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- Table of Contents
Facts about Rapamycin-insensitive companion of mTOR.
MTORC2 seems to work upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. MTORC2 promotes the serum-induced formation of stress-fibers or F-actin.
Mouse | |
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Gene Name: | Rictor |
Uniprot: | Q6QI06 |
Entrez: | 78757 |
Belongs to: |
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RICTOR family |
AVO3 homolog; AVO3; hAVO3; KIAA1999DKFZp686B11164; mAVO3; MGC39830; PIA; Pianissimo; rapamycin-insensitive companion of mTOR; Rictor; RPTOR independent companion of MTOR, complex 2; TORC2-specific protein AVO3
Mass (kDA):
191.57 kDA
Mouse | |
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Location: | 15|15 A1 |
Sequence: | 15; |
Boster Bio has many advantages: Researchers can submit results for species, applications, special samples, and more. Researchers can also get product credits for their findings. These credits are available to all scientists worldwide. Boster Bio: Best Uses of The RICTORMarker
HMGB1 upregulation with RICTOR mRNA, in HCC cell cells, is associated with enhanced Autophagy and inhibits development of the Disease. HMGB1 was shown to play a crucial role in tumor growth. Study results showed that HMGB1 deficiencies inhibited the development and progression of the disease by inhibiting the autophagy process.
HMGB1 expression was examined in liver tissue from 11 patients with HCC. It was found to be significantly higher in tumors than normal tissue and para-tumor tissue. It is still not clear what role HMGB1 plays in the development and progression of early HCC. HMGB1 is important in the carcinogenesis of HCC, but its role in its expression is not yet known.
Autophagy is a process in the cell that regulates many aspects of tumor growth and progression. It is also involved in preventing the damage caused by cell death. Inhibition of autophagy leads to accumulation of the tumor-promoting protein p62. This can result in tumor initiation. Moreover, autophagy is also inhibited when HMGB1 is down-regulated. This is critical for HCC progression.
This study provides preliminary evidence to suggest that HMGB1 may be co-regulated with RICTOR mRNA at early stage HCC. HMGB1 expression in HBV+ early stage HCC was significantly associated to RICTOR. These findings are important for RNA-based therapeutic targeting. CeRNA regulation appears to be a specific type of HCC.
We first investigated how RICTOR interferes in bone formation and osteogenesis. This was done by inhibiting mRNAs containing HMGB1-RICTOR genes. These two genes are involved in skeletal development and the bone-forming process. They both promote the development of adipogenesis. Specifically RICTOR inhibits mRNAs encoding the HMGB1 receptor.
To understand how RICTOR interferes with bone-forming cells, we used an array of biological samples that included HCC cell lines. We found several genes that co-express RICTOR1 and HMGB1. In a subset of these genes, HMGB1 and RICTOR were co-expressed in HBV-positive early-stage tumors. HBV-negative cells had this tendency, however.
Mice that lack siRICTOR were given siRICTOR, an anti-RICTOR mRNA. These mice had lower BMDs and BV/TV. The mRNAs that regulate RICTOR and its targets were also significantly decreased. These animals also had higher miR-152 levels and decreased RICTOR levels. Mice without siRICTOR had an increased rate of bone loss.
The miR-200 family has many members including HMGB1 and RICTOR. MiR-200a/200b/429 imitators inhibit mRNA transcription in HMGB1 (RICTOR). Both of these molecules interfer with mTOR and their interferences with HMGB1/RICTOR were significant. The effects of miR200a/200b/429 imitations in RICTOR targeted tumors are consistent and similar to the effects of HMGB1.
Boster Bio researchers recently demonstrated that RICTOR can be overexpressed in cancer cells to rescue malignant proliferation in HMGB1-positive KDHC cells. This could be due to epigenetically regulated upregulation HMGB1 mRNA. Further, they show that overexpression of RICTOR might help regulate PD-L1+ exosome activity.
Overexpression of RICTOR was found to inhibit cell growth and prevent cell death in liver cancer cells. These results were consistent with a prior study that showed that RICTOR was not required to prevent the development hepatocellular carcinoma. These results have implications for recombinant liver cancer cells. Further studies are needed to confirm if RICTOR overexpression causes an increased risk for cancer.
This study found that Rictor deficiencies inhibited T.ALL development and prevented leukemic cells from growing. FoxO3a is an important regulator of T-ALL growth. In addition, it inhibits the development of certain types of cancer in mice. These results suggest Rictor may be associated to a lower chance of developing cancer. This study could ultimately lead to the development of a new vaccine for T.ALL.
In vitro, RICTOR has been shown to inhibit HCC cell proliferation. T-ALL cells in a mouse model were seeded in the upper compartment of a transwell-based insert. The lower chambers of the insert were treated with BM, spleen or BM cells. The migration index was calculated based a percentage GFP+ cells that had successfully migrated.
The RICTOR marker, an important regulator protein, plays a role within the insulin signalling pathway. The Ant-215 microRNA increased Rictor expression in H4IIE cell transfected with it. In a separate study, miR-215 knockdown significantly reduced Rictor protein expression in the liver of CD rats and HFD rats. This finding suggests that miR-215 may be a useful tool when studying insulin resistance.
The Rictor 3’-UTR is a plasmid that contains regulatory elements for miR-215. The KOD Plus mutagenesis tool from Toyobo Life Science was used for mutation of the plasmid. H4IIE cells had been cultured in a 48 well plate and were co-transfected by Rictor-3’-UTR weight, pGL3basic internal reference, and miR-215 replicas-NC. Cells were then lysed for 48 hours following transfection.
The Boster Bio RICTOR monoclonally-produced antibodies have excellent binding properties, which make them a good choice for immunotherapy and gene therapy applications. These antibodies have been validated in various methods, including Western Blotting, Flow Cytometry, ELISA, and immunohistochemistry. They are also compatible with a variety of cell types including human, monkey, and mice.
China's study indicates that inhibition of RICTOR expression by HSCs may lead increase in cardiomyocyte differentiation. The knockdown Rictor resulted in a decrease in expression of cardiac-specific proteins such as a-Actinin. Rictor-deficient MES cells also showed a decrease at the rate of beating embryoid corps. Ultimately, RICTOR might be a useful reference for induced pluripent stem cells.
Although both mTORC2 und RICTOR regulate mTOR's activity, they act in distinct ways. In addition to regulating cell cycle and survival, RICTOR regulates apoptosis and innate immune responses. A decrease in RICTOR expression results in reduced AKT signalling, and an increase of nuclear FOXO1 protein expression. RICTOR also inhibits AKT activation which results in impaired phosphorylation.
Knockdown Rictor resulted in a decrease of three cell junction protein abundances. It reduced the phosphorylation forms Cx43. Knockdown Rictor resulted in a reduction of ventricular cells. Rictor knockdown resulted in a reduction of the electrophysiological features, including arrhythmia, in cardiac myocytes. These findings suggest that Rictor/mTORC2 have a critical role in normal cardiomyocyte development. If these findings are confirmed, it could be possible to use this knowledge to develop effective treatment strategies for cardiovascular diseases.
The knockdown of Rictor decreases the cell viability of monocytes and macrophages. Atherosclerosis rates were dramatically reduced in male and female mice with the RICTOR-mutation. This suggests that reducing RICTOR expression at HSCs may inhibit cardiomyocyte differentiation in patients suffering from congenital heart disease. The mTOR level of Rictor-deficient mice is also reduced. This suggests the knockdown Rictor may reduce the phosphorylation Akt, a key mTOR-substrate.
PMID: 15467718 by Jacinto E., et al. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive.
PMID: 16962829 by Shiota C., et al. Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability.