1. Kinase-catalyzed crosslinking: A comparison of ATP-crosslinker analogs.
- Author
-
Bremer HJ, Herppich AA, and Pflum MKH
- Subjects
- Benzophenones chemistry, Benzophenones chemical synthesis, Molecular Structure, Azides chemistry, Humans, Kinetics, Phosphorylation, Adenosine Triphosphate metabolism, Adenosine Triphosphate chemistry, Cross-Linking Reagents chemistry, Cross-Linking Reagents chemical synthesis
- Abstract
Protein phosphorylation is catalyzed by kinases to regulate cellular events and disease states. Identifying kinase-substrate relationships represents a powerful strategy to understand cell biology and disease yet remains challenging due to the rapid dynamics of phosphorylation. Over the last decade, several γ-phosphoryl modified ATP analogs containing crosslinkers were developed to covalently conjugate kinases, their substrates, and their associated proteins for subsequent characterization. Here, kinetics and crosslinking experiments demonstrated that the UV-activated analogs, ATP-aryl azide and ATP-benzophenone, offered the most robust crosslinking, whereas electrophilic ATP-aryl fluorosulfate promoted the most effective proximity-enabled crosslinking. The data will guide future applications of kinase-catalyzed crosslinking to study normal and disease biology., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)
- Published
- 2024
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