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Targeted Proteomic Approaches for Proteome-Wide Characterizations of the AMP-Binding Capacities of Kinases.
Miao, Weili; Yin, Jiekai; Porter, Douglas F; Jiang, Xiaogang; Khavari, Paul A; Wang, Yinsheng.
Afiliación
  • Miao W; Program in Epithelial Biology, Stanford University School of Medicine, Stanford, California 94305, United States.
  • Porter DF; Program in Epithelial Biology, Stanford University School of Medicine, Stanford, California 94305, United States.
  • Khavari PA; Program in Epithelial Biology, Stanford University School of Medicine, Stanford, California 94305, United States.
J Proteome Res ; 21(8): 2063-2070, 2022 08 05.
Article en En | MEDLINE | ID: mdl-35820187
ABSTRACT
Kinases play important roles in cell signaling, and adenosine monophosphate (AMP) is known to modulate cellular energy homeostasis through AMP-activated protein kinase (AMPK). Here, we explored novel AMP-binding kinases by employing a desthiobiotin-conjugated AMP acyl-phosphate probe to enrich efficiently AMP-binding proteins. Together with a parallel-reaction monitoring-based targeted proteomic approach, we uncovered 195 candidate AMP-binding kinases. We also enriched desthiobiotin-labeled peptides from adenine nucleotide-binding sites of kinases and analyzed them using LC-MS/MS in the multiple-reaction monitoring mode, which resulted in the identification of 44 peptides derived from 43 kinases displaying comparable or better binding affinities toward AMP relative to adenosine triphosphate (ATP). Moreover, our proteomic data revealed a potential involvement of AMP in the MAPK pathway through binding directly to the relevant kinases, especially MEK2 and MEK3. Together, we revealed the AMP-binding capacities of a large number of kinases, and our work built a strong foundation for understanding how AMP functions as a second messenger to modulate cell signaling.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteoma / Proteómica Idioma: En Revista: J Proteome Res Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteoma / Proteómica Idioma: En Revista: J Proteome Res Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos
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