RapamycinFungusV1, Main, Exploration, bibRecord, 000C19

Significance of filamin A in mTORC2 function in glioblastoma.

Identifieur interne : 000C19 ( Main/Exploration ); précédent : 000C18; suivant : 000C20

Significance of filamin A in mTORC2 function in glioblastoma.

Auteurs : Naphat Chantaravisoot [États-Unis] ; Piriya Wongkongkathep [États-Unis] ; Joseph A. Loo [États-Unis] ; Paul S. Mischel [États-Unis] ; Fuyuhiko Tamanoi [États-Unis]

Source :

Molecular cancer [ 1476-4598 ] ; 2015.

RBID : pubmed:26134617

Descripteurs français

KwdFr :
- Activation enzymatique (effets des médicaments et des substances chimiques), Adhérence cellulaire (effets des médicaments et des substances chimiques), Compagnon de mTOR insensible à la rapamycine (MeSH), Complexe-2 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (antagonistes et inhibiteurs), Complexes multiprotéiques (métabolisme), Cytosquelette d'actine (métabolisme), Filamines (métabolisme), Glioblastome (anatomopathologie), Glioblastome (métabolisme), Humains (MeSH), Indoles (pharmacologie), Liaison aux protéines (MeSH), Lignée cellulaire tumorale (MeSH), Mouvement cellulaire (effets des médicaments et des substances chimiques), Phosphorylation (MeSH), Protéines de transport (métabolisme), Purines (pharmacologie), Sérine-thréonine kinases TOR (antagonistes et inhibiteurs), Sérine-thréonine kinases TOR (métabolisme).
MESH :
- anatomopathologie : Glioblastome.
- antagonistes et inhibiteurs : Complexes multiprotéiques, Sérine-thréonine kinases TOR.
- effets des médicaments et des substances chimiques : Activation enzymatique, Adhérence cellulaire, Mouvement cellulaire.
- métabolisme : Complexes multiprotéiques, Cytosquelette d'actine, Filamines, Glioblastome, Protéines de transport, Sérine-thréonine kinases TOR.
- pharmacologie : Indoles, Purines.
- Compagnon de mTOR insensible à la rapamycine, Complexe-2 cible mécanistique de la rapamycine, Humains, Liaison aux protéines, Lignée cellulaire tumorale, Phosphorylation.

English descriptors

KwdEn :
- Actin Cytoskeleton (metabolism), Carrier Proteins (metabolism), Cell Adhesion (drug effects), Cell Line, Tumor (MeSH), Cell Movement (drug effects), Enzyme Activation (drug effects), Filamins (metabolism), Glioblastoma (metabolism), Glioblastoma (pathology), Humans (MeSH), Indoles (pharmacology), Mechanistic Target of Rapamycin Complex 2 (MeSH), Multiprotein Complexes (antagonists & inhibitors), Multiprotein Complexes (metabolism), Phosphorylation (MeSH), Protein Binding (MeSH), Purines (pharmacology), Rapamycin-Insensitive Companion of mTOR Protein (MeSH), TOR Serine-Threonine Kinases (antagonists & inhibitors), TOR Serine-Threonine Kinases (metabolism).
MESH :
- chemical , antagonists & inhibitors : Multiprotein Complexes, TOR Serine-Threonine Kinases.
- chemical , metabolism : Carrier Proteins, Filamins, Multiprotein Complexes, TOR Serine-Threonine Kinases.
- drug effects : Cell Adhesion, Cell Movement, Enzyme Activation.
- metabolism : Actin Cytoskeleton, Glioblastoma.
- pathology : Glioblastoma.
- chemical , pharmacology : Indoles, Purines.
- Cell Line, Tumor, Humans, Mechanistic Target of Rapamycin Complex 2, Phosphorylation, Protein Binding, Rapamycin-Insensitive Companion of mTOR Protein.

Abstract

BACKGROUND

Glioblastoma multiforme (GBM) is one of the most highly metastatic cancers. GBM has been associated with a high level of the mechanistic target of rapamycin complex 2 (mTORC2) activity. We aimed to observe roles of mTORC2 in GBM cells especially on actin cytoskeleton reorganization, cell migration and invasion, and further determine new important players involved in the regulation of these cellular processes.

METHODS

To further investigate the significance of mTORC2 in GBM, we treated GBM cells with PP242, an ATP-competitive inhibitor of mTOR, and used RICTOR siRNA to knock down mTORC2 activity. Effects on actin cytoskeleton, focal adhesion, migration, and invasion of GBM cells were examined. To gain insight into molecular basis of the mTORC2 effects on cellular cytoskeletal arrangement and motility/invasion, we affinity purified mTORC2 from GBM cells and identified proteins of interest by mass spectrometry. Characterization of the protein of interest was performed.

RESULTS

In addition to the inhibition of mTORC2 activity, we demonstrated significant alteration of actin distribution as revealed by the use of phalloidin staining. Furthermore, vinculin staining was altered which suggests changes in focal adhesion. Inhibition of cell migration and invasion was observed with PP242. Two major proteins that are associated with this mTORC2 multiprotein complex were found. Mass spectrometry identified one of them as Filamin A (FLNA). Association of FLNA with RICTOR but not mTOR was demonstrated. Moreover, in vitro, purified mTORC2 can phosphorylate FLNA likewise its known substrate, AKT. In GBM cells, colocalization of FLNA with RICTOR was observed, and the overall amounts of FLNA protein as well as phosphorylated FLNA are high. Upon treatments of RICTOR siRNA or PP242, phosphorylated FLNA levels at the regulatory residue (Ser2152) decreased. This treatment also disrupted colocalization of Actin filaments and FLNA.

CONCLUSIONS

Our results support FLNA as a new downstream effector of mTORC2 controlling GBM cell motility. This new mTORC2-FLNA signaling pathway plays important roles in motility and invasion of glioblastoma cells.

DOI: 10.1186/s12943-015-0396-z
PubMed: 26134617
PubMed Central: PMC4489161

Affiliations:

États-Unis

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

to stream Main, to step Corpus: 000C30
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Le document en format XML

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<series><title level="j">Molecular cancer</title>
<idno type="eISSN">1476-4598</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actin Cytoskeleton (metabolism)</term>
<term>Carrier Proteins (metabolism)</term>
<term>Cell Adhesion (drug effects)</term>
<term>Cell Line, Tumor (MeSH)</term>
<term>Cell Movement (drug effects)</term>
<term>Enzyme Activation (drug effects)</term>
<term>Filamins (metabolism)</term>
<term>Glioblastoma (metabolism)</term>
<term>Glioblastoma (pathology)</term>
<term>Humans (MeSH)</term>
<term>Indoles (pharmacology)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (MeSH)</term>
<term>Multiprotein Complexes (antagonists & inhibitors)</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein Binding (MeSH)</term>
<term>Purines (pharmacology)</term>
<term>Rapamycin-Insensitive Companion of mTOR Protein (MeSH)</term>
<term>TOR Serine-Threonine Kinases (antagonists & inhibitors)</term>
<term>TOR Serine-Threonine Kinases (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (effets des médicaments et des substances chimiques)</term>
<term>Adhérence cellulaire (effets des médicaments et des substances chimiques)</term>
<term>Compagnon de mTOR insensible à la rapamycine (MeSH)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (MeSH)</term>
<term>Complexes multiprotéiques (antagonistes et inhibiteurs)</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Cytosquelette d'actine (métabolisme)</term>
<term>Filamines (métabolisme)</term>
<term>Glioblastome (anatomopathologie)</term>
<term>Glioblastome (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Indoles (pharmacologie)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Lignée cellulaire tumorale (MeSH)</term>
<term>Mouvement cellulaire (effets des médicaments et des substances chimiques)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protéines de transport (métabolisme)</term>
<term>Purines (pharmacologie)</term>
<term>Sérine-thréonine kinases TOR (antagonistes et inhibiteurs)</term>
<term>Sérine-thréonine kinases TOR (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Multiprotein Complexes</term>
<term>TOR Serine-Threonine Kinases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carrier Proteins</term>
<term>Filamins</term>
<term>Multiprotein Complexes</term>
<term>TOR Serine-Threonine Kinases</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Glioblastome</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Complexes multiprotéiques</term>
<term>Sérine-thréonine kinases TOR</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Adhesion</term>
<term>Cell Movement</term>
<term>Enzyme Activation</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Activation enzymatique</term>
<term>Adhérence cellulaire</term>
<term>Mouvement cellulaire</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Actin Cytoskeleton</term>
<term>Glioblastoma</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexes multiprotéiques</term>
<term>Cytosquelette d'actine</term>
<term>Filamines</term>
<term>Glioblastome</term>
<term>Protéines de transport</term>
<term>Sérine-thréonine kinases TOR</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Glioblastoma</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Indoles</term>
<term>Purines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Indoles</term>
<term>Purines</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cell Line, Tumor</term>
<term>Humans</term>
<term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Phosphorylation</term>
<term>Protein Binding</term>
<term>Rapamycin-Insensitive Companion of mTOR Protein</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Compagnon de mTOR insensible à la rapamycine</term>
<term>Complexe-2 cible mécanistique de la rapamycine</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire tumorale</term>
<term>Phosphorylation</term>
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<front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b>
</p>
<p>Glioblastoma multiforme (GBM) is one of the most highly metastatic cancers. GBM has been associated with a high level of the mechanistic target of rapamycin complex 2 (mTORC2) activity. We aimed to observe roles of mTORC2 in GBM cells especially on actin cytoskeleton reorganization, cell migration and invasion, and further determine new important players involved in the regulation of these cellular processes.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>METHODS</b>
</p>
<p>To further investigate the significance of mTORC2 in GBM, we treated GBM cells with PP242, an ATP-competitive inhibitor of mTOR, and used RICTOR siRNA to knock down mTORC2 activity. Effects on actin cytoskeleton, focal adhesion, migration, and invasion of GBM cells were examined. To gain insight into molecular basis of the mTORC2 effects on cellular cytoskeletal arrangement and motility/invasion, we affinity purified mTORC2 from GBM cells and identified proteins of interest by mass spectrometry. Characterization of the protein of interest was performed.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RESULTS</b>
</p>
<p>In addition to the inhibition of mTORC2 activity, we demonstrated significant alteration of actin distribution as revealed by the use of phalloidin staining. Furthermore, vinculin staining was altered which suggests changes in focal adhesion. Inhibition of cell migration and invasion was observed with PP242. Two major proteins that are associated with this mTORC2 multiprotein complex were found. Mass spectrometry identified one of them as Filamin A (FLNA). Association of FLNA with RICTOR but not mTOR was demonstrated. Moreover, in vitro, purified mTORC2 can phosphorylate FLNA likewise its known substrate, AKT. In GBM cells, colocalization of FLNA with RICTOR was observed, and the overall amounts of FLNA protein as well as phosphorylated FLNA are high. Upon treatments of RICTOR siRNA or PP242, phosphorylated FLNA levels at the regulatory residue (Ser2152) decreased. This treatment also disrupted colocalization of Actin filaments and FLNA.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b>
</p>
<p>Our results support FLNA as a new downstream effector of mTORC2 controlling GBM cell motility. This new mTORC2-FLNA signaling pathway plays important roles in motility and invasion of glioblastoma cells.</p>
</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26134617</PMID>
<DateCompleted><Year>2016</Year>
<Month>03</Month>
<Day>24</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>12</Month>
<Day>11</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1476-4598</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>14</Volume>
<PubDate><Year>2015</Year>
<Month>Jul</Month>
<Day>02</Day>
</PubDate>
</JournalIssue>
<Title>Molecular cancer</Title>
<ISOAbbreviation>Mol Cancer</ISOAbbreviation>
</Journal>
<ArticleTitle>Significance of filamin A in mTORC2 function in glioblastoma.</ArticleTitle>
<Pagination><MedlinePgn>127</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1186/s12943-015-0396-z</ELocationID>
<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Glioblastoma multiforme (GBM) is one of the most highly metastatic cancers. GBM has been associated with a high level of the mechanistic target of rapamycin complex 2 (mTORC2) activity. We aimed to observe roles of mTORC2 in GBM cells especially on actin cytoskeleton reorganization, cell migration and invasion, and further determine new important players involved in the regulation of these cellular processes.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="METHODS">To further investigate the significance of mTORC2 in GBM, we treated GBM cells with PP242, an ATP-competitive inhibitor of mTOR, and used RICTOR siRNA to knock down mTORC2 activity. Effects on actin cytoskeleton, focal adhesion, migration, and invasion of GBM cells were examined. To gain insight into molecular basis of the mTORC2 effects on cellular cytoskeletal arrangement and motility/invasion, we affinity purified mTORC2 from GBM cells and identified proteins of interest by mass spectrometry. Characterization of the protein of interest was performed.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">In addition to the inhibition of mTORC2 activity, we demonstrated significant alteration of actin distribution as revealed by the use of phalloidin staining. Furthermore, vinculin staining was altered which suggests changes in focal adhesion. Inhibition of cell migration and invasion was observed with PP242. Two major proteins that are associated with this mTORC2 multiprotein complex were found. Mass spectrometry identified one of them as Filamin A (FLNA). Association of FLNA with RICTOR but not mTOR was demonstrated. Moreover, in vitro, purified mTORC2 can phosphorylate FLNA likewise its known substrate, AKT. In GBM cells, colocalization of FLNA with RICTOR was observed, and the overall amounts of FLNA protein as well as phosphorylated FLNA are high. Upon treatments of RICTOR siRNA or PP242, phosphorylated FLNA levels at the regulatory residue (Ser2152) decreased. This treatment also disrupted colocalization of Actin filaments and FLNA.</AbstractText>
<AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">Our results support FLNA as a new downstream effector of mTORC2 controlling GBM cell motility. This new mTORC2-FLNA signaling pathway plays important roles in motility and invasion of glioblastoma cells.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chantaravisoot</LastName>
<ForeName>Naphat</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, Immunology & Molecular Genetics, University of California, Los Angeles, CA, 90095, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wongkongkathep</LastName>
<ForeName>Piriya</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, University of California, Los Angeles, CA, 90095, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Loo</LastName>
<ForeName>Joseph A</ForeName>
<Initials>JA</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, University of California, Los Angeles, CA, 90095, USA.</Affiliation>
</AffiliationInfo>
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   |texte=   Significance of filamin A in mTORC2 function in glioblastoma.
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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

Significance of filamin A in mTORC2 function in glioblastoma.

Significance of filamin A in mTORC2 function in glioblastoma.

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