Phosphorylation Regulates FOXC2-Mediated Transcription in Lymphatic Endothelial Cells
Identifieur interne : 003300 ( Main/Exploration ); précédent : 003299; suivant : 003301Phosphorylation Regulates FOXC2-Mediated Transcription in Lymphatic Endothelial Cells
Auteurs : Konstantin I. Ivanov ; Yan Agalarov ; Leena Valmu ; Olga Samuilova ; Johanna Liebl ; Nawal Houhou ; Hélène Maby-El Hajjami ; Camilla Norrmén ; Muriel Jaquet ; Naoyuki Miura ; Nadine Zangger ; Seppo Yl Herttuala ; Mauro Delorenzi ; Tatiana V. PetrovaSource :
- Molecular and Cellular Biology [ 0270-7306 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux, Cellules COS, Cellules HEK293, Cellules HepG2, Cellules cultivées, Cellules endothéliales (métabolisme), Cercopithecus aethiops, Données de séquences moléculaires, Facteurs de transcription Forkhead (génétique), Facteurs de transcription Forkhead (métabolisme), Humains, Immunotransfert, Microscopie confocale, Mutation, Phosphorylation, Proline (génétique), Proline (métabolisme), RT-PCR, Régulation de l'expression des gènes, Sites de fixation (génétique), Souris, Souris transgéniques, Séquence d'acides aminés, Séquençage par oligonucléotides en batterie, Sérine (génétique), Sérine (métabolisme), Thréonine (génétique), Thréonine (métabolisme), Transcription génétique (génétique).
- MESH :
- génétique : Facteurs de transcription Forkhead, Proline, Sites de fixation, Sérine, Thréonine, Transcription génétique.
- métabolisme : Cellules endothéliales, Facteurs de transcription Forkhead, Proline, Sérine, Thréonine.
- Animaux, Cellules COS, Cellules HEK293, Cellules HepG2, Cellules cultivées, Cercopithecus aethiops, Données de séquences moléculaires, Humains, Immunotransfert, Microscopie confocale, Mutation, Phosphorylation, RT-PCR, Régulation de l'expression des gènes, Souris, Souris transgéniques, Séquence d'acides aminés, Séquençage par oligonucléotides en batterie.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Binding Sites (genetics), COS Cells, Cells, Cultured, Cercopithecus aethiops, Endothelial Cells (metabolism), Forkhead Transcription Factors (genetics), Forkhead Transcription Factors (metabolism), Gene Expression Regulation, HEK293 Cells, Hep G2 Cells, Humans, Immunoblotting, Mice, Mice, Transgenic, Microscopy, Confocal, Molecular Sequence Data, Mutation, Oligonucleotide Array Sequence Analysis, Phosphorylation, Proline (genetics), Proline (metabolism), Reverse Transcriptase Polymerase Chain Reaction, Serine (genetics), Serine (metabolism), Threonine (genetics), Threonine (metabolism), Transcription, Genetic (genetics).
- MESH :
- chemical , genetics : Forkhead Transcription Factors, Proline, Serine, Threonine.
- genetics : Binding Sites, Transcription, Genetic.
- metabolism : Endothelial Cells, Forkhead Transcription Factors, Proline, Serine, Threonine.
- Amino Acid Sequence, Animals, COS Cells, Cells, Cultured, Cercopithecus aethiops, Gene Expression Regulation, HEK293 Cells, Hep G2 Cells, Humans, Immunoblotting, Mice, Mice, Transgenic, Microscopy, Confocal, Molecular Sequence Data, Mutation, Oligonucleotide Array Sequence Analysis, Phosphorylation, Reverse Transcriptase Polymerase Chain Reaction.
Abstract
One of the key mechanisms linking cell signaling and control of gene expression is reversible phosphorylation of transcription factors. FOXC2 is a forkhead transcription factor that is mutated in the human vascular disease lymphedema-distichiasis and plays an essential role in lymphatic vascular development. However, the mechanisms regulating FOXC2 transcriptional activity are not well understood. We report here that FOXC2 is phosphorylated on eight evolutionarily conserved proline-directed serine/threonine residues. Loss of phosphorylation at these sites triggers substantial changes in the FOXC2 transcriptional program. Through genome-wide location analysis in lymphatic endothelial cells, we demonstrate that the changes are due to selective inhibition of FOXC2 recruitment to chromatin. The extent of the inhibition varied between individual binding sites, suggesting a novel rheostat-like mechanism by which expression of specific genes can be differentially regulated by FOXC2 phosphorylation. Furthermore, unlike the wild-type protein, the phosphorylation-deficient mutant of FOXC2 failed to induce vascular remodeling
Url:
DOI: 10.1128/MCB.01387-12
PubMed: 23878394
PubMed Central: 3811871
Affiliations:
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Le document en format XML
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<series><title level="j">Molecular and Cellular Biology</title>
<idno type="ISSN">0270-7306</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Binding Sites (genetics)</term>
<term>COS Cells</term>
<term>Cells, Cultured</term>
<term>Cercopithecus aethiops</term>
<term>Endothelial Cells (metabolism)</term>
<term>Forkhead Transcription Factors (genetics)</term>
<term>Forkhead Transcription Factors (metabolism)</term>
<term>Gene Expression Regulation</term>
<term>HEK293 Cells</term>
<term>Hep G2 Cells</term>
<term>Humans</term>
<term>Immunoblotting</term>
<term>Mice</term>
<term>Mice, Transgenic</term>
<term>Microscopy, Confocal</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
<term>Oligonucleotide Array Sequence Analysis</term>
<term>Phosphorylation</term>
<term>Proline (genetics)</term>
<term>Proline (metabolism)</term>
<term>Reverse Transcriptase Polymerase Chain Reaction</term>
<term>Serine (genetics)</term>
<term>Serine (metabolism)</term>
<term>Threonine (genetics)</term>
<term>Threonine (metabolism)</term>
<term>Transcription, Genetic (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Cellules COS</term>
<term>Cellules HEK293</term>
<term>Cellules HepG2</term>
<term>Cellules cultivées</term>
<term>Cellules endothéliales (métabolisme)</term>
<term>Cercopithecus aethiops</term>
<term>Données de séquences moléculaires</term>
<term>Facteurs de transcription Forkhead (génétique)</term>
<term>Facteurs de transcription Forkhead (métabolisme)</term>
<term>Humains</term>
<term>Immunotransfert</term>
<term>Microscopie confocale</term>
<term>Mutation</term>
<term>Phosphorylation</term>
<term>Proline (génétique)</term>
<term>Proline (métabolisme)</term>
<term>RT-PCR</term>
<term>Régulation de l'expression des gènes</term>
<term>Sites de fixation (génétique)</term>
<term>Souris</term>
<term>Souris transgéniques</term>
<term>Séquence d'acides aminés</term>
<term>Séquençage par oligonucléotides en batterie</term>
<term>Sérine (génétique)</term>
<term>Sérine (métabolisme)</term>
<term>Thréonine (génétique)</term>
<term>Thréonine (métabolisme)</term>
<term>Transcription génétique (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Forkhead Transcription Factors</term>
<term>Proline</term>
<term>Serine</term>
<term>Threonine</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Binding Sites</term>
<term>Transcription, Genetic</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteurs de transcription Forkhead</term>
<term>Proline</term>
<term>Sites de fixation</term>
<term>Sérine</term>
<term>Thréonine</term>
<term>Transcription génétique</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endothelial Cells</term>
<term>Forkhead Transcription Factors</term>
<term>Proline</term>
<term>Serine</term>
<term>Threonine</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellules endothéliales</term>
<term>Facteurs de transcription Forkhead</term>
<term>Proline</term>
<term>Sérine</term>
<term>Thréonine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>COS Cells</term>
<term>Cells, Cultured</term>
<term>Cercopithecus aethiops</term>
<term>Gene Expression Regulation</term>
<term>HEK293 Cells</term>
<term>Hep G2 Cells</term>
<term>Humans</term>
<term>Immunoblotting</term>
<term>Mice</term>
<term>Mice, Transgenic</term>
<term>Microscopy, Confocal</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
<term>Oligonucleotide Array Sequence Analysis</term>
<term>Phosphorylation</term>
<term>Reverse Transcriptase Polymerase Chain Reaction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules COS</term>
<term>Cellules HEK293</term>
<term>Cellules HepG2</term>
<term>Cellules cultivées</term>
<term>Cercopithecus aethiops</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Immunotransfert</term>
<term>Microscopie confocale</term>
<term>Mutation</term>
<term>Phosphorylation</term>
<term>RT-PCR</term>
<term>Régulation de l'expression des gènes</term>
<term>Souris</term>
<term>Souris transgéniques</term>
<term>Séquence d'acides aminés</term>
<term>Séquençage par oligonucléotides en batterie</term>
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<front><div type="abstract" xml:lang="en"><p>One of the key mechanisms linking cell signaling and control of gene expression is reversible phosphorylation of transcription factors. FOXC2 is a forkhead transcription factor that is mutated in the human vascular disease lymphedema-distichiasis and plays an essential role in lymphatic vascular development. However, the mechanisms regulating FOXC2 transcriptional activity are not well understood. We report here that FOXC2 is phosphorylated on eight evolutionarily conserved proline-directed serine/threonine residues. Loss of phosphorylation at these sites triggers substantial changes in the FOXC2 transcriptional program. Through genome-wide location analysis in lymphatic endothelial cells, we demonstrate that the changes are due to selective inhibition of FOXC2 recruitment to chromatin. The extent of the inhibition varied between individual binding sites, suggesting a novel rheostat-like mechanism by which expression of specific genes can be differentially regulated by FOXC2 phosphorylation. Furthermore, unlike the wild-type protein, the phosphorylation-deficient mutant of FOXC2 failed to induce vascular remodeling <italic>in vivo</italic>
. Collectively, our results point to the pivotal role of phosphorylation in the regulation of FOXC2-mediated transcription in lymphatic endothelial cells and underscore the importance of FOXC2 phosphorylation in vascular development.</p>
</div>
</front>
</TEI>
<affiliations><list></list>
<tree><noCountry><name sortKey="Agalarov, Yan" sort="Agalarov, Yan" uniqKey="Agalarov Y" first="Yan" last="Agalarov">Yan Agalarov</name>
<name sortKey="Delorenzi, Mauro" sort="Delorenzi, Mauro" uniqKey="Delorenzi M" first="Mauro" last="Delorenzi">Mauro Delorenzi</name>
<name sortKey="Houhou, Nawal" sort="Houhou, Nawal" uniqKey="Houhou N" first="Nawal" last="Houhou">Nawal Houhou</name>
<name sortKey="Ivanov, Konstantin I" sort="Ivanov, Konstantin I" uniqKey="Ivanov K" first="Konstantin I." last="Ivanov">Konstantin I. Ivanov</name>
<name sortKey="Jaquet, Muriel" sort="Jaquet, Muriel" uniqKey="Jaquet M" first="Muriel" last="Jaquet">Muriel Jaquet</name>
<name sortKey="Liebl, Johanna" sort="Liebl, Johanna" uniqKey="Liebl J" first="Johanna" last="Liebl">Johanna Liebl</name>
<name sortKey="Maby El Hajjami, Helene" sort="Maby El Hajjami, Helene" uniqKey="Maby El Hajjami H" first="Hélène" last="Maby-El Hajjami">Hélène Maby-El Hajjami</name>
<name sortKey="Miura, Naoyuki" sort="Miura, Naoyuki" uniqKey="Miura N" first="Naoyuki" last="Miura">Naoyuki Miura</name>
<name sortKey="Norrmen, Camilla" sort="Norrmen, Camilla" uniqKey="Norrmen C" first="Camilla" last="Norrmén">Camilla Norrmén</name>
<name sortKey="Petrova, Tatiana V" sort="Petrova, Tatiana V" uniqKey="Petrova T" first="Tatiana V." last="Petrova">Tatiana V. Petrova</name>
<name sortKey="Samuilova, Olga" sort="Samuilova, Olga" uniqKey="Samuilova O" first="Olga" last="Samuilova">Olga Samuilova</name>
<name sortKey="Valmu, Leena" sort="Valmu, Leena" uniqKey="Valmu L" first="Leena" last="Valmu">Leena Valmu</name>
<name sortKey="Yl Herttuala, Seppo" sort="Yl Herttuala, Seppo" uniqKey="Yl Herttuala S" first="Seppo" last="Yl Herttuala">Seppo Yl Herttuala</name>
<name sortKey="Zangger, Nadine" sort="Zangger, Nadine" uniqKey="Zangger N" first="Nadine" last="Zangger">Nadine Zangger</name>
</noCountry>
</tree>
</affiliations>
</record>
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