Structural Mechanisms Underlying Posttranslational Modification by Ubiquitin-Like Proteins

Dye, Billy T.; Schulman, Brenda A.

doi:10.1146/annurev.biophys.36.040306.132820

Cited by 234 publications

(210 citation statements)

References 104 publications

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“…Competitive binding experiments revealed UBC9 to be an E2 enzyme that dissociate with E1 before formation of E3 complex for sumoylation [43] which strengthens our postulation that RPL27 could deregulate sumolyation through formation of distinct complexes. …”

Section: Rpl27/ubc9 (Pdb Id: 1a3s)supporting

confidence: 83%

Bioinformatics Analysis of the Ribosomal Proteins,RPL27, RPL37a and RPL41: 3-D Protein Modeling and Protein-protein Interaction Prediction

Chan¹,

Sim²

2013

IJBBB

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Abstract-Ribosomal proteins (RPs) are constituents of ribosome important for protein biosynthesis but likely to have extraribosomal functions. Many RPs are associated with various diseases and cancers. A previous study reported RPL27, RPL37a and RPL41 gene to be downregulated in nasopharyngeal carcinoma (NPC) derived cell lines compared to their normal counterpart. However, their actual physiological roles in organogenesis or tumorigenesis have not been properly defined. In this paper, we report on the findings of structural prediction of these three genes and infer their interactions with other proteins using structural neighbor prediction and molecular docking strategies. Our results revealed that RPL27 interact with SYNJ2 and UBC9. RPL27 is predicted to mediate RNA binding protein and deregulate sumolyation. RPL37a is suggested to interact with CTNNB1, SCMH1 and ATBF1. It is predicted to deregulate Wnt degradation pathway, inhibit β-catenin migration and regulate homeotic transcription. Our studies on RPL41 did not allow logical inference on possible interacting factors. Nevertheless, results on RPL27 and RPL37a provide rational data for the elucidation of their molecular activities.Index Terms-Protein modeling, extraribosomal functions, protein-protein interaction prediction, ribosomal protein.

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Section: Rpl27/ubc9 (Pdb Id: 1a3s)supporting

confidence: 83%

Bioinformatics Analysis of the Ribosomal Proteins,RPL27, RPL37a and RPL41: 3-D Protein Modeling and Protein-protein Interaction Prediction

Chan¹,

Sim²

2013

IJBBB

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“…The conjugation of ubiquitin and UBLs requires the consecutive action of three specific enzymes: Ubl-activating enzymes (E1s), Ubl-conjugating enzymes (E2s) and Ublprotein ligases (E3s). Specific proteases reverse this process, removing ubiquitin from target proteins [19,20]. Ubiquitin is a highly conserved, small protein of 8.5 kDa involved in diverse functions, such as protein degradation, endocytic trafficking, signal transduction and DNA repair, among others.…”

Section: Ubiquitination and Ubiquitin-like Modifiers (Ubls)mentioning

confidence: 99%

Post-translational add-ons mark the path in exosomal protein sorting

Moreno-Gonzalo

Fernández-Delgado

Sánchez‐Madrid

2017

Cell. Mol. Life Sci.

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“…Proteins are targeted to the proteasome by modification with ubiquitin chains, whose assembly depends on a cascade of E1, E2, and E3 enzymes (1,2). E3s containing a RING-domain recruit substrates and ubiquitin-charged E2s, and promote the transfer of ubiquitin from the E2 active site to a substrate lysine.…”

mentioning

confidence: 99%

Identification of a physiological E2 module for the human anaphase-promoting complex

Williamson

Wickliffe

Mellone

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

270

380

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Ubiquitination by the anaphase-promoting complex (APC/C) is essential for proliferation in all eukaryotes. The human APC/C promotes the degradation of mitotic regulators by assembling K11-linked ubiquitin chains, the formation of which is initiated by its E2 UbcH10. Here, we identify the conserved Ube2S as a K11-specific chain elongating E2 for human and Drosophila APC/C. Ube2S depends on the cell cycledependent association with the APC/C activators Cdc20 and Cdh1 for its activity. While depletion of Ube2S already inhibits APC/C in cells, the loss of the complete UbcH10/Ube2S-module leads to dramatic stabilization of APC/C substrates, severe spindle defects, and a strong mitotic delay. Ube2S and UbcH10 are tightly co-regulated in the cell cycle by APC/C-dependent degradation. We conclude that UbcH10 and Ube2S constitute a physiological E2-module for APC/C, the activity of which is required for spindle assembly and cell division.K11-linked chain ͉ proteasome ͉ ubiquitin

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Structural Mechanisms Underlying Posttranslational Modification by Ubiquitin-Like Proteins

Cited by 234 publications

References 104 publications

Bioinformatics Analysis of the Ribosomal Proteins,RPL27, RPL37a and RPL41: 3-D Protein Modeling and Protein-protein Interaction Prediction

Bioinformatics Analysis of the Ribosomal Proteins,RPL27, RPL37a and RPL41: 3-D Protein Modeling and Protein-protein Interaction Prediction

Post-translational add-ons mark the path in exosomal protein sorting

Identification of a physiological E2 module for the human anaphase-promoting complex

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