Oligosaccharide recognition and binding to the carbohydrate binding module of AMP‐activated protein kinase

Koay, Ann; Rimmer, Kieran; Mertens, Haydyn D. T.; Gooley, Paul R.; Stapleton, David

doi:10.1016/j.febslet.2007.09.044

Cited by 37 publications

(32 citation statements)

References 24 publications

(31 reference statements)

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“…They show addition of glycogen to rat liver AMPK is inhibitory, and when recombinant AMPK is expressed in CCL13 cells, this inhibition is dependent on the presence of CBM. In agreement with Koay et al (256), they provide evidence that inhibition is mediated by the ␣136 linkages and require the key sugar binding Trp residues in the CBM. Isomaltose, but not maltose, inhibited rat liver AMPK with a half-maximal effect at 16 mM (317).…”

Section: E Ampk Interaction With Glycogensupporting

confidence: 75%

“…Another feature of the structure is the extension of the side chain of Leu-146 through the core of the bound cyclodextrin. Solution studies using NMR have also been reported, showing that the CBM binds maltohexose and maltohepulose with K D values Ͻ1 mM while shorter oligosaccharides bind substantially less strongly (256). The NMR results also showed chemical shifts in all the key sugar binding residues in the presence of maltoheptulose with the exception of Trp-100.…”

Section: E Ampk Interaction With Glycogenmentioning

confidence: 71%

“…The NMR results also showed chemical shifts in all the key sugar binding residues in the presence of maltoheptulose with the exception of Trp-100. Because the CBM binds most tightly to carbohydrates containing ␣ 1-4 glycosidic linkages with a single glucose ␣ 1-6 branch, it has been proposed that AMPK may bind to partially degraded glycogen (184,256).…”

Section: E Ampk Interaction With Glycogenmentioning

confidence: 99%

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AMPK in Health and Disease

Steinberg¹,

Kemp²

2009

Physiological Reviews

1,443

1,419

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The function and survival of all organisms is dependent on the dynamic control of energy metabolism, when energy demand is matched to energy supply. The AMP-activated protein kinase (AMPK) αβγ heterotrimer has emerged as an important integrator of signals that control energy balance through the regulation of multiple biochemical pathways in all eukaryotes. In this review, we begin with the discovery of the AMPK family and discuss the recent structural studies that have revealed the molecular basis for AMP binding to the enzyme's γ subunit. AMPK's regulation involves autoinhibitory features and phosphorylation of both the catalytic α subunit and the β-targeting subunit. We review the role of AMPK at the cellular level through examination of its many substrates and discuss how it controls cellular energy balance. We look at how AMPK integrates stress responses such as exercise as well as nutrient and hormonal signals to control food intake, energy expenditure, and substrate utilization at the whole body level. Lastly, we review the possible role of AMPK in multiple common diseases and the role of the new age of drugs targeting AMPK signaling.

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Section: E Ampk Interaction With Glycogensupporting

confidence: 75%

Section: E Ampk Interaction With Glycogenmentioning

confidence: 71%

Section: E Ampk Interaction With Glycogenmentioning

confidence: 99%

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AMPK in Health and Disease

Steinberg¹,

Kemp²

2009

Physiological Reviews

1,443

1,419

View full text Add to dashboard Cite

show abstract

“…Most b subunits also contain carbohydrate-binding modules (CBMs), noncatalytic domains also found in enzymes (in both prokaryotes and eukaryotes) that metabolize starch and glycogen (Machovic and Janecek 2006). The CBMs cause mammalian AMPK to bind to glycogen in intact cells (Hudson et al 2003;Polekhina et al 2003Polekhina et al , 2005Koay et al 2007;Bendayan et al 2009). The physiological role of this remains uncertain, although one function may be to localize AMPK with downstream targets also bound to glycogen, such as glycogen synthase (Carling and Hardie 1989;Jorgensen et al 2004).…”

Section: Role Of Ampk Orthologs In Nonmammalian Eukaryotesmentioning

confidence: 99%

AMP-activated protein kinase—an energy sensor that regulates all aspects of cell function

Hardie¹

2011

Genes Dev.

1,347

1,179

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AMP-activated protein kinase (AMPK) is a sensor of energy status that maintains cellular energy homeostasis. It arose very early during eukaryotic evolution, and its ancestral role may have been in the response to starvation. Recent work shows that the kinase is activated by increases not only in AMP, but also in ADP. Although best known for its effects on metabolism, AMPK has many other functions, including regulation of mitochondrial biogenesis and disposal, autophagy, cell polarity, and cell growth and proliferation. Both tumor cells and viruses establish mechanisms to down-regulate AMPK, allowing them to escape its restraining influences on growth.Living cells use ATP and ADP in a manner similar to the chemicals in a rechargeable battery. Most cellular processes require energy and are driven (directly or indirectly) by the hydrolysis of ATP to ADP and phosphate (or, less frequently, to AMP and pyrophosphate), thus ''flattening the battery.'' In heterotrophic organisms, the battery is recharged by catabolism; i.e., the oxidation of reduced carbon compounds of organic origin, such as glucose. In most cells (especially quiescent cells), oxidation of glucose usually proceeds completely to carbon dioxide via the process of oxidative phosphorylation. Under these conditions, most ATP synthesis occurs at the inner mitochondrial membrane, ATP being generated when protons pumped out via the respiratory chain flow back across the membrane via channels in complex V (the ATP synthase). It has been argued that the endosymbiotic acquisition of aerobic bacteria to form mitochondria was the crucial event in the development of the eukaryotes (Lane and Martin 2010). The large increase in surface area of membrane available for proton transfer (in the form of the inner mitochondrial membrane) allowed a large increase in capacity to generate ATP, which may in turn have allowed the dramatic increase in complexity displayed by eukaryotic cells and organisms. When mitochondria became the main cellular power source, one additional event required was the development of systems that sense energy status in the cytoplasm and then signal this information back to modulate mitochondrial function. Interestingly, AMP-activated protein kinase (AMPK, the subject of this review) fulfills this role and appears to be almost universal in eukaryotes. One interesting exception is Encephalitozoon cuniculi, a eukaryote with a strippeddown genome that appears to have lost not only its mitochondria, but also AMPK (Miranda-Saavedra et al. 2007). However, as it is an obligate intracellular parasite, the host cell would provide both of these missing functions.The obvious way to achieve energy sensing would be to have proteins that monitor the cellular ratio of ATP:ADP. However, because of the very active adenylate kinases in all eukaryotic cells, which catalyze the interconversion of adenine nucleotides (2ADP 4 ATP + AMP), the AMP:ATP ratio tends to change in concert with, and to an even greater extent than, the ADP:ATP ratio (Hardie and Hawley 2001). Thus,...

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“…Previously, CBMs were thought to be motifs that are functionally independent from the catalytic domains located distal to the active sites, and it has been proposed that they enhance the interaction between the carbohydrate substrate and protein (52)(53)(54)(55). For many amylolytic enzymes, CBMs were reportedly involved in starch hydrolysis by disrupting the starch granule structure, which allowed for a concentration of catalytic domains on the surface and carbohydrate starch hydrolysis by proximity (56 -59).…”

Section: Discussionmentioning

confidence: 99%

Association of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus marinus

Jung

Park

et al. 2012

Journal of Biological Chemistry

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Background: Maltogenic amylases that are known to date form dimers to perform hydrolysis. Results: The structure of maltogenic amylase from Staphylothermus showed a novel domain at the N terminus associated with the active site. Conclusion:Staphylothermus amylase has all of its substrate-binding structural components in a single monomer. Significance: This is the first report of the newly observed domain arrangement adopted by hyperthermophilic archaic maltogenic amylase.

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Oligosaccharide recognition and binding to the carbohydrate binding module of AMP‐activated protein kinase

Cited by 37 publications

References 24 publications

AMPK in Health and Disease

AMPK in Health and Disease

AMP-activated protein kinase—an energy sensor that regulates all aspects of cell function

Association of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus marinus

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