments, supporting F-actin remodeling in differentiating cells and tissues. In the ocular lens, the actin cytoskeleton is critical for maintaining tissue biomechanical properties during fiber cell maturation. To assess CAP2's role in the lens, we examined lens-specific CAP2 knockout ( ) mice at cellular and tissue levels. lenses were normal in size, shape, and transparency but exhibited increased stiffness under compression and enhanced recovery after load removal. While total actin levels and F-actin were unchanged, immunofluorescence revealed higher levels of Tropomodulin 1 (Tmod1, F-actin pointed-end capping), Tropomyosin3.5 (Tpm3.5, F-actin stabilizing), and T-plastin (F-actin bundling) in F-actin-rich membrane protrusions of mature fibers, while α-actinin-1 (F-actin cross-linking) was reduced. These findings suggest that CAP2 loss disrupts F-actin remodeling, promoting filament stabilization through Tpm3.5 binding, Tmod1 capping and T-plastin bundling. Consequently, F-actin networks become stiffer and more resilient, altering lens biomechanics. This study provides the first evidence that CAP2 regulates cell biomechanical properties in a non-muscle tissue through modulation of F-actin-associated proteins. - Source: PubMed
Publication date: 2025/10/15
Cheheltani SepidehCoffin MeganFowler Velia M - Tropomodulins (TMODs) are a group of proteins that stabilize the actin filament network by capping the slow-growing end of F-actin. Although their roles in tissue morphogenesis have been extensively studied in triploblastic organisms, their function in diploblastic remained unexplored. This study identified that in , expression is strongly upregulated in ectodermal cells at the parent-offspring junction during basal constriction formation and bud detachment. Notably, siRNA-mediated knockdown inhibits basal constriction formation, a pre-requisite morphological event for bud detachment. knockdown polyps show fragmented stress fibers and altered cell morphology adjacent to the basal constriction site. Finally, pharmacological studies showed that FGFR signaling is necessary for expression. Collectively, our results establish that Hydra is an FGFR-ERK2 signaling-regulated gene that is exclusively expressed in the epitheliomuscular ectodermal cells at the parent-offspring junction and is essential for bud separation from the parent polyp by promoting F-actin polymerization/stabilization. - Source: PubMed
Publication date: 2025/10/15
Kulkarni ShravaniMaity ShreyaTadasare NirajJoshi BhagyashriWagh GaneshBhakta SwarnavPatra Chinmoy - Tropomodulin-1 (TMOD1) is a key regulator of actin filament dynamics that functions as an actin-binding protein. It specifically caps the slow-growing (pointed) ends of actin filaments, and the interaction is further stabilized by tropomyosin (TPM). By modulating actin monomer polymerization and depolymerization, TMOD1 critically controls filament length, thereby maintaining both the stability and plasticity of actin-based structures. Emerging evidence has highlighted the participation of TMOD1 in diverse cellular processes, such as cytoskeletal organization, neurite outgrowth, cell motility, and cancer progression. This review summarizes recent advances in TMOD1 research and offers a comprehensive overview of its multifaceted biological roles and implications for future studies. - Source: PubMed
Publication date: 2025/10/22
Li YalongPan XuyiGong ZixuanZhu LinMu PingLu Fangjin