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TORC2-Gad8-dependent myosin phosphorylation modulates regulation by calcium.

Identifieur interne : 000213 ( Main/Exploration ); précédent : 000212; suivant : 000214

TORC2-Gad8-dependent myosin phosphorylation modulates regulation by calcium.

Auteurs : Karen Baker [Royaume-Uni] ; Irene A. Gyamfi [Royaume-Uni] ; Gregory I. Mashanov [Royaume-Uni] ; Justin E. Molloy [Royaume-Uni] ; Michael A. Geeves [Royaume-Uni] ; Daniel P. Mulvihill [Royaume-Uni]

Source :

RBID : pubmed:31566560

Descripteurs français

English descriptors

Abstract

Cells respond to changes in their environment through signaling networks that modulate cytoskeleton and membrane organization to coordinate cell-cycle progression, polarized cell growth and multicellular development. Here, we define a novel regulatory mechanism by which the motor activity and function of the fission yeast type one myosin, Myo1, is modulated by TORC2-signalling-dependent phosphorylation. Phosphorylation of the conserved serine at position 742 (S742) within the neck region changes both the conformation of the neck region and the interactions between Myo1 and its associating calmodulin light chains. S742 phosphorylation thereby couples the calcium and TOR signaling networks that are involved in the modulation of myosin-1 dynamics to co-ordinate actin polymerization and membrane reorganization at sites of endocytosis and polarised cell growth in response to environmental and cell-cycle cues.

DOI: 10.7554/eLife.51150
PubMed: 31566560
PubMed Central: PMC6802964


Affiliations:


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


Le document en format XML

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<term>Mechanistic Target of Rapamycin Complex 2 (metabolism)</term>
<term>Myosin Heavy Chains (chemistry)</term>
<term>Myosin Heavy Chains (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
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<term>Protein-Serine-Threonine Kinases (metabolism)</term>
<term>Schizosaccharomyces (physiology)</term>
<term>Schizosaccharomyces pombe Proteins (chemistry)</term>
<term>Schizosaccharomyces pombe Proteins (metabolism)</term>
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<term>Adaptation physiologique (MeSH)</term>
<term>Calcium (métabolisme)</term>
<term>Chaînes lourdes de myosine (composition chimique)</term>
<term>Chaînes lourdes de myosine (métabolisme)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
<term>Protéines de Schizosaccharomyces pombe (composition chimique)</term>
<term>Protéines de Schizosaccharomyces pombe (métabolisme)</term>
<term>Schizosaccharomyces (physiologie)</term>
<term>Transduction du signal (MeSH)</term>
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<term>Myosin Heavy Chains</term>
<term>Schizosaccharomyces pombe Proteins</term>
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<term>Calcium</term>
<term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Myosin Heavy Chains</term>
<term>Protein-Serine-Threonine Kinases</term>
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<term>Chaînes lourdes de myosine</term>
<term>Protéines de Schizosaccharomyces pombe</term>
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<term>Calcium</term>
<term>Chaînes lourdes de myosine</term>
<term>Complexe-2 cible mécanistique de la rapamycine</term>
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<term>Protéines de Schizosaccharomyces pombe</term>
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<term>Conformation des protéines</term>
<term>Maturation post-traductionnelle des protéines</term>
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<div type="abstract" xml:lang="en">Cells respond to changes in their environment through signaling networks that modulate cytoskeleton and membrane organization to coordinate cell-cycle progression, polarized cell growth and multicellular development. Here, we define a novel regulatory mechanism by which the motor activity and function of the fission yeast type one myosin, Myo1, is modulated by TORC2-signalling-dependent phosphorylation. Phosphorylation of the conserved serine at position 742 (S742) within the neck region changes both the conformation of the neck region and the interactions between Myo1 and its associating calmodulin light chains. S742 phosphorylation thereby couples the calcium and TOR signaling networks that are involved in the modulation of myosin-1 dynamics to co-ordinate actin polymerization and membrane reorganization at sites of endocytosis and polarised cell growth in response to environmental and cell-cycle cues.</div>
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