Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.31 (AMP-activated protein kinase)
 13,065 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Snf1/AMPK protein kinase family is widely conserved in eukaryotes. In Saccharomyces cerevisiae, the Snf1 kinase is an essential element of the glucose response pathway and has diverse regulatory roles. The Snf1 complex contains one of the related proteins Sip1, Sip2 and Gal83, which are also conserved in higher eukaryotes. Previous studies showed that the Sip1/Sip2/Gal83 component plays a structural role in the complex. We present evidence that this component also mediates the interaction of the Snf1 kinase complex with specific targets. We show that Gal83 mediates the association of the kinase with Sip4, a Snf1-regulated transcription activator of gluconeogenic genes. Gal83 interacts with Sip4 in two-hybrid assays in vivo, and bacterially expressed proteins bind in vitro. Moreover, Gal83 is required for the two-hybrid interaction of Sip4 with the Snf1 kinase. Gal83 also facilitates the rapid Snf1-dependent phosphorylation and activation of Sip4 in response to glucose limitation, indicating that Gal83 mediates the functional interaction of Snf1 with Sip4. Evidence indicates that Sip1 and Sip2 do not interact with Sip4. We propose that members of the Sip1/Sip2/Gal83 family confer specificity to the kinase complex in its interactions with target proteins.
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PMID:Gal83 mediates the interaction of the Snf1 kinase complex with the transcription activator Sip4. 1058 Dec 41

The Arabidopsis thaliana SOS2 and SOS3 genes are required for intracellular Na(+) and K(+) homeostasis and plant tolerance to high Na(+) and low K(+) environments. SOS3 is an EF hand type calcium-binding protein having sequence similarities with animal neuronal calcium sensors and the yeast calcineurin B. SOS2 is a serine/threonine protein kinase in the SNF1/AMPK family. We report here that SOS3 physically interacts with and activates SOS2 protein kinase. Genetically, sos2sos3 double mutant analysis indicates that SOS2 and SOS3 function in the same pathway. Biochemically, SOS2 interacts with SOS3 in the yeast two-hybrid system and in vitro binding assays. The interaction is mediated by the C-terminal regulatory domain of SOS2. SOS3 activates SOS2 protein kinase activity in a Ca(2+)-dependent manner. Therefore, SOS3 and SOS2 define a novel regulatory pathway important for the control of intracellular ion homeostasis and salt tolerance in plants.
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PMID:The Arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein SOS3. 1072 50

In filamentous ascomycetes, glucose repression is mediated by CRE1, a zinc-finger protein related to Miglp from yeast. Five putative AMPK phosphorylation motifs identified in the glucose repressor from the phytopathogenic fungus Sclerotinia sclerotiorum were mutated in a GFP::CRE1 translational fusion. Complementation experiments in Aspergillus nidulans and fluorescence microscopy analyses showed that mutation of one site (Ser266) abolishes the repressor activity of the fusion protein but not its nuclear targeting, suggesting that an AMPK protein kinase may be involved in the function of the fungal glucose repressor.
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PMID:Mutation of a putative AMPK phosphorylation site abolishes the repressor activity but not the nuclear targeting of the fungal glucose regulator CRE1. 1085 70

Yeast Snf4 is a prototype of activating gamma-subunits of conserved Snf1/AMPK-related protein kinases (SnRKs) controlling glucose and stress signaling in eukaryotes. The catalytic subunits of Arabidopsis SnRKs, AKIN10 and AKIN11, interact with Snf4 and suppress the snf1 and snf4 mutations in yeast. By expression of an Arabidopsis cDNA library in yeast, heterologous multicopy snf4 suppressors were isolated. In addition to AKIN10 and AKIN11, the deficiency of yeast snf4 mutant to grown on non-fermentable carbon source was suppressed by Arabidopsis Myb30, CAAT-binding factor Hap3b, casein kinase I, zinc-finger factors AZF2 and ZAT10, as well as orthologs of hexose/UDP-hexose transporters, calmodulin, SMC1-cohesin and Snf4. Here we describe the characterization of AtSNF4, a functional Arabidopsis Snf4 ortholog, that interacts with yeast Snf1 and specifically binds to the C-terminal regulatory domain of Arabidopsis SnRKs AKIN10 and AKIN11.
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PMID:Functional identification of an Arabidopsis snf4 ortholog by screening for heterologous multicopy suppressors of snf4 deficiency in yeast. 1092 6

The winged helix transcription factor Qin is the avian homolog of the mammalian brain factor 1 (BF-1) and has the potential to act as an oncogenic protein. We used representational difference analysis to identify genes that are differentially expressed in chicken embryo fibroblasts (CEF) transformed by Qin. One of the up-regulated Qin targets identified in this analysis is a serine-threonine kinase termed Qik (Qin-induced kinase). Qik belongs to the AMPK/SNF1 kinase family. It is a ubiquitously expressed protein and is upregulated rapidly after a hormone-regulated form of Qin is activated. In vitro kinase tests demonstrate that Qik is capable of autophosphorylation. Elevated levels of Qik transcripts are also observed in Src-transformed cells, suggesting that Src and Qin share some targets.
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PMID:The new serine-threonine kinase, Qik, is a target of the Qin oncogene. 1102 14

Modification of histones is an important element in the regulation of gene expression. Previous work suggested a link between acetylation and phosphorylation, but questioned its mechanistic basis. We have purified a histone H3 serine-10 kinase complex from Saccharomyces cerevisiae and have identified its catalytic subunit as Snf1. The Snf1/AMPK family of kinases function in conserved signal transduction pathways. Our results show that Snf1 and the acetyltransferase Gcn5 function in an obligate sequence to enhance INO1 transcription by modifying histone H3 serine-10 and lysine-14. Thus, phosphorylation and acetylation are targeted to the same histone by promoter-specific regulation by a kinase/acetyltransferase pair, supporting models of gene regulation wherein transcription is controlled by coordinated patterns of histone modification.
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PMID:Snf1--a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. 1149 92

The AMP-activated protein kinase cascade is a sensor of cellular energy charge, and its existence provides strong support for the energy charge hypothesis first proposed by Daniel Atkinson in the 1960s. The system is activated in an ultrasensitive manner by cellular stresses that deplete ATP (and consequently elevate AMP), either by inhibiting ATP production (e.g., hypoxia), or by accelerating ATP consumption (e.g., exercise in muscle). Once activated, it switches on catabolic pathways, both acutely by phosphorylation of metabolic enzymes and chronically by effects on gene expression, and switches off many ATP-consuming processes. Recent work suggests that activation of AMPK is responsible for many of the effects of physical exercise, both the rapid metabolic effects and the adaptations that occur during training. Dominant mutations in regulatory subunit isoforms (gamma2 and gamma3) of AMPK, which appear to increase the basal activity in the absence of AMP, lead to hypertrophy of cardiac and skeletal muscle respectively.
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PMID:AMP-activated protein kinase: the energy charge hypothesis revisited. 1174 30

Sensory signals regulate multiple developmental and behavioral circuits in C. elegans, providing a genetically tractable system in which to investigate the mechanisms underlying the acquisition and integration of sensory information. kin-29 mutants are defective in the expression of a set of chemoreceptor genes, and exhibit characteristics associated with altered sensory signaling, including increased lifespan, decreased body size, and deregulated entry into the dauer developmental stage. kin-29 encodes a Ser/Thr kinase with similarity to the MARK and AMPK/SNF1 family of kinases. We show that KIN-29 acts cell-autonomously and non-cell-autonomously in sensory neurons to regulate chemoreceptor expression, body size, and the dauer decision, suggesting that kin-29 function is essential for the correct acquisition and transduction of sensory information.
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PMID:Regulation of chemosensory receptor expression and sensory signaling by the KIN-29 Ser/Thr kinase. 1183 25

Increased fatty acid metabolism can decrease cardiac function and efficiency, and may therefore contribute to the outcome of ischemic injury in the diabetic. Alterations in the control of myocardial malonyl CoA levels is an important contributing factor to these high fatty acid oxidation rates. This includes alterations in AMPK, ACC, and MCD activity in the diabetic rat heart. A further understanding of how malonyl CoA controls fatty acid oxidation in the diabetic heart should help identify new targets for pharmacological intervention which decreases the reliance of the heart on fatty acid oxidation, and ultimately improves heart function.
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PMID:Malonyl CoA control of fatty acid oxidation in the diabetic rat heart. 1190 Mar 64

We studied the effects of exercise on GLUT4 gene transcription in several lines of transgenic mice expressing the chloramphenicol acyltransferase (CAT) reporter gene, driven by various lengths of the human GLUT4 promoter (2400, 1600, 895, and 730 bp). In all transgenic lines examined, endogenous GLUT4 mRNA increased in response to exercise (19-90%, P < 0.05). Exercise increased CAT mRNA (51-83%, P < 0.05) in mice when the transgene was driven by at least 895 bp of the promoter but showed no effect in mice in which the transgene was driven by only 730 bp. These results suggest that the exercise-induced increase in the transcriptional activity of the human GLUT4 gene is mediated, at least in part, by element(s) within -895 bp of the promoter. These observations reveal a striking similarity to the time course and regional promoter requirements of AMPK-induced GLUT4 gene expression, providing further evidence that AMPK may be mediating the effects of exercise on GLUT4 expression.
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PMID:Exercise-induced transcription of the muscle glucose transporter (GLUT 4) gene. 1190 77


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