The Ubc9 modulates the function of SLP-76 in T cell activation both by direct interaction and by SUMOylation of SLP-76 and that the Ubc9-SLP-76 module acts as a novel regulatory complex in the control of T cell activation.
With the aim of investigating RHES 3D structure and function bioinformatic analyses and molecular modelling have been performed in the present study based on which RHES regions predicted to be involved in the interaction with mHtt or the SUMOE2 ligase Ubc9 have been identified.
The results indicate that SUMO interacts with VP24 and promotes its USP7-mediated deubiquitination playing a key role in the interference with the innate immune response mediated by the viral protein.
Findings suggest that nuclear DNA leakage activates nucleophagy through UBC9-mediated SUMOylation of lamin A/C leading to degradation of nuclear components including lamin A/C and leaked nuclear DNA.
It demonstrates the enzyme/substrate nature of Ubc9/CRMP2 binding and identify hot spots on CRMP2 that may form the basis of future drug discovery campaigns disrupting the CRMP2-Ubc9 interaction to recapitulate allosteric regulation of NaV1.7 for pain relief.
Data show that the forkhead Box Protein P3 (FOXP3) response element at the -310 bp region but not the -2182 bp region is mainly required for ubiquitin conjugating enzyme 9 (UBC9) activation by FOXP3.
Study demonstrated overexpression of Ubc9 protein in osteosarcoma. Silencing Ubc9 in osteosarcoma cell lines induced decoupling of SUMO1 from Cx43 generating increased free Cx43 levels which is important for reconstructing gap junction intercellular communication and recovering cellular functions.
Detailed structural thermodynamic and kinetics results of the interactions between Ubc9 and its K65 acetylated variant (Ac-Ubc9(K65)) with three NDSMs derived from Elk1 CBP and Calpain2 were shown to rationalize the mechanism beneath this reduced binding.
Ubc9 is an essential regulator of ADAP where it is required for TCR-induced membrane recruitment of the small GTPase Rap1 and its effector protein RapL and for activation of the small GTPase Rac1 in T cell adhesion.
Sumoylation of PML with SUMO2 by UBC9/UBE2I can lead to formation of polymeric SUMO chains. Data suggest that coordination of growing poly-SUMO chain with "back side" binding site on UBC9/UBE2I appears to be required for SUMO chain elongation on PML. (PML = promyelocytic leukemia protein; SUMO2 = small ubiquitin-like modifier 2; UBC9/UBE2I = ubiquitin-conjugating enzyme UBC9/UBE2I)
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