Glycoprotein hormone receptors: link between receptor homodimerization and negative cooperativity.
Identifieur interne : 002337 ( PubMed/Corpus ); précédent : 002336; suivant : 002338Glycoprotein hormone receptors: link between receptor homodimerization and negative cooperativity.
Auteurs : Eneko Urizar ; Lucia Montanelli ; Tiffany Loy ; Marco Bonomi ; Stéphane Swillens ; Céline Gales ; Michel Bouvier ; Guillaume Smits ; Gilbert Vassart ; Sabine CostagliolaSource :
- The EMBO journal [ 0261-4189 ] ; 2005.
English descriptors
- KwdEn :
- Allosteric Regulation, Animals, Bacterial Proteins (analysis), Binding Sites, Cell Line, Cell Membrane (metabolism), Cyclic AMP (biosynthesis), Dimerization, Fluorescence Resonance Energy Transfer, Horses, Humans, Kidney, Luminescent Proteins (analysis), Models, Molecular, Protein Binding, Protein Interaction Mapping, Protein Multimerization, Protein Structure, Tertiary, Receptors, FSH (chemistry), Receptors, FSH (metabolism), Receptors, LH (chemistry), Receptors, LH (metabolism), Receptors, Thyrotropin (chemistry), Receptors, Thyrotropin (metabolism), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (metabolism), Sus scrofa, Thyroid Gland (metabolism), Transfection.
- MESH :
- chemical , analysis : Bacterial Proteins, Luminescent Proteins.
- chemical , biosynthesis : Cyclic AMP.
- chemical , chemistry : Receptors, FSH, Receptors, LH, Receptors, Thyrotropin, Recombinant Fusion Proteins.
- metabolism : Cell Membrane, Receptors, FSH, Receptors, LH, Receptors, Thyrotropin, Recombinant Fusion Proteins, Thyroid Gland.
- Allosteric Regulation, Animals, Binding Sites, Cell Line, Dimerization, Fluorescence Resonance Energy Transfer, Horses, Humans, Kidney, Models, Molecular, Protein Binding, Protein Interaction Mapping, Protein Multimerization, Protein Structure, Tertiary, Sus scrofa, Transfection.
Abstract
The monomeric model of rhodopsin-like G protein-coupled receptors (GPCRs) has progressively yielded the floor to the concept of GPCRs being oligo(di)mers, but the functional correlates of dimerization remain unclear. In this report, dimers of glycoprotein hormone receptors were demonstrated in living cells, with a combination of biophysical (bioluminescence resonance energy transfer and homogenous time resolved fluorescence/fluorescence resonance energy transfer), functional and biochemical approaches. Thyrotropin (TSHr) and lutropin (LH/CGr) receptors form homo- and heterodimers, via interactions involving primarily their heptahelical domains. The large hormone-binding ectodomains were dispensable for dimerization but modulated protomer interaction. Dimerization was not affected by agonist binding. Observed functional complementation indicates that TSHr dimers may function as a single functional unit. Finally, heterologous binding-competition studies, performed with heterodimers between TSHr and LH/CG-TSHr chimeras, demonstrated the unsuspected existence of strong negative cooperativity of hormone binding. Tracer desorption experiments indicated an allosteric behavior in TSHr and, to a lesser extent, in LH/CGr and FSHr homodimers. This study is the first report of homodimerization associated with negative cooperativity in rhodopsin-like GPCRs. As such, it may warrant revisitation of allosterism in the whole GPCR family.
DOI: 10.1038/sj.emboj.7600686
PubMed: 15889138
Links to Exploration step
pubmed:15889138Le document en format XML
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Thyrotropin (metabolism)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Sus scrofa</term><term>Thyroid Gland (metabolism)</term><term>Transfection</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Bacterial Proteins</term><term>Luminescent Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Cyclic AMP</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Receptors, FSH</term><term>Receptors, LH</term><term>Receptors, Thyrotropin</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Receptors, FSH</term><term>Receptors, LH</term><term>Receptors, Thyrotropin</term><term>Recombinant Fusion Proteins</term><term>Thyroid Gland</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Allosteric Regulation</term><term>Animals</term><term>Binding Sites</term><term>Cell Line</term><term>Dimerization</term><term>Fluorescence Resonance Energy Transfer</term><term>Horses</term><term>Humans</term><term>Kidney</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Interaction Mapping</term><term>Protein Multimerization</term><term>Protein Structure, Tertiary</term><term>Sus scrofa</term><term>Transfection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The monomeric model of rhodopsin-like G protein-coupled receptors (GPCRs) has progressively yielded the floor to the concept of GPCRs being oligo(di)mers, but the functional correlates of dimerization remain unclear. In this report, dimers of glycoprotein hormone receptors were demonstrated in living cells, with a combination of biophysical (bioluminescence resonance energy transfer and homogenous time resolved fluorescence/fluorescence resonance energy transfer), functional and biochemical approaches. Thyrotropin (TSHr) and lutropin (LH/CGr) receptors form homo- and heterodimers, via interactions involving primarily their heptahelical domains. The large hormone-binding ectodomains were dispensable for dimerization but modulated protomer interaction. Dimerization was not affected by agonist binding. Observed functional complementation indicates that TSHr dimers may function as a single functional unit. Finally, heterologous binding-competition studies, performed with heterodimers between TSHr and LH/CG-TSHr chimeras, demonstrated the unsuspected existence of strong negative cooperativity of hormone binding. Tracer desorption experiments indicated an allosteric behavior in TSHr and, to a lesser extent, in LH/CGr and FSHr homodimers. This study is the first report of homodimerization associated with negative cooperativity in rhodopsin-like GPCRs. As such, it may warrant revisitation of allosterism in the whole GPCR family.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15889138</PMID><DateCompleted><Year>2005</Year><Month>08</Month><Day>02</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0261-4189</ISSN><JournalIssue CitedMedium="Print"><Volume>24</Volume><Issue>11</Issue><PubDate><Year>2005</Year><Month>Jun</Month><Day>01</Day></PubDate></JournalIssue><Title>The EMBO journal</Title><ISOAbbreviation>EMBO J.</ISOAbbreviation></Journal><ArticleTitle>Glycoprotein hormone receptors: link between receptor homodimerization and negative cooperativity.</ArticleTitle><Pagination><MedlinePgn>1954-64</MedlinePgn></Pagination><Abstract><AbstractText>The monomeric model of rhodopsin-like G protein-coupled receptors (GPCRs) has progressively yielded the floor to the concept of GPCRs being oligo(di)mers, but the functional correlates of dimerization remain unclear. In this report, dimers of glycoprotein hormone receptors were demonstrated in living cells, with a combination of biophysical (bioluminescence resonance energy transfer and homogenous time resolved fluorescence/fluorescence resonance energy transfer), functional and biochemical approaches. Thyrotropin (TSHr) and lutropin (LH/CGr) receptors form homo- and heterodimers, via interactions involving primarily their heptahelical domains. The large hormone-binding ectodomains were dispensable for dimerization but modulated protomer interaction. Dimerization was not affected by agonist binding. Observed functional complementation indicates that TSHr dimers may function as a single functional unit. Finally, heterologous binding-competition studies, performed with heterodimers between TSHr and LH/CG-TSHr chimeras, demonstrated the unsuspected existence of strong negative cooperativity of hormone binding. Tracer desorption experiments indicated an allosteric behavior in TSHr and, to a lesser extent, in LH/CGr and FSHr homodimers. This study is the first report of homodimerization associated with negative cooperativity in rhodopsin-like GPCRs. As such, it may warrant revisitation of allosterism in the whole GPCR family.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Urizar</LastName><ForeName>Eneko</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>IRIBHM, Université Libre de Bruxelles, Campus Erasme, Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Montanelli</LastName><ForeName>Lucia</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Loy</LastName><ForeName>Tiffany</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Bonomi</LastName><ForeName>Marco</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Swillens</LastName><ForeName>Stéphane</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Gales</LastName><ForeName>Céline</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Bouvier</LastName><ForeName>Michel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Smits</LastName><ForeName>Guillaume</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Vassart</LastName><ForeName>Gilbert</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Costagliola</LastName><ForeName>Sabine</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>05</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>EMBO 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Bacteria</NameOfSubstance></Chemical><Chemical><RegistryNumber>E0399OZS9N</RegistryNumber><NameOfSubstance UI="D000242">Cyclic AMP</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000494" MajorTopicYN="N">Allosteric Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000378" 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Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025941" MajorTopicYN="N">Protein Interaction Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011962" MajorTopicYN="N">Receptors, FSH</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011974" MajorTopicYN="N">Receptors, LH</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011989" MajorTopicYN="N">Receptors, Thyrotropin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D034421" MajorTopicYN="N">Sus scrofa</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013961" MajorTopicYN="N">Thyroid Gland</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014162" 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