Ask about this productRelated genes to: Rictor antibody
- Gene:
- RICTOR NIH gene
- Name:
- RPTOR independent companion of MTOR complex 2
- Previous symbol:
- -
- Synonyms:
- MGC39830, AVO3, PIA, KIAA1999
- Chromosome:
- 5p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2009-05-29
- Date modifiied:
- 2019-03-19
Related products to: Rictor antibody
Related articles to: Rictor antibody
- mTORC2, defined by its core component RICTOR, is a key regulator of immune cell function and inflammation, yet its roles have long been underappreciated due to lack of specific inhibitors and in vivo tools. - Source: PubMed
Publication date: 2026/09/17
Xu JingtingZhong WenxinXin FeiXu FeiZheng ZehangGuo Fengjing - Apoptosis and mitochondrial bioenergetic dysfunction are hallmarks of cardiotoxicity that drive cardiac damage, particularly following exposure to chemotherapeutic agents such as doxorubicin. Doxorubicin induces pro-apoptotic signaling and disrupts mitochondrial homeostasis and cellular energy metabolism, leading to cardiac injury. Ambrisentan, a selective endothelin A (ET) receptor antagonist, was investigated in this study for its protective effects against doxorubicin-induced injury in H9c2 cardiomyoblasts, focusing on the p53 and mTOR signaling pathways. Pre-treatment with ambrisentan preserved cardiomyocyte viability, attenuated apoptosis, reduced cytosolic and mitochondrial reactive oxygen species accumulation, restored mitochondrial membrane potential, and improved mitochondrial respiration and glycolytic capacity following doxorubicin exposure. Transcriptional and translational analyses showed that these effects were consistent with an induced pro-survival phenotype and improved mitochondrial integrity. Specifically, ambrisentan suppressed apoptotic markers (p-p53/p53, BAX), the mitochondrial fission regulator DNM1, and endothelin components (ET-1, ET receptor). Concurrently, it restored the anti-apoptotic regulator Bcl-2, key mitochondrial regulators (NRF1, PGC1α, OPA1, ATP5A), and mTOR-associated proteins (p-mTOR/mTOR, Rictor, Raptor), while reducing Beclin-1 expression. Pharmacological modulation further demonstrated that the p53 inhibitor pifithrin-α enhanced the protective effects of ambrisentan; conversely, the p53 activator nutlin-3 reduced them, suggesting a possible role for p53 signaling in mediating these responses. Moreover, inhibition of mTOR signaling with rapamycin attenuated the beneficial effects of ambrisentan on oxidative stress, apoptosis, and mitochondrial dysfunction. Collectively, these findings suggest that ambrisentan protects cardiomyocytes from doxorubicin-mediated injury, with potential involvement of p53- and mTOR-associated signaling in preserving redox homeostasis and cellular bioenergetics. - Source: PubMed
Publication date: 2026/09/11
Khine Hnin Ei EiMangmool SupachokeParichatikanond Warisara - - Source: PubMed
Morrison Joly MeghanHicks Donna JJones BayleySanchez VioletaEstrada Monica ValeriaYoung ChristianWilliams MichelleRexer Brent NSarbassov Dos DMuller William JBrantley-Sieders DanaCook Rebecca S - Type 1 diabetes (T1D) is a systemic metabolic disorder associated with male reproductive dysfunction. Given the pivotal role of actin cytoskeleton remodeling in spermatogenesis and sperm function, this study investigated the effects of T1D on actin-regulating pathways in rat testis and spermatozoa (SPZ). Adult Wistar rats were rendered diabetic by streptozotocin administration (65 mg/kg, i.p.). Testicular analysis revealed a reduced F-/G-actin ratio together with marked F-actin disorganization, consistent with altered actin cytoskeleton remodeling. To investigate the molecular mechanisms underlying these alterations, key regulators of actin dynamics were examined. Diabetic animals displayed impaired expression of EPS8, Fascin, N-WASP, and the ARP2/3 complex, suggesting altered regulation of actin assembly, bundling, and branching. Further analyses demonstrated dysregulation of signaling pathways governing cytoskeletal organization. Reduced levels of phosphorylated Disheveled-2, DAAM1, RhoA-GTP, and ROCK1 indicated impairment of the planar cell polarity pathway. In parallel, changes in LIMK1/cofilin phosphorylation supported abnormal regulation of actin filament turnover. Alterations in the RICTOR/PKC/MARCKS signaling pathway further highlighted defects in cytoskeletal control. Similar abnormalities were observed in mature SPZ, where altered F-actin distribution and DAAM1 localization suggested persistent cytoskeletal defects. Moreover, diabetic SPZ exhibited a reduced ability to undergo acrosome reaction, accompanied by altered MARCKS phosphorylation, highlighting defects in actin-dependent processes essential for sperm function and fertilizing capacity. These findings indicate that disruption of actin cytoskeleton dynamics may represent a major mechanism contributing to testicular and sperm abnormalities in T1D, providing new insights into the mechanisms underlying diabetes-associated male reproductive dysfunction. - Source: PubMed
Publication date: 2026/08/19
Ambruosi Maria RosariaBiasi AlessandraBoccella SerenaRomdhani IlefFalvo SaraGuida FrancescaMaione SabatinoMinucci SergioVenditti Massimo - Programmed cell death 4 (Pdcd4) is a well-established tumor suppressor as well as an inhibitor of protein translation. Although Pdcd4-mediated translational repression contributes to tumor suppression, emerging evidence suggests that Pdcd4 also exerts translation-independent functions. In this study, we found that Pdcd4 suppresses tumorigenesis through disrupting mTORC2 complex formation by binding with the rapamycin-insensitive companion of mTOR (Rictor), a core component of the mTORC2 complex. Using deletion mapping and site-directed mutagenesis, we defined the Rictor-binding domain of Pdcd4 and identified three critical residues, R105, K108, and R110, for this interaction. Co-immunoprecipitation and in vitro kinase assays demonstrated that Pdcd4 binding to Rictor disrupted mTORC2 complex assembly and inhibited its kinase activity. Reverse phase protein array analysis revealed that 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (PFKFB3), a key regulator of glycolysis, was markedly upregulated in Pdcd4-knockdown cells. Restoration of wild-type Pdcd4, but not a Rictor-binding-deficient mutant, reduced PFKFB3 protein abundance by promoting ubiquitin-proteasome-mediated degradation. Functionally, Pdcd4-Rictor interaction suppressed glycolytic activity and inhibited tumor cell proliferation in cultured cells and xenograft models. Consistent with these findings, non-small cell lung cancer (NSCLC) tissues exhibited significantly elevated protein levels of Rictor and PFKFB3 compared with adjacent normal tissues, with a positive correlation between their expression. Collectively, these results demonstrate that Pdcd4-Rictor interaction disrupts mTORC2 signaling and downregulates PFKFB3, which plays a critical role in suppressing NSCLC growth and glycolysis. - Source: PubMed
Publication date: 2026/08/26
Wang QingXin YumengZokaei ElhamZeng LiangPiecoro DavaChen MinZhang YanquanYang Katie SWang ChiLiu XiaoqiYang Hsin-Sheng