Solution structure of the kinase‐associated domain 1 of mouse microtubule‐associated protein/microtubule affinity‐regulating kinase 3

Tochio, N.; Koshiba, S.; Kobayashi, Naohiro; Yabuki, Takashi; Aoki, Masaaki; Seki, Eiko; Matsuda, Takayoshi; Tomo, Yasuko; Motoda, Yoko; Kobayashi, Atsuo; Tanaka, Akiko; Hayashizaki, Yoshihide; Terada, Takaho; Shirouzu, Mikako; Kigawa, T.; Yokoyama, Shigeyuki

doi:10.1110/ps.062391106

Cited by 41 publications

(43 citation statements)

References 65 publications

(88 reference statements)

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“…The ␤ Tyr-267 is juxtaposed to ␥1 aromatic residue, Phe-51 in the mammalian structure (556). The ␣-subunit COOH-terminal fragment forms a discreet ␣-helical/␤-strand domain that shares topology with components of the AMPK-related MARK kinases (499). The Townley structure has provided a clear picture explaining the earlier truncation mutagenesis results that showed that the COOH-terminal 25 residues of ␤ (246 -270) were essential for ␥ binding, whereas ␣ binding required 85 residues ␤ (186 -270) (227) (Fig.…”

Section: Subunit Structuresmentioning

confidence: 99%

AMPK in Health and Disease

Steinberg¹,

Kemp²

2009

Physiological Reviews

1,459

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: Subunit Structuresmentioning

confidence: 99%

AMPK in Health and Disease

Steinberg¹,

Kemp²

2009

Physiological Reviews

1,459

1,419

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“…The SnRK1 RD contains a subdomain of unknown function, the kinase-associated1 (KA1) domain, that was reported in the SnRK3.11/Salt Overly Sensitive2 (SOS2) protein kinase to closely superimpose on the protein phosphatase interaction domain (Sánchez-Barrena et al, 2007), a docking site for the clade A PP2C ABI2 (Ohta et al, 2003). Modeling SnRK1.1 with the structures resolved for the KA1 domain in SnRK3.11 (Sánchez-Barrena et al, 2007), the AMPK-related microtubule-affinity-regulating kinase3 (Tochio et al, 2006), and for AMPKa (Xiao et al, 2011), revealed that in SnRK1.1, this subdomain spans residues 390 to 512 (see Supplemental Figure 2 online). As shown, the KA1 domain was both required and sufficient for the interaction with the phosphatase ( Figure 1A).…”

Section: Abi1 and Pp2ca Interact With The Snrk1 Catalytic Subunitmentioning

confidence: 99%

ABI1 and PP2CA Phosphatases Are Negative Regulators of Snf1-Related Protein Kinase1 Signaling in Arabidopsis

et al. 2013

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Plant survival under environmental stress requires the integration of multiple signaling pathways into a coordinated response, but the molecular mechanisms underlying this integration are poorly understood. Stress-derived energy deprivation activates the Snf1-related protein kinases1 (SnRK1s), triggering a vast transcriptional and metabolic reprogramming that restores homeostasis and promotes tolerance to adverse conditions. Here, we show that two clade A type 2C protein phosphatases (PP2Cs), established repressors of the abscisic acid (ABA) hormonal pathway, interact with the SnRK1 catalytic subunit causing its dephosphorylation and inactivation. Accordingly, SnRK1 repression is abrogated in double and quadruple pp2c knockout mutants, provoking, similarly to SnRK1 overexpression, sugar hypersensitivity during early seedling development. Reporter gene assays and SnRK1 target gene expression analyses further demonstrate that PP2C inhibition by ABA results in SnRK1 activation, promoting SnRK1 signaling during stress and once the energy deficit subsides. Consistent with this, SnRK1 and ABA induce largely overlapping transcriptional responses. Hence, the PP2C hub allows the coordinated activation of ABA and energy signaling, strengthening the stress response through the cooperation of two key and complementary pathways.

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“…crystallography and NMR spectroscopy, respectively (13,14), whereas the N-terminal header and the central spacer domains appear to be largely disordered (see Fig. 1A).…”

mentioning

confidence: 99%

Microtubule Affinity Regulating Kinase Activity in Living Neurons Was Examined by a Genetically Encoded Fluorescence Resonance Energy Transfer/Fluorescence Lifetime Imaging-based Biosensor

Timm

Kries

et al. 2011

Journal of Biological Chemistry

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Background: Deregulation of the protein kinase MARK has been linked to Alzheimer disease. Results: Mark-specific inhibitors and a biosensor are identified. Conclusion:The inhibitors and the biosensor are tools to provide new insights into the role of MARK during polarity establishment and maintenance of neurons. Significance: The inhibitors might possess therapeutic potential by interfering with abnormal Tau phosphorylation in Alzheimer disease.

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Solution structure of the kinase‐associated domain 1 of mouse microtubule‐associated protein/microtubule affinity‐regulating kinase 3

Cited by 41 publications

References 65 publications

AMPK in Health and Disease

AMPK in Health and Disease

ABI1 and PP2CA Phosphatases Are Negative Regulators of Snf1-Related Protein Kinase1 Signaling in Arabidopsis

Microtubule Affinity Regulating Kinase Activity in Living Neurons Was Examined by a Genetically Encoded Fluorescence Resonance Energy Transfer/Fluorescence Lifetime Imaging-based Biosensor

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