Chemical Synthesis of Diubiquitin-Based Photoaffinity Probes for Selectively Profiling Ubiquitin-Binding Proteins

2017 ◽  
Vol 129 (10) ◽  
pp. 2788-2792 ◽  
Author(s):  
Jun Liang ◽  
Lin Zhang ◽  
Xiang-Long Tan ◽  
Yun-Kun Qi ◽  
Shan Feng ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Binding Proteins ◽  
Ubiquitin Binding ◽  
Photoaffinity Probes

Chemical Synthesis of Diubiquitin-Based Photoaffinity Probes for Selectively Profiling Ubiquitin-Binding Proteins

2017 ◽  
Vol 56 (10) ◽  
pp. 2744-2748 ◽  
Author(s):  
Jun Liang ◽  
Lin Zhang ◽  
Xiang-Long Tan ◽  
Yun-Kun Qi ◽  
Shan Feng ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Binding Proteins ◽  
Ubiquitin Binding ◽  
Photoaffinity Probes

scholarly journals Non-traditional Functions of Ubiquitin and Ubiquitin-binding Proteins

2003 ◽  
Vol 278 (38) ◽  
pp. 35857-35860 ◽  
Author(s):  
Joshua D. Schnell ◽  
Linda Hicke
Keyword(s):  
Binding Proteins ◽  
Ubiquitin Binding

Ubiquilins in the crosstalk among proteolytic pathways

2012 ◽  
Vol 393 (6) ◽  
pp. 441-447 ◽  
Author(s):  
Dong Yun Lee ◽  
Eric J. Brown
Keyword(s):  
Protein Degradation ◽  
Binding Proteins ◽  
Major Protein ◽  
Degradation Pathways ◽  
Cytosolic Proteins ◽  
Sequestosome 1 ◽  
Ubiquitin Binding ◽  
Proteolytic Pathways

Abstract Protein degradation occurs through several distinct proteolytic pathways for membrane and cytosolic proteins. There is evidence that these processes are linked and that crosstalk among these major protein degradation pathways occurs. Ubiquilins, a family of ubiquitin-binding proteins, are involved in all protein degradation pathways. This minireview provides an overview of ubiquilin function in protein degradation and contrasts it with sequestosome-1 (p62), a protein that also has been implicated in multiple proteolytic pathways.

scholarly journals Regulation of ubiquitin-binding proteins by monoubiquitination

2006 ◽  
Vol 8 (2) ◽  
pp. 163-169 ◽  
Author(s):  
Daniela Hoeller ◽  
Nicola Crosetto ◽  
Blagoy Blagoev ◽  
Camilla Raiborg ◽  
Ritva Tikkanen ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Ubiquitin Binding

scholarly journals It's all about talking: two-way communication between proteasomal and lysosomal degradation pathways via ubiquitin

2016 ◽  
Vol 311 (2) ◽  
pp. C166-C178 ◽  
Author(s):  
Martina P. Liebl ◽  
Thorsten Hoppe
Keyword(s):  
Binding Proteins ◽  
Covalent Attachment ◽  
Special Importance ◽  
Heat Shock Factors ◽  
Substrate Selection ◽  
E3 Ligases ◽  
Age Related ◽  
General Decline ◽  
Ubiquitin Binding ◽  
Proteolytic Pathways

Selective degradation of proteins requires a fine-tuned coordination of the two major proteolytic pathways, the ubiquitin-proteasome system (UPS) and autophagy. Substrate selection and proteolytic activity are defined by a plethora of regulatory cofactors influencing each other. Both proteolytic pathways are initiated by ubiquitylation to mark substrate proteins for degradation, although the size and/or topology of the modification are different. In this context E3 ubiquitin ligases, ensuring the covalent attachment of activated ubiquitin to the substrate, are of special importance. The regulation of E3 ligase activity, competition between different E3 ligases for binding E2 conjugation enzymes and substrates, as well as their interplay with deubiquitylating enzymes (DUBs) represent key events in the cross talk between the UPS and autophagy. The coordination between both degradation routes is further influenced by heat shock factors and ubiquitin-binding proteins (UBPs) such as p97, p62, or optineurin. Mutations in enzymes and ubiquitin-binding proteins or a general decline of both proteolytic systems during aging result in accumulation of damaged and aggregated proteins. Thus further mechanistic understanding of how UPS and autophagy communicate might allow therapeutic intervention especially against age-related diseases.

Total chemical synthesis of the phosphorylated p62 UBA domain reveals that Ser407Pi but not Ser403Pi enhances ubiquitin binding

2020 ◽  
Vol 18 (42) ◽  
pp. 8709-8715
Author(s):  
Ling Xu ◽  
Yan Zhang ◽  
Yi-Ming Li ◽  
Xian-Fu Lu
Keyword(s):  
Chemical Synthesis ◽  
Binding Affinity ◽  
Ubiquitin Binding ◽  
Uba Domain

Based on total chemical synthesis we prepared four types of phosphorylated p62 UBAs and found that phosphorylation at S407 but not at S403 enhanced the binding affinity between UBA and Ub.

scholarly journals RPN10: A Case Study for Ubiquitin Binding Proteins and More

2019 ◽  
Vol 31 (7) ◽  
pp. 1398-1399 ◽  
Author(s):  
Pascal Genschik
Keyword(s):  
Binding Proteins ◽  
Ubiquitin Binding

Molecular control of the NEMO family of ubiquitin-binding proteins

2013 ◽  
Vol 14 (10) ◽  
pp. 673-685 ◽  
Author(s):  
Kristopher Clark ◽  
Sambit Nanda ◽  
Philip Cohen
Keyword(s):  
Binding Proteins ◽  
Molecular Control ◽  
Ubiquitin Binding
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