How does TRIP12 interact with dcaf7?
Best insight from top research papers
TRIP12 interacts with DCAF7 by mediating branched K11-linked ubiquitylation of FBW7, regulating its stability and affecting the abundance of SCFFBW7 substrates . Additionally, DCAF7, also known as WDR68, binds DYRK1A and DYRK1B, playing a crucial role in maintaining normal levels of these kinases . Furthermore, Trip12 is involved in the ubiquitination of Sox6, a transcription factor in muscle cells, leading to its polyubiquitination and subsequent degradation via the ubiquitin-proteasome system . These interactions highlight the diverse roles of TRIP12 in regulating the stability and activity of various proteins involved in critical cellular processes.
Answers from top 5 papers
More filters
Papers (5) | Insight |
---|---|
Not addressed in the paper. | |
37 Citations | Not addressed in the paper. |
15 Citations | Not addressed in the paper. |
39 Citations | Not addressed in the paper. |
9 Citations | Not addressed in the paper. |
Related Questions
How is IL-12 responsivness down regulated with IL-12RB1?5 answersIL-12 responsiveness is downregulated through various mechanisms involving IL-12RB1. One mechanism involves RNA-DNA differences (RDDs) in IL12RB1 mRNA, altering the amino acid sequence and negatively impacting IL-12 binding. Additionally, the processing of IL12RB1 pre-mRNA into Isoform 2 by intragenic competition and microRNA-mediated knockdown experiments promotes IL-12 responses, influencing T cell differentiation. Furthermore, the Jagged-1-Notch signaling pathway can suppress IL-12-induced Th17 cell skewing by downregulating IL-12RB1 expression, leading to reduced IL-12 responsiveness. These findings collectively highlight the intricate regulatory mechanisms involved in modulating IL-12 responsiveness through IL12RB1.
How is DYRK1A related to TRIP12?4 answersDYRK1A, a gene associated with intellectual disability and neurological disorders, has been extensively studied for its diverse roles. It is linked to microcephaly, global developmental delay, and distinctive facial features. Knocking out DYRK1A in zebrafish models revealed implications in neuronal regulation and brain development, particularly in autism-related mobility disorders. Additionally, DYRK1A's overexpression is associated with Down syndrome characteristics like mental retardation and heart defects, indicating its involvement in neurodevelopmental disorders and tumorigenesis. Interestingly, recent research has unveiled a novel role for DYRK1A in regulating the expression of ACE2 and DPP4, crucial receptors for SARS-CoV-2 and other coronaviruses, suggesting its significance in viral entry and infection.
How cannabidiol interacts with nrf2 expression?]?5 answersCannabidiol (CBD) interacts with Nrf2 expression by activating the FXR/Nrf2 pathway, which plays a crucial role in cellular protection against oxidative stress and inflammation. CBD has been shown to increase Nrf2 expression significantly, indicating its potential in enhancing the cytoprotective response under oxidative stress conditions. Additionally, CBD influences the redox balance and inflammation by stimulating the transcription activity of Nrf2 and inhibiting the NFκB pathway, thus promoting antioxidant and anti-inflammatory effects. This interaction highlights CBD's ability to modulate key pathways involved in cellular defense mechanisms, making it a promising candidate for therapeutic interventions targeting oxidative stress-related diseases.
Does trip12 interact with CUL4?5 answersTRIP12 interacts with CUL4. TRIP12 is a putative cofactor of Cullin4 (Cul4) ubiquitin ligase complexes. TRIP12 is an E3 ubiquitin ligase that recognizes and polyubiquitinates Sox6. TRIP12 mediates branched K11-linked ubiquitylation of FBW7, a substrate adaptor for the E3 ubiquitin ligase complex SKP1-CUL1-F-box (SCF). TRIP12 is a member of the HECT domain-containing E3 ubiquitin ligase family. TRIP12 is involved in the regulation of major biological processes through ubiquitination-mediated degradation of key protein substrates.
What is the mechanism by which P120 interacts with the transcription factor Kaiso?5 answersP120 interacts with the transcription factor Kaiso through multiple mechanisms. Firstly, AKT1 can phosphorylate a specific threonine residue (T606) within the RSSTIP motif of Kaiso in the cytoplasm, leading to the formation of pT606-Kaiso. This phosphorylated form of Kaiso can directly bind to 14-3-3 family proteins, and the interaction is dependent on the phosphorylation of T606. Additionally, the interaction between Kaiso and its binding partner P120ctn is essential for the accumulation of pT606-Kaiso in the cytoplasm. The nuclear entry of P120ctn in complex with MUC1-CT promotes the nuclear-to-cytoplasmic translocation of Kaiso. Furthermore, P120ctn can regulate the binding of Kaiso to the β-catenin promoter region, thereby affecting the transcription of β-catenin. These findings suggest that P120 interacts with Kaiso through phosphorylation-dependent binding to 14-3-3 proteins, as well as through its role in the nuclear translocation and regulation of Kaiso's target genes.
What are the roles of FABP7 in neural cell movement?5 answersFABP7 plays a role in neural cell movement. Knockdown of FABP7 reduces the migration of glioblastoma neural stem-like cells. FABP7 is overexpressed in brain tumor stem-like cells (BTSC) and its down-regulation significantly reduces the migration of BTSC. FABP7 is also involved in tumor proliferation and migration in different tumors. FABP7 is expressed in oligodendrocyte progenitor cells (OPCs) and its knockout leads to a decrease in OPC population and impaired differentiation into oligodendrocytes. FABP7 is highly expressed in neural stem cells and its binding target has been identified as a neural stem cell-specific BODIPY derivative compound.