Crystal structure of the kinase and UBA domains of SNRK reveals a distinct UBA binding mode in the AMPK family

Wang, Yulu; Wang, Jue; Chen, Xiang; Wang, Zhixin; Wu, Jiawei

doi:10.1016/j.bbrc.2017.10.105

Cited by 14 publications

(13 citation statements)

References 31 publications

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“…SOS2, a large family of protein kinases, has two similar kinases in yeast and mammals: sucrose nonfermenting 1 (SNF1) and AMP-activated protein kinases (AMPKs). In plants, these proteins are generally referred to as SNF1-related kinases (SnRKs), which play a major role in regulating gene expression in plant cells [ 64 ]. In several plants, members of the SnRK subfamily have been identified [ 65 , 66 ].…”

Section: Ionic Stress Signalingmentioning

confidence: 99%

Sensing of Abiotic Stress and Ionic Stress Responses in Plants

Zhang

Jahan

et al. 2018

IJMS

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Plants need to cope with complex environments throughout their life cycle. Abiotic stresses, including drought, cold, salt and heat, can cause a reduction in plant growth and loss of crop yield. Plants sensing stress signals and adapting to adverse environments are fundamental biological problems. We review the stress sensors in stress sensing and the responses, and then discuss ionic stress signaling and the responses. During ionic stress, the calcineurin B-like proteins (CBL) and CBL-interacting protein kinases (CBL−CIPK) complex is identified as a primary element of the calcium sensor for perceiving environmental signals. The CBL−CIPK system shows specificity and variety in its response to different stresses. Obtaining a deeper understanding of stress signaling and the responses will mitigate or solve crop yield crises in extreme environments with fast-growing populations.

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Section: Ionic Stress Signalingmentioning

confidence: 99%

Sensing of Abiotic Stress and Ionic Stress Responses in Plants

Zhang

Jahan

et al. 2018

IJMS

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“…SNRK was first identified in 1996 in 3T3-L1 adipocytes where its expression was observed during differentiation into an adipocyte-like cell [9] . SNRK is a monomeric enzyme containing a nuclear localization signal (NLS) domain, an ATP-binding domain, and an active S/T kinase domain with a conserved T-loop threonine residue (T173) [10] [ Figure 1]. Kinases that regulate SNRK activity have been identified.…”

Section: Introductionmentioning

confidence: 99%

SNRK: a metabolic regulator with multifaceted role in development and disease

Thirugnanam¹,

Ramchandran²

2020

Vessel Plus

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Sucrose nonfermenting 1-related kinase (SNRK) is a serine/threonine kinase and a member of the adenosine monophosphate (AMP)-activated protein kinase (AMPK) family that is involved in the metabolic regulatory mechanisms in various cell types. SNRK is an important mediator in maintaining cellular metabolic homeostasis. In this review, we discuss the role of SNRK in metabolic tissues where it is expressed, including heart and adipose tissue. We discuss its role in regulating inflammation in these tissues and the pathways associated with regulating inflammation. We also discuss SNRK's role in vascular development and the processes associated with it. Finally, we review SNRK's potential as a target in various metabolic dysfunction-associated diseases such as cardiovascular diseases, diabetes, obesity, and cancer. This comprehensive review on SNRK suggests that it has therapeutic value in the suppression of inflammation in cardiac and adipose tissue.

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“…2). The computational analyses suggest that KER-I folds and functions like an UBA-like domain by unknown mechanisms, likely maintaining the integrity of the kinase domain, as shown in the nonfermenting (Snf1)-related kinase (54).…”

Section: Discussionmentioning

confidence: 94%

Adaptation to Endoplasmic Reticulum Stress Requires Transphosphorylation within the Activation Loop of Protein Kinases Kin1 and Kin2, Orthologs of Human Microtubule Affinity-Regulating Kinase

Ghosh

Sathe

Paprocki

et al. 2018

Molecular and Cellular Biology

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Perturbations in endoplasmic reticulum (ER) homeostasis, a condition termed the "ER stress", activate the unfolded protein response (UPR), an intracellular network of signaling pathways. Recently, we have shown that protein kinase Kin1 and its paralog Kin2 in the budding yeast (orthologs of microtubule affinity-regulating kinase in humans) contribute to the UPR function. These Kin kinases contain a conserved kinase domain and an auto-inhibitory kinase-associated 1 (KA1) domain separated by a long undefined domain. Here, we show that Kin1 or Kin2 protein requires minimally a kinase domain and an adjacent kinase extension region (KER) for the UPR function. We also show that the functional mini Kin2 protein is predominantly visualized inside the cells and precipitated with the cellular membrane fraction, suggesting its association with the cellular endomembrane system. Furthermore, we show that trans-phosphorylation of the Kin1 residue T302 and the analogous Kin2 residue T281 within the activation loop are important for the full kinase activity. Collectively, our data suggest that, during the ER stress, the Kin kinase domain is released from its auto-inhibitory KA1 domain and is activated by trans-phosphorylation.

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Crystal structure of the kinase and UBA domains of SNRK reveals a distinct UBA binding mode in the AMPK family

Cited by 14 publications

References 31 publications

Sensing of Abiotic Stress and Ionic Stress Responses in Plants

Sensing of Abiotic Stress and Ionic Stress Responses in Plants

SNRK: a metabolic regulator with multifaceted role in development and disease

Adaptation to Endoplasmic Reticulum Stress Requires Transphosphorylation within the Activation Loop of Protein Kinases Kin1 and Kin2, Orthologs of Human Microtubule Affinity-Regulating Kinase

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