RapamycinFungusV1, Main, Exploration, bibRecord, 001359

A herpesvirus kinase that masquerades as Akt: you don't have to look like Akt, to act like it.

Identifieur interne : 001359 ( Main/Exploration ); précédent : 001358; suivant : 001360

A herpesvirus kinase that masquerades as Akt: you don't have to look like Akt, to act like it.

Auteurs : Uyanga Chuluunbaatar [États-Unis] ; Ian Mohr

Source :

Cell cycle (Georgetown, Tex.) [ 1551-4005 ] ; 2011.

RBID : pubmed:21606676

Descripteurs français

KwdFr :
- Biosynthèse des protéines (MeSH), Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (MeSH), Facteurs d'initiation eucaryotes (métabolisme), Herpesviridae (enzymologie), Herpesviridae (physiologie), Humains (MeSH), Phosphoprotéines (métabolisme), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéine-2 du complexe de la sclérose tubéreuse (MeSH), Protéines (métabolisme), Protéines adaptatrices de la transduction du signal (métabolisme), Protéines proto-oncogènes c-akt (génétique), Protéines proto-oncogènes c-akt (métabolisme), Protéines suppresseurs de tumeurs (métabolisme), Protéines virales (génétique), Protéines virales (métabolisme), Sérine-thréonine kinases TOR (métabolisme), Transduction du signal (génétique).
MESH :
- enzymologie : Herpesviridae.
- génétique : Protein-Serine-Threonine Kinases, Protéines proto-oncogènes c-akt, Protéines virales, Transduction du signal.
- métabolisme : Facteurs d'initiation eucaryotes, Phosphoprotéines, Protein-Serine-Threonine Kinases, Protéines, Protéines adaptatrices de la transduction du signal, Protéines proto-oncogènes c-akt, Protéines suppresseurs de tumeurs, Protéines virales, Sérine-thréonine kinases TOR.
- physiologie : Herpesviridae.
- Biosynthèse des protéines, Complexe-1 cible mécanistique de la rapamycine, Complexes multiprotéiques, Humains, Protéine-2 du complexe de la sclérose tubéreuse.

English descriptors

KwdEn :
- Adaptor Proteins, Signal Transducing (metabolism), Eukaryotic Initiation Factors (metabolism), Herpesviridae (enzymology), Herpesviridae (physiology), Humans (MeSH), Mechanistic Target of Rapamycin Complex 1 (MeSH), Multiprotein Complexes (MeSH), Phosphoproteins (metabolism), Protein Biosynthesis (MeSH), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Proteins (metabolism), Proto-Oncogene Proteins c-akt (genetics), Proto-Oncogene Proteins c-akt (metabolism), Signal Transduction (genetics), TOR Serine-Threonine Kinases (metabolism), Tuberous Sclerosis Complex 2 Protein (MeSH), Tumor Suppressor Proteins (metabolism), Viral Proteins (genetics), Viral Proteins (metabolism).
MESH :
- chemical , genetics : Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins c-akt, Viral Proteins.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, Eukaryotic Initiation Factors, Phosphoproteins, Protein-Serine-Threonine Kinases, Proteins, Proto-Oncogene Proteins c-akt, TOR Serine-Threonine Kinases, Tumor Suppressor Proteins, Viral Proteins.
- enzymology : Herpesviridae.
- genetics : Signal Transduction.
- physiology : Herpesviridae.
- Humans, Mechanistic Target of Rapamycin Complex 1, Multiprotein Complexes, Protein Biosynthesis, Tuberous Sclerosis Complex 2 Protein.

Abstract

The cellular protein synthesis machinery is tightly regulated and capable of rapid reaction to a variety of physiological inputs critical in stress-response, cell cycle control, cancer biology, and virus infection. One important strategy for stimulating protein synthesis involves the ser/thr kinase Akt, which subsequently triggers inactivation of the cap-dependent translational repressor 4E-BP1 by an mTOR-containing protein complex (mTORC1). A recent paper demonstrated that herpes simplex virus utilizes a remarkable tactic to activate mTOR in infected cells. Instead of using the cellular Akt, the virus produces a ser / thr kinase called Us3 that doesn't look like Akt, but masquerades as Akt. By making the Akt-like protein unrecognizable, this disguise allows it to bypass the strict limits normally imposed on the real cellular Akt. Importantly, preventing the virus Akt-imposter from triggering mTORC1 inhibited viral growth, suggesting a new way to block herpes simplex virus. This study also raises the possibility that other Akt-impersonators may lurk hidden in our own genomes, possibly contributing to diseases ranging from diabetes to cancer.

DOI: 10.4161/cc.10.13.16242
PubMed: 21606676
PubMed Central: PMC3154360

Affiliations:

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

to stream Main, to step Corpus: 001292
to stream Main, to step Curation: 001292

Le document en format XML

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<front><div type="abstract" xml:lang="en">The cellular protein synthesis machinery is tightly regulated and capable of rapid reaction to a variety of physiological inputs critical in stress-response, cell cycle control, cancer biology, and virus infection. One important strategy for stimulating protein synthesis involves the ser/thr kinase Akt, which subsequently triggers inactivation of the cap-dependent translational repressor 4E-BP1 by an mTOR-containing protein complex (mTORC1). A recent paper demonstrated that herpes simplex virus utilizes a remarkable tactic to activate mTOR in infected cells. Instead of using the cellular Akt, the virus produces a ser / thr kinase called Us3 that doesn't look like Akt, but masquerades as Akt. By making the Akt-like protein unrecognizable, this disguise allows it to bypass the strict limits normally imposed on the real cellular Akt. Importantly, preventing the virus Akt-imposter from triggering mTORC1 inhibited viral growth, suggesting a new way to block herpes simplex virus. This study also raises the possibility that other Akt-impersonators may lurk hidden in our own genomes, possibly contributing to diseases ranging from diabetes to cancer.</div>
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<Abstract><AbstractText>The cellular protein synthesis machinery is tightly regulated and capable of rapid reaction to a variety of physiological inputs critical in stress-response, cell cycle control, cancer biology, and virus infection. One important strategy for stimulating protein synthesis involves the ser/thr kinase Akt, which subsequently triggers inactivation of the cap-dependent translational repressor 4E-BP1 by an mTOR-containing protein complex (mTORC1). A recent paper demonstrated that herpes simplex virus utilizes a remarkable tactic to activate mTOR in infected cells. Instead of using the cellular Akt, the virus produces a ser / thr kinase called Us3 that doesn't look like Akt, but masquerades as Akt. By making the Akt-like protein unrecognizable, this disguise allows it to bypass the strict limits normally imposed on the real cellular Akt. Importantly, preventing the virus Akt-imposter from triggering mTORC1 inhibited viral growth, suggesting a new way to block herpes simplex virus. This study also raises the possibility that other Akt-impersonators may lurk hidden in our own genomes, possibly contributing to diseases ranging from diabetes to cancer.</AbstractText>
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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

A herpesvirus kinase that masquerades as Akt: you don't have to look like Akt, to act like it.

A herpesvirus kinase that masquerades as Akt: you don't have to look like Akt, to act like it.

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