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results disclose the mechanism by which cIAP1 RING dimer activates UbcH5B approximately Ub and indicate that noncovalent Ubiquitin (Ub) binding further stabilizes the cIAP1-UbcH5B approximately Ubiquitin (Ub) complex in the active conformation to stimulate Ub transfer
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These results point to an important role of the affinity between RNF4 and its cognate RAD6B or UBCH5B in governing the multiplicity of substrate ubiquitination.
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Knockdown of UBE2D2 caused an increase in p53 protein levels, and knockdown of p53 attenuated not only cadmium-induced apoptosis, but also cadmium-induced apoptosis-related gene expression.
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mutations having marked effects on function only minimally affect the intermolecular interactions between the AO7 RING and UbcH5B, establishing a high degree of complexity in activation through the RING-E2 interface.
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Data show that ubiquitin E2 enzymes UBE2D1/2/3 and E3 ligase RNF138 accumulate at DNA-damage sites and act at early resection stages by promoting CtIP protein ubiquitylation and accrual.
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together with UBE2L3 and UBE2N, synergistically contribute to Parkin-mediated mitophagy
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Presented is the structure of the human dimeric RING domain from BIRC7 in complex with the E2 UbcH5B covalently linked to Ub.
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Whereas UbcH5(A, B and C) is highly efficient in converting IkBa into monoubiquitinated forms, Cdc34 drives ubiquitin (Ub)-Ub conjugation
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determined the 2.2 A crystal structure of an intermediate of UbcH5b approximately ubiquitin (Ub) conjugate, which is assembled into an infinite spiral through the backside interaction.
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role of WW3 and WW4 domains of Nedd4-2 in dopamine transporter ubiquitination was demonstrated; siRNA analysis demonstrated that this polyubiquitination is mediated by Nedd4-2 cooperation with UBE2D and UBE2L3 E2 ubiquitin-conjugating enzymes
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Results describe the crystal structure of a complex between the HECT domain of NEDD4L and the E2 UbcH5B bearing a covalently linked Ub at its active site (UbcH5B approximately Ub).
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Data show that binding of the CNOT4 RING finger to the ubiquitin-conjugating enzyme (E2) UbcH5B is highly selective.
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UbcH5B/C are E2s for Mdm2, which contribute to the maintenance of low levels of p53 and Mdm2 in unstressed cells; inhibition of p53 ubiquitination and degradation by targeting UbcH5B/C is not sufficient to up-regulate p53 transcriptional activity.
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Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation
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UBE2D2 is required for GCMa ubiquitination and for association with the SCF(FBXW2) complex.
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The results imply that the interaction specificity between c-Cbl, UbcH7 and UbcH5b is required but not sufficient for transfer of ubiquitin to potential targets.
