Viroporin-mediated calcium-activated autophagy

Crawford, Sue E.; Estes, Mary K.

doi:10.4161/auto.23959

Cited by 49 publications

(52 citation statements)

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“…Further study found that NSP4 activates the release of calcium from the ER into the cytoplasm, inducing calcium/calmodulindependent kinase kinase-β (CaMKK-β) signaling to trigger autophagy ( Fig. 5.3) [28,29]. Besides CaMKK-β signaling, a mutually complementary mechanism about a new small RNA was found in RV-initiated autophagy.…”

Section: Dsrna Virusesmentioning

confidence: 97%

Autophagy and Viral Infection

Mao

Lin

et al. 2019

Advances in Experimental Medicine and Biology

112

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Autophagy is an intracellular recycling process that maintains cellular homeostasis by orchestrating immunity upon viral infection. Following viral infection, autophagy is often initiated to curtail infection by delivering viral particles for lysosomal degradation and further integrating with innate pattern recognition receptor signaling to induce interferon (IFN)-mediated viral clearance. However, some viruses have evolved anti-autophagy strategies to escape host immunity and to promote viral replication. In this chapter, we illustrate how autophagy prevents viral infection to generate an optimal anti-viral milieu, and then concentrate on how viruses subvert and hijack the autophagic process to evade immunosurveillance, thereby facilitating viral replication and pathogenesis. Understanding the interplays between autophagy and viral infection is anticipated to guide the development of effective anti-viral therapeutics to fight against infectious diseases.

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Section: Dsrna Virusesmentioning

confidence: 97%

Autophagy and Viral Infection

Mao

Lin

et al. 2019

Advances in Experimental Medicine and Biology

112

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“…CaM was originally identified in snake venom as an activator of cyclic nucleotide phosphodiesterase (PDE) [57] and subsequently shown to require [59] and bind Ca 2+ [60]. Shortly thereafter, the protein was independently “discovered” by several investigators working on different biological systems and given different names.…”

Section: A Key Ca2+/cam-dependent Kinase Cascade Emergesmentioning

confidence: 99%

“…Determining the subcellular localization of the active versus inactive forms of this kinase, in basal versus stimulated states, will shed light on unappreciated functions of CaMKK2. Various studies implicate CaMKK2 activity with phagocytosis [37], secretion [52], and autophagy [57], which involve trafficking of membrane-associated and soluble proteins. Whether CaMKK2 is tethered to any intracellular membranes and what mechanisms are in place to regulate its trafficking within the cell are important questions that warrant further investigation.…”

Section: Concluding Remarks and Future Perspectivesmentioning

confidence: 99%

The Ca 2+ /Calmodulin/CaMKK2 Axis: Nature's Metabolic CaMshaft

Marcelo

Means

York

2016

Trends in Endocrinology & Metabolism

176

142

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Calcium (Ca2+) is an essential ligand that binds its primary intracellular receptor Calmodulin (CaM) to trigger a variety of downstream processes and pathways. Central to the actions of Ca2+/CaM is the activation of a highly conserved Ca2+/CaM kinase (CaMK) cascade, which amplifies Ca2+ signals through a series of subsequent phosphorylation events. Proper regulation of Ca2+ flux is necessary for whole-body metabolism and disruption of Ca2+ homeostasis has been linked to a variety of metabolic diseases. Herein, we provide a synthesis of recent advances that highlight the roles of the Ca2+/CaM kinase axis in key metabolic tissues. An appreciation of this information is critical in order to understand the mechanisms by which Ca2+/CaM-dependent signaling contributes to metabolic homeostasis and disease.

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“…ER is closely associated with autophagy, since ER is proposed to be the potential membrane source of autophagosomes, 14 and provides calcium signaling for autophagy induction. 15,16 Moreover, a variety of studies indicates that autophagy compensates for disposal of accumulated proteins result from ER stress, [17][18][19] suggesting that ER stress may be a trigger for autophagy induction. In the context of cerebral ischemia, the role of autophagy is under debate.…”

Section: Introductionmentioning

confidence: 99%

Endoplasmic reticulum stress induced by tunicamycin and thapsigargin protects against transient ischemic brain injury

Zhang¹,

et al. 2014

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Transient cerebral ischemia leads to endoplasmic reticulum (ER) stress. However, the contributions of ER stress to cerebral ischemia are not clear. To address this issue, the ER stress activators tunicamycin (TM) and thapsigargin (TG) were administered to transient middle cerebral artery occluded (tMCAO) mice and oxygen-glucose deprivation-reperfusion (OGD-Rep.)-treated neurons. Both TM and TG showed significant protection against ischemia-induced brain injury, as revealed by reduced brain infarct volume and increased glucose uptake rate in ischemic tissue. In OGD-Rep.-treated neurons, 4-PBA, the ER stress releasing mechanism, counteracted the neuronal protection of TM and TG, which also supports a protective role of ER stress in transient brain ischemia. Knocking down the ER stress sensor Eif2s1, which is further activated by TM and TG, reduced the OGD-Rep.-induced neuronal cell death. In addition, both TM and TG prevented PARK2 loss, promoted its recruitment to mitochondria, and activated mitophagy during reperfusion after ischemia. The neuroprotection of TM and TG was reversed by autophagy inhibition (3-methyladenine and Atg7 knockdown) as well as Park2 silencing. The neuroprotection was also diminished in Park2(+/-) mice. Moreover, Eif2s1 and downstream Atf4 silencing reduced PARK2 expression, impaired mitophagy induction, and counteracted the neuroprotection. Taken together, the present investigation demonstrates that the ER stress induced by TM and TG protects against the transient ischemic brain injury. The PARK2-mediated mitophagy may be underlying the protection of ER stress. These findings may provide a new strategy to rescue ischemic brains by inducing mitophagy through ER stress activation.

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Viroporin-mediated calcium-activated autophagy

Abstract: hijacked through viroporinactivated calcium/calmodulin-dependent kinase kinase-β signaling is required for rotavirus replication.

Cited by 49 publications

References 0 publications

Autophagy and Viral Infection

Autophagy and Viral Infection

The Ca 2+ /Calmodulin/CaMKK2 Axis: Nature's Metabolic CaMshaft

Endoplasmic reticulum stress induced by tunicamycin and thapsigargin protects against transient ischemic brain injury

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