Ubiquitin-binding domains

Hicke, Linda A; Schubert, Heidi; Hill, Christopher P.

doi:10.1038/nrm1701

Cited by 722 publications

(737 citation statements)

References 103 publications

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“…Novel UBD in ABIN proteins S Wagner et al is comparable to the affinities of other UBD-Ub interactions (Hicke et al, 2005). The analysis of sequential distribution of Ds in ubiquitin is shown in Figure 2b.…”

Section: Novel Ubd In Abin Proteinsmentioning

confidence: 76%

Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins

et al. 2008

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Deregulated nuclear factor jB (NF-jB) activation plays an important role in inflammation and tumorigenesis. ABIN proteins have been characterized as negative regulators of NF-jB signaling. However, their mechanism of NF-jB inhibition remained unclear. With the help of a yeast two-hybrid screen, we identified ABIN proteins as novel ubiquitin-interacting proteins. The minimal ubiquitin-binding domain (UBD) corresponds to the ABIN homology domain 2 (AHD2) and is highly conserved in ABIN-1, ABIN-2 and ABIN-3. Moreover, this region is also present in NF-jB essential modulator/IjB kinase c (NEMO/IKKc) and the NEMO-like protein optineurin, and is therefore termed UBD in ABIN proteins and NEMO (UBAN). Nuclear magnetic resonance studies of the UBAN domain identify it as a novel type of UBD, with the binding surface on ubiquitin being significantly different from the binding surface of other UBDs. ABIN-1 specifically binds ubiquitinated NEMO via a bipartite interaction involving its UBAN and NEMO-binding domain. Mutations in the UBAN domain led to a loss of ubiquitin binding and impaired the NF-jB inhibitory potential of ABINs. Taken together, these data illustrate an important role for ubiquitin binding in the negative regulation of NF-jB signaling by ABINs and identify UBAN as a novel UBD.

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Section: Novel Ubd In Abin Proteinsmentioning

confidence: 76%

Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins

et al. 2008

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“…Actually, dDsk2 contains a single ubiquitin-binding site of low affinity (K d B400 mM), which is in contrast to most ubiquitin receptors that contain several ubiquitin-binding sites that act synergistically to provide high-affinity binding 2,3,46 . Similarly, the interaction of dDsk2 with H2Bub1 is of low specificity since selective recognition of ubiquitylated substrates is largely based on the recognition of the linkage type, length and anchoring site of a polyubiquitin chain 2,3,46 , and, consequently, requires the presence of several ubiquitin-binding sites. In fact, the UBA domain of dDsk2 recognizes a monoubiquitylation in PTEN with a similar affinity as in H2B (Fig.…”

Section: Discussionmentioning

confidence: 99%

dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

et al. 2015

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dDsk2 is a conserved extraproteasomal ubiquitin receptor that targets ubiquitylated proteins for degradation. Here we report that dDsk2 plays a nonproteolytic function in transcription regulation. dDsk2 interacts with the dHP1c complex, localizes at promoters of developmental genes and is required for transcription. Through the ubiquitin-binding domain, dDsk2 interacts with H2Bub1, a modification that occurs at dHP1c complex-binding sites. H2Bub1 is not required for binding of the complex; however, dDsk2 depletion strongly reduces H2Bub1. Co-depletion of the H2Bub1 deubiquitylase dUbp8/Nonstop suppresses this reduction and rescues expression of target genes. RNA polymerase II is strongly paused at promoters of dHP1c complex target genes and dDsk2 depletion disrupts pausing. Altogether, these results suggest that dDsk2 prevents dUbp8/Nonstop-dependent H2Bub1 deubiquitylation at promoters of dHP1c complex target genes and regulates RNA polymerase II pausing. These results expand the catalogue of nonproteolytic functions of ubiquitin receptors to the epigenetic regulation of chromatin modifications.

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“…In particular, some residues crucial for protein-protein interactions are rather rigid in solution (Ile44, His68). 5, 65 As far as assignments and S CC values are available, the first loop is quite rigid in Ubi-P, however. On the other hand, enhanced dynamics can be detected in Ubi-P residues between Gln40 and Leu50 (Leu43, Ile44) or may be present in others that could not be assigned or analyzed in (2Q,1Q) correlation spectra.…”

Section: Additional Motional Processes and The Influence Ofmentioning

confidence: 99%

Probing Molecular Motion by Double-Quantum (¹³C,¹³C) Solid-State NMR Spectroscopy: Application to Ubiquitin

et al. 2009

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Abstract:We demonstrate the use of two-dimensional ( 13 C, 13 C) double-quantum spectroscopy to detect molecular dynamics by solid-state NMR. Data collected on tyrosine-ethylester (TEE) are in line with previously determined ( 1 H, 13 C) order parameters. Application of these experiments to microcrystalline ubiquitin reveals the presence of dynamics on millisecond or faster time scales and differences in local mobility depending on microcrystal preparation. In addition, solid-state NMR-based structure calculation indicates conformational variability of loop regions between different solid-phase ubiquitin preparations. Our data relate preparation-dependent changes observed in NMR spectral parameters such as chemical shifts and through-space correlations to differences in ubiquitin dynamics and conformation and suggest a prominent role of molecular mobility in microcrystalline ubiquitin.

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Ubiquitin-binding domains

Cited by 722 publications

References 103 publications

Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins

Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins

dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

Probing Molecular Motion by Double-Quantum (¹³C,¹³C) Solid-State NMR Spectroscopy: Application to Ubiquitin

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Ubiquitin-binding domains

Cited by 722 publications

References 103 publications

Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins

Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins

dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

Probing Molecular Motion by Double-Quantum (13C,13C) Solid-State NMR Spectroscopy: Application to Ubiquitin

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Probing Molecular Motion by Double-Quantum (¹³C,¹³C) Solid-State NMR Spectroscopy: Application to Ubiquitin