RapamycinFungusV1, Main, Exploration, bibRecord, 000A45

Phosphorylation of the amino-terminus of the AGC kinase Gad8 prevents its interaction with TORC2.

Identifieur interne : 000A45 ( Main/Exploration ); précédent : 000A44; suivant : 000A46

Phosphorylation of the amino-terminus of the AGC kinase Gad8 prevents its interaction with TORC2.

Auteurs : Wei Du [Royaume-Uni] ; Gabriella M. Forte [Royaume-Uni] ; Duncan Smith [Royaume-Uni] ; Janni Petersen [Australie]

Source :

Open biology [ 2046-2441 ] ; 2016.

RBID : pubmed:26935949

Descripteurs français

English descriptors

KwdEn :
- Actins (metabolism), Mechanistic Target of Rapamycin Complex 2 (MeSH), Multiprotein Complexes (metabolism), Phosphorylation (MeSH), Potassium (metabolism), Protein Binding (MeSH), Protein Interaction Maps (MeSH), Protein Kinase C (metabolism), Protein-Serine-Threonine Kinases (chemistry), Protein-Serine-Threonine Kinases (metabolism), Schizosaccharomyces (chemistry), Schizosaccharomyces (cytology), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (chemistry), Schizosaccharomyces pombe Proteins (metabolism), Stress, Physiological (MeSH), TOR Serine-Threonine Kinases (metabolism), Threonine (chemistry), Threonine (metabolism).
MESH :
- chemical , chemistry : Protein-Serine-Threonine Kinases, Schizosaccharomyces pombe Proteins, Threonine.
- chemical , metabolism : Actins, Multiprotein Complexes, Potassium, Protein Kinase C, Protein-Serine-Threonine Kinases, Schizosaccharomyces pombe Proteins, TOR Serine-Threonine Kinases, Threonine.
- chemical : Mechanistic Target of Rapamycin Complex 2.
- chemistry : Schizosaccharomyces.
- cytology : Schizosaccharomyces.
- metabolism : Schizosaccharomyces.
- Phosphorylation, Protein Binding, Protein Interaction Maps, Stress, Physiological.

Abstract

Cell proliferation, metabolism, migration and survival are coordinated through the tight control of two target of rapamycin (TOR) kinase complexes: TORC1 and TORC2. Here, we show that a novel phosphorylation of fission yeast Gad8 (AGC kinase) on the evolutionarily conserved threonine 6 (Thr6) prevents the physical association between Gad8 and TORC2. Accordingly, this block to protein interactions by Gad8 Thr6 phosphorylation decreases TORC2-controlled activation of Gad8. Likewise, phosphorylation of Gad8 Thr6, possibly by PKC, prevents the association of Gad8 with TORC2 thereby increasing TORC2 activity, because it reduces Gad8-mediated feedback inhibition of TORC2. Consistently, the introduction of a Gad8 T6D mutant, that mimics phosphorylation, increased TORC2 activity. Increased PKC(Pck2) expression prevented Gad8-TORC2 binding and so reduced the TORC2-mediated phosphorylation of Gad8 serine 546 that activates Gad8. Interestingly, independent of the Ser546 phosphorylation status, Gad8 Thr6 phosphorylation is important for remodelling the actin cytoskeleton and survival upon potassium ion and heat stresses. In contrast, Ser546 phosphorylation is required for the control of G1 arrest, mating, cell length at division and vascular size. Finally, these findings reveal a novel mode of TORC2 activation that is essential for cell survival following stress.

DOI: 10.1098/rsob.150189
PubMed: 26935949
PubMed Central: PMC4821236

Affiliations:

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

to stream Main, to step Corpus: 000A90
to stream Main, to step Curation: 000A90

Le document en format XML

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<term>Mechanistic Target of Rapamycin Complex 2 (MeSH)</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Potassium (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Interaction Maps (MeSH)</term>
<term>Protein Kinase C (metabolism)</term>
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<term>Protein-Serine-Threonine Kinases (metabolism)</term>
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<term>TOR Serine-Threonine Kinases (metabolism)</term>
<term>Threonine (chemistry)</term>
<term>Threonine (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Actines (métabolisme)</term>
<term>Cartes d'interactions protéiques (MeSH)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (MeSH)</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
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<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
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<term>Schizosaccharomyces (métabolisme)</term>
<term>Stress physiologique (MeSH)</term>
<term>Sérine-thréonine kinases TOR (métabolisme)</term>
<term>Thréonine (composition chimique)</term>
<term>Thréonine (métabolisme)</term>
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<term>Schizosaccharomyces pombe Proteins</term>
<term>Threonine</term>
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<term>Protein Kinase C</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Schizosaccharomyces pombe Proteins</term>
<term>TOR Serine-Threonine Kinases</term>
<term>Threonine</term>
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<term>Protéines de Schizosaccharomyces pombe</term>
<term>Schizosaccharomyces</term>
<term>Thréonine</term>
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<front><div type="abstract" xml:lang="en">Cell proliferation, metabolism, migration and survival are coordinated through the tight control of two target of rapamycin (TOR) kinase complexes: TORC1 and TORC2. Here, we show that a novel phosphorylation of fission yeast Gad8 (AGC kinase) on the evolutionarily conserved threonine 6 (Thr6) prevents the physical association between Gad8 and TORC2. Accordingly, this block to protein interactions by Gad8 Thr6 phosphorylation decreases TORC2-controlled activation of Gad8. Likewise, phosphorylation of Gad8 Thr6, possibly by PKC, prevents the association of Gad8 with TORC2 thereby increasing TORC2 activity, because it reduces Gad8-mediated feedback inhibition of TORC2. Consistently, the introduction of a Gad8 T6D mutant, that mimics phosphorylation, increased TORC2 activity. Increased PKC(Pck2) expression prevented Gad8-TORC2 binding and so reduced the TORC2-mediated phosphorylation of Gad8 serine 546 that activates Gad8. Interestingly, independent of the Ser546 phosphorylation status, Gad8 Thr6 phosphorylation is important for remodelling the actin cytoskeleton and survival upon potassium ion and heat stresses. In contrast, Ser546 phosphorylation is required for the control of G1 arrest, mating, cell length at division and vascular size. Finally, these findings reveal a novel mode of TORC2 activation that is essential for cell survival following stress. </div>
</front>
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<Abstract><AbstractText>Cell proliferation, metabolism, migration and survival are coordinated through the tight control of two target of rapamycin (TOR) kinase complexes: TORC1 and TORC2. Here, we show that a novel phosphorylation of fission yeast Gad8 (AGC kinase) on the evolutionarily conserved threonine 6 (Thr6) prevents the physical association between Gad8 and TORC2. Accordingly, this block to protein interactions by Gad8 Thr6 phosphorylation decreases TORC2-controlled activation of Gad8. Likewise, phosphorylation of Gad8 Thr6, possibly by PKC, prevents the association of Gad8 with TORC2 thereby increasing TORC2 activity, because it reduces Gad8-mediated feedback inhibition of TORC2. Consistently, the introduction of a Gad8 T6D mutant, that mimics phosphorylation, increased TORC2 activity. Increased PKC(Pck2) expression prevented Gad8-TORC2 binding and so reduced the TORC2-mediated phosphorylation of Gad8 serine 546 that activates Gad8. Interestingly, independent of the Ser546 phosphorylation status, Gad8 Thr6 phosphorylation is important for remodelling the actin cytoskeleton and survival upon potassium ion and heat stresses. In contrast, Ser546 phosphorylation is required for the control of G1 arrest, mating, cell length at division and vascular size. Finally, these findings reveal a novel mode of TORC2 activation that is essential for cell survival following stress. </AbstractText>
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Phosphorylation of the amino-terminus of the AGC kinase Gad8 prevents its interaction with TORC2.

Phosphorylation of the amino-terminus of the AGC kinase Gad8 prevents its interaction with TORC2.

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