Identification of AMP-activated protein kinase targets by a consensus sequence search of the proteome

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• 作者：Traci L Marin (1) (5)
  Brendan Gongol (1) (5)
  Marcy Martin (1) (2)
  Stephanie J King (1)
  Lemar Smith (1)
  David A Johnson (1)
  Shankar Subramaniam (3)
  Shu Chien (3) (4)
  John Y-J Shyy (1) (2)
  
  1. Divisions of Biochemistry and Molecular Biology and Biomedical Sciences ; University of California ; Riverside ; CA ; 92521-0121 ; USA
  5. Department of Cardiopulmonary Sciences and Anatomy ; Schools of Allied Health and Medicine ; Loma Linda University ; Loma Linda ; CA ; 92350 ; USA
  2. Division of Cardiology ; Department of Medicine ; University of California ; San Diego ; La Jolla ; CA ; 92093 ; USA
  3. Division of Physiology ; Department of Medicine ; University of California ; San Diego ; La Jolla ; CA ; 92093 ; USA
  4. Department of Bioengineering and Institute of Engineering in Medicine ; University of California ; San Diego La Jolla ; CA ; 92093 ; USA
  
• 关键词：AMPK ; AKT2 ; ATF2 ; MMP ; 2 ; FOXO3a ; NADSYN1 ; Phosphorylation consensus sequence ; Bioinformatics ; Proteome ; Network prediction
• 刊名：BMC Systems Biology
• 出版年：2015
• 出版时间：December 2015
• 年：2015
• 卷：9
• 期：1
• 全文大小：1,928 KB
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• 刊物主题：Bioinformatics; Systems Biology; Simulation and Modeling; Computational Biology/Bioinformatics; Physiological, Cellular and Medical Topics; Algorithms;
• 出版者：BioMed Central
• ISSN：1752-0509

文摘

Background AMP-activated protein kinase (AMPK) is a heterotrimeric serine/threonine protein kinase that is activated by cellular perturbations associated with ATP depletion or stress. While AMPK modulates the activity of a variety of targets containing a specific phosphorylation consensus sequence, the number of AMPK targets and their influence over cellular processes is currently thought to be limited. Results We queried the human and the mouse proteomes for proteins containing AMPK phosphorylation consensus sequences. Integration of this database into Gaggle software facilitated the construction of probable AMPK-regulated networks based on known and predicted molecular associations. In vitro kinase assays were conducted for preliminary validation of 12 novel AMPK targets across a variety of cellular functional categories, including transcription, translation, cell migration, protein transport, and energy homeostasis. Following initial validation, pathways that include NAD synthetase 1 (NADSYN1) and protein kinase B (AKT2) were hypothesized and experimentally tested to provide a mechanistic basis for AMPK regulation of cell migration and maintenance of cellular NAD+ concentrations during catabolic processes. Conclusions This study delineates an approach that encompasses both in silico procedures and in vitro experiments to produce testable hypotheses for AMPK regulation of cellular processes.