RapamycinFungusV1, Main, Exploration, bibRecord, 000A43

Porcine Circovirus Type 2 Activates CaMMKβ to Initiate Autophagy in PK-15 Cells by Increasing Cytosolic Calcium.

Identifieur interne : 000A43 ( Main/Exploration ); précédent : 000A42; suivant : 000A44

Porcine Circovirus Type 2 Activates CaMMKβ to Initiate Autophagy in PK-15 Cells by Increasing Cytosolic Calcium.

Auteurs : Yuanxing Gu [République populaire de Chine] ; Baozhu Qi [République populaire de Chine] ; Yingshan Zhou [République populaire de Chine] ; Xiaowu Jiang [République populaire de Chine] ; Xian Zhang [République populaire de Chine] ; Xiaoliang Li [République populaire de Chine] ; Weihuan Fang [République populaire de Chine]

Source :

Viruses [ 1999-4915 ] ; 2016.

RBID : pubmed:27213427

Descripteurs français

KwdFr :
- AMP-Activated Protein Kinases (métabolisme), Animaux (MeSH), Autophagie (MeSH), Calcium (métabolisme), Calcium-Calmodulin-Dependent Protein Kinase Kinase (métabolisme), Calcium-Calmodulin-Dependent Protein Kinase Type 1 (métabolisme), Cellules épithéliales (physiologie), Cellules épithéliales (virologie), Circovirus (pathogénicité), Interactions hôte-pathogène (MeSH), Lignée cellulaire (MeSH), Récepteurs à l'inositol 1,4,5-triphosphate (métabolisme), Signalisation calcique (MeSH), Suidae (MeSH).
MESH :
- métabolisme : AMP-Activated Protein Kinases, Calcium, Calcium-Calmodulin-Dependent Protein Kinase Kinase, Calcium-Calmodulin-Dependent Protein Kinase Type 1, Récepteurs à l'inositol 1,4,5-triphosphate.
- pathogénicité : Circovirus.
- physiologie : Cellules épithéliales.
- virologie : Cellules épithéliales.
- Animaux, Autophagie, Interactions hôte-pathogène, Lignée cellulaire, Signalisation calcique, Suidae.

English descriptors

KwdEn :
- AMP-Activated Protein Kinases (metabolism), Animals (MeSH), Autophagy (MeSH), Calcium (metabolism), Calcium Signaling (MeSH), Calcium-Calmodulin-Dependent Protein Kinase Kinase (metabolism), Calcium-Calmodulin-Dependent Protein Kinase Type 1 (metabolism), Cell Line (MeSH), Circovirus (pathogenicity), Epithelial Cells (physiology), Epithelial Cells (virology), Host-Pathogen Interactions (MeSH), Inositol 1,4,5-Trisphosphate Receptors (metabolism), Swine (MeSH).
MESH :
- chemical , metabolism : AMP-Activated Protein Kinases, Calcium, Calcium-Calmodulin-Dependent Protein Kinase Kinase, Calcium-Calmodulin-Dependent Protein Kinase Type 1, Inositol 1,4,5-Trisphosphate Receptors.
- pathogenicity : Circovirus.
- physiology : Epithelial Cells.
- virology : Epithelial Cells.
- Animals, Autophagy, Calcium Signaling, Cell Line, Host-Pathogen Interactions, Swine.

Abstract

Porcine circovirus type 2 (PCV2) induces autophagy via the 5' adenosine monophosphate-activated protein kinase (AMPK)/extracellular signal-regulated kinase (ERK)/tuberous sclerosis complex 2 (TSC2)/mammalian target of rapamycin (mTOR) pathway in pig kidney PK-15 cells. However, the underlying mechanisms of AMPK activation in autophagy induction remain unknown. With specific inhibitors and RNA interference (RNAi), we show that PCV2 infection upregulated calcium/calmodulin-dependent protein kinase kinase-beta (CaMKKβ) by increasing cytosolic Ca(2+) via inositol 1,4,5-trisphosphate receptor (IP3R). Elevation of cytosolic calcium ion (Ca(2+)) did not seem to involve inositol 1,4,5-trisphosphate (IP3) release from phosphatidylinositol 4,5-bisphosphate (PIP2) by phosphoinositide phospholipase C-gamma (PLC-γ). CaMKKβ then activated both AMPK and calcium/calmodulin-dependent protein kinase I (CaMKI). PCV2 employed CaMKI and Trp-Asp (WD) repeat domain phosphoinositide-interacting protein 1 (WIPI1) as another pathway additional to AMPK signaling in autophagy initiation. Our findings could help better understanding of the signaling pathways of autophagy induction as part of PCV2 pathogenesis. Further research is warranted to study if PCV2 interacts directly with IP3R or indirectly with the molecules that antagonize IP3R activity responsible for increased cytosolic Ca(2+) both in PK-15 cells and PCV2-targeted primary cells from pigs.

DOI: 10.3390/v8050135
PubMed: 27213427
PubMed Central: PMC4885090

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000A46
to stream Main, to step Curation: 000A46

Le document en format XML

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<term>Animals (MeSH)</term>
<term>Autophagy (MeSH)</term>
<term>Calcium (metabolism)</term>
<term>Calcium Signaling (MeSH)</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Kinase (metabolism)</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Type 1 (metabolism)</term>
<term>Cell Line (MeSH)</term>
<term>Circovirus (pathogenicity)</term>
<term>Epithelial Cells (physiology)</term>
<term>Epithelial Cells (virology)</term>
<term>Host-Pathogen Interactions (MeSH)</term>
<term>Inositol 1,4,5-Trisphosphate Receptors (metabolism)</term>
<term>Swine (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>AMP-Activated Protein Kinases (métabolisme)</term>
<term>Animaux (MeSH)</term>
<term>Autophagie (MeSH)</term>
<term>Calcium (métabolisme)</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Kinase (métabolisme)</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Type 1 (métabolisme)</term>
<term>Cellules épithéliales (physiologie)</term>
<term>Cellules épithéliales (virologie)</term>
<term>Circovirus (pathogénicité)</term>
<term>Interactions hôte-pathogène (MeSH)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Récepteurs à l'inositol 1,4,5-triphosphate (métabolisme)</term>
<term>Signalisation calcique (MeSH)</term>
<term>Suidae (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>AMP-Activated Protein Kinases</term>
<term>Calcium</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Kinase</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Type 1</term>
<term>Inositol 1,4,5-Trisphosphate Receptors</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>AMP-Activated Protein Kinases</term>
<term>Calcium</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Kinase</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Type 1</term>
<term>Récepteurs à l'inositol 1,4,5-triphosphate</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Circovirus</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Circovirus</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cellules épithéliales</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Epithelial Cells</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Cellules épithéliales</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Epithelial Cells</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Autophagy</term>
<term>Calcium Signaling</term>
<term>Cell Line</term>
<term>Host-Pathogen Interactions</term>
<term>Swine</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Autophagie</term>
<term>Interactions hôte-pathogène</term>
<term>Lignée cellulaire</term>
<term>Signalisation calcique</term>
<term>Suidae</term>
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<front><div type="abstract" xml:lang="en">Porcine circovirus type 2 (PCV2) induces autophagy via the 5' adenosine monophosphate-activated protein kinase (AMPK)/extracellular signal-regulated kinase (ERK)/tuberous sclerosis complex 2 (TSC2)/mammalian target of rapamycin (mTOR) pathway in pig kidney PK-15 cells. However, the underlying mechanisms of AMPK activation in autophagy induction remain unknown. With specific inhibitors and RNA interference (RNAi), we show that PCV2 infection upregulated calcium/calmodulin-dependent protein kinase kinase-beta (CaMKKβ) by increasing cytosolic Ca(2+) via inositol 1,4,5-trisphosphate receptor (IP3R). Elevation of cytosolic calcium ion (Ca(2+)) did not seem to involve inositol 1,4,5-trisphosphate (IP3) release from phosphatidylinositol 4,5-bisphosphate (PIP2) by phosphoinositide phospholipase C-gamma (PLC-γ). CaMKKβ then activated both AMPK and calcium/calmodulin-dependent protein kinase I (CaMKI). PCV2 employed CaMKI and Trp-Asp (WD) repeat domain phosphoinositide-interacting protein 1 (WIPI1) as another pathway additional to AMPK signaling in autophagy initiation. Our findings could help better understanding of the signaling pathways of autophagy induction as part of PCV2 pathogenesis. Further research is warranted to study if PCV2 interacts directly with IP3R or indirectly with the molecules that antagonize IP3R activity responsible for increased cytosolic Ca(2+) both in PK-15 cells and PCV2-targeted primary cells from pigs.</div>
</front>
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<DateCompleted><Year>2017</Year>
<Month>09</Month>
<Day>20</Day>
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<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<Title>Viruses</Title>
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<Abstract><AbstractText>Porcine circovirus type 2 (PCV2) induces autophagy via the 5' adenosine monophosphate-activated protein kinase (AMPK)/extracellular signal-regulated kinase (ERK)/tuberous sclerosis complex 2 (TSC2)/mammalian target of rapamycin (mTOR) pathway in pig kidney PK-15 cells. However, the underlying mechanisms of AMPK activation in autophagy induction remain unknown. With specific inhibitors and RNA interference (RNAi), we show that PCV2 infection upregulated calcium/calmodulin-dependent protein kinase kinase-beta (CaMKKβ) by increasing cytosolic Ca(2+) via inositol 1,4,5-trisphosphate receptor (IP3R). Elevation of cytosolic calcium ion (Ca(2+)) did not seem to involve inositol 1,4,5-trisphosphate (IP3) release from phosphatidylinositol 4,5-bisphosphate (PIP2) by phosphoinositide phospholipase C-gamma (PLC-γ). CaMKKβ then activated both AMPK and calcium/calmodulin-dependent protein kinase I (CaMKI). PCV2 employed CaMKI and Trp-Asp (WD) repeat domain phosphoinositide-interacting protein 1 (WIPI1) as another pathway additional to AMPK signaling in autophagy initiation. Our findings could help better understanding of the signaling pathways of autophagy induction as part of PCV2 pathogenesis. Further research is warranted to study if PCV2 interacts directly with IP3R or indirectly with the molecules that antagonize IP3R activity responsible for increased cytosolic Ca(2+) both in PK-15 cells and PCV2-targeted primary cells from pigs.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gu</LastName>
<ForeName>Yuanxing</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, China. guzi.123@163.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Qi</LastName>
<ForeName>Baozhu</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, China. qibaozhu@yeah.net.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhou</LastName>
<ForeName>Yingshan</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, China. yszhou@zju.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jiang</LastName>
<ForeName>Xiaowu</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, China. cqrcxwj@163.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Xian</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, China. zhangxian073@163.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Xiaoliang</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, China. xlli@zju.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fang</LastName>
<ForeName>Weihuan</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, China. whfang@zju.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>05</Month>
<Day>20</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Switzerland</Country>
<MedlineTA>Viruses</MedlineTA>
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<MeshHeading><DescriptorName UI="D020013" MajorTopicYN="Y">Calcium Signaling</DescriptorName>
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<MeshHeading><DescriptorName UI="D054737" MajorTopicYN="N">Calcium-Calmodulin-Dependent Protein Kinase Kinase</DescriptorName>
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<MeshHeading><DescriptorName UI="D054729" MajorTopicYN="N">Calcium-Calmodulin-Dependent Protein Kinase Type 1</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017925" MajorTopicYN="N">Circovirus</DescriptorName>
<QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004847" MajorTopicYN="N">Epithelial Cells</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
<QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054884" MajorTopicYN="Y">Host-Pathogen Interactions</DescriptorName>
</MeshHeading>
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<MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName>
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	Serveur d'exploration sur la rapamycine et les champignons
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Porcine Circovirus Type 2 Activates CaMMKβ to Initiate Autophagy in PK-15 Cells by Increasing Cytosolic Calcium.

Porcine Circovirus Type 2 Activates CaMMKβ to Initiate Autophagy in PK-15 Cells by Increasing Cytosolic Calcium.

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