About: Opposite Roles of RNase and Kinase Activities of Inositol-Requiring Enzyme 1 (IRE1) on HSV-1 Replication

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About: Opposite Roles of RNase and Kinase Activities of Inositol-Requiring Enzyme 1 (IRE1) on HSV-1 Replication Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Opposite Roles of RNase and Kinase Activities of Inositol-Requiring Enzyme 1 (IRE1) on HSV-1 Replication
Creator	Wu, Zhiwei Wang, Xiaohui Chen, Deyan Wang, Huanru Li, Yanlei Su, Airong
source	Medline; PMC
abstract	In response to the endoplasmic reticulum (ER) stress induced by herpes simplex virus type 1 (HSV-1) infection, host cells activate the unfolded protein response (UPR) to reduce the protein-folding burden in the ER. The regulation of UPR upon HSV-1 infection is complex, and the downstream effectors can be detrimental to viral replication. Therefore, HSV-1 copes with the UPR to create a beneficial environment for its replication. UPR has three branches, including protein kinase RNA (PKR)-like ER kinase (PERK), inositol-requiring enzyme 1 (IRE1), and activated transcription factor 6 (ATF6). IRE1α is the most conserved branch of UPR which has both RNase and kinase activities. Previous studies have shown that IRE1α RNase activity was inactivated during HSV-1 infection. However, the effect of the two activities of IRE1α on HSV-1 replication remains unknown. Results in this study showed that IRE1α expression was up-regulated during HSV-1 infection. We found that in HEC-1-A cells, increasing RNase activity, or inhibiting kinase activity of IRE1α led to viral suppression, indicating that the kinase activity of IRE1α was beneficial, while the RNase activity was detrimental to viral replication. Further evidence showed that the kinase activity of IRE1α leads to the activation of the JNK (c-Jun N-terminal kinases) pathway, which enhances viral replication. Taken together, our evidence suggests that IRE1α is involved in HSV-1 replication, and its RNase and kinase activities play differential roles during viral infection.
has issue date	2017-08-23(xsd:dateTime)
bibo:doi	10.3390/v9090235
bibo:pmid	28832521
has license	cc-by
sha1sum (hex)	aeb63d391feee1b548adf8d5a208d70c3ee5c802
schema:url	https://doi.org/10.3390/v9090235
resource representing a document's title	Opposite Roles of RNase and Kinase Activities of Inositol-Requiring Enzyme 1 (IRE1) on HSV-1 Replication
has PubMed Central identifier	PMC5618002
has PubMed identifier	28832521
schema:publication	Viruses
resource representing a document's body	covid:aeb63d391feee1b548adf8d5a208d70c3ee5c802#body_text
is schema:about of	named entity 'JUN' named entity 'INCREASING' named entity 'ACTIVITIES' named entity 'INACTIVATED' named entity 'PREVIOUS' named entity 'IRE1' named entity 'DOWNSTREAM' named entity 'KINASE ACTIVITY' named entity 'INFECTION' named entity 'FOUND' named entity 'DIFFERENTIAL' named entity 'HOST CELLS' named entity 'RNASE ACTIVITY' named entity 'LIKE' named entity 'ENVIRONMENT' named entity 'UNFOLDED PROTEIN RESPONSE' named entity 'RESPONSE TO' named entity 'RNASE' named entity 'KINASE' named entity 'INOSITOL-REQUIRING ENZYME 1' named entity 'ACTIVATE' named entity 'KINASES' named entity 'BRANCHES' named entity 'COMPLEX' named entity 'EFFECT' named entity 'PROTEIN KINASE' named entity 'INDUCED' named entity 'OUR' named entity 'HEC-1-A' named entity 'PATHWAY' named entity 'UNKNOWN' named entity 'TAKEN' named entity 'EXPRESSION' named entity 'PLAY' named entity 'HSV-1' named entity 'REPLICATION' covid:arg/aeb63d391feee1b548adf8d5a208d70c3ee5c802 named entity 'ROLES' named entity 'OPPOSITE' named entity 'HERPES SIMPLEX VIRUS TYPE 1' named entity 'INCLUDING' named entity 'N-TERMINAL ' named entity 'ACTIVATION' named entity 'INOSITOL-REQUIRING ENZYME 1' named entity 'VIRAL SUPPRESSION' named entity 'CONSERVED' named entity 'COPES' named entity 'PROTEIN-FOLDING' named entity 'BURDEN' named entity 'BRANCH OF' named entity 'RNA' named entity 'CREATE' named entity 'CELLS' named entity 'STUDIES' named entity 'INVOLVED' named entity 'UP-REGULATED' named entity 'KINASE' named entity 'ACTIVITIES' named entity 'HSV-1' named entity 'RNASE' named entity 'INHIBITING' named entity 'JNK' named entity 'TO REDUCE' named entity 'BENEFICIAL' named entity 'HSV-1 INFECTION' named entity 'INDICATING' named entity 'ENDOPLASMIC RETICULUM' named entity 'LED' named entity 'VIRAL INFECTION' named entity 'ITS' named entity 'REPLICATION' named entity 'STRESS' named entity 'TRANSCRIPTION FACTOR 6' named entity 'VIRAL REPLICATION' named entity 'EVIDENCE' named entity 'REGULATION'

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