Structure of the Tuberous Sclerosis Complex 2 (TSC2) N Terminus Provides Insight into Complex Assembly and Tuberous Sclerosis Pathogenesis.
Identifieur interne : 000A05 ( Main/Exploration ); précédent : 000A04; suivant : 000A06Structure of the Tuberous Sclerosis Complex 2 (TSC2) N Terminus Provides Insight into Complex Assembly and Tuberous Sclerosis Pathogenesis.
Auteurs : Reinhard Zech [Allemagne] ; Stephan Kiontke [Allemagne] ; Uwe Mueller ; Andrea Oeckinghaus ; Daniel Kümmel [Allemagne]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2016.
Descripteurs français
- KwdFr :
- Cellules HEK293 (MeSH), Chaetomium (composition chimique), Chaetomium (génétique), Chaetomium (métabolisme), Complexe de la sclérose tubéreuse (MeSH), Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (génétique), Complexes multiprotéiques (métabolisme), Domaines protéiques (MeSH), Humains (MeSH), Neuropeptides (génétique), Neuropeptides (métabolisme), Protéine homologue de Ras enrichie dans le cerveau (MeSH), Protéine-1 du complexe de la sclérose tubéreuse (MeSH), Protéine-2 du complexe de la sclérose tubéreuse (MeSH), Protéines G monomériques (génétique), Protéines G monomériques (métabolisme), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines suppresseurs de tumeurs (composition chimique), Protéines suppresseurs de tumeurs (génétique), Protéines suppresseurs de tumeurs (métabolisme), Similitude structurale de protéines (MeSH), Sérine-thréonine kinases TOR (génétique), Sérine-thréonine kinases TOR (métabolisme).
- MESH :
- composition chimique : Chaetomium, Protéines fongiques, Protéines suppresseurs de tumeurs.
- génétique : Chaetomium, Complexes multiprotéiques, Neuropeptides, Protéines G monomériques, Protéines fongiques, Protéines suppresseurs de tumeurs, Sérine-thréonine kinases TOR.
- métabolisme : Chaetomium, Complexes multiprotéiques, Neuropeptides, Protéines G monomériques, Protéines fongiques, Protéines suppresseurs de tumeurs, Sérine-thréonine kinases TOR.
- Cellules HEK293, Complexe de la sclérose tubéreuse, Complexe-1 cible mécanistique de la rapamycine, Domaines protéiques, Humains, Protéine homologue de Ras enrichie dans le cerveau, Protéine-1 du complexe de la sclérose tubéreuse, Protéine-2 du complexe de la sclérose tubéreuse, Similitude structurale de protéines.
English descriptors
- KwdEn :
- Chaetomium (chemistry), Chaetomium (genetics), Chaetomium (metabolism), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), HEK293 Cells (MeSH), Humans (MeSH), Mechanistic Target of Rapamycin Complex 1 (MeSH), Monomeric GTP-Binding Proteins (genetics), Monomeric GTP-Binding Proteins (metabolism), Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Neuropeptides (genetics), Neuropeptides (metabolism), Protein Domains (MeSH), Ras Homolog Enriched in Brain Protein (MeSH), Structural Homology, Protein (MeSH), TOR Serine-Threonine Kinases (genetics), TOR Serine-Threonine Kinases (metabolism), Tuberous Sclerosis (MeSH), Tuberous Sclerosis Complex 1 Protein (MeSH), Tuberous Sclerosis Complex 2 Protein (MeSH), Tumor Suppressor Proteins (chemistry), Tumor Suppressor Proteins (genetics), Tumor Suppressor Proteins (metabolism).
- MESH :
- chemical , chemistry : Fungal Proteins, Tumor Suppressor Proteins.
- chemistry : Chaetomium.
- genetics : Chaetomium, Fungal Proteins, Monomeric GTP-Binding Proteins, Multiprotein Complexes, Neuropeptides, TOR Serine-Threonine Kinases, Tumor Suppressor Proteins.
- metabolism : Chaetomium, Fungal Proteins, Monomeric GTP-Binding Proteins, Multiprotein Complexes, Neuropeptides, TOR Serine-Threonine Kinases, Tumor Suppressor Proteins.
- HEK293 Cells, Humans, Mechanistic Target of Rapamycin Complex 1, Protein Domains, Ras Homolog Enriched in Brain Protein, Structural Homology, Protein, Tuberous Sclerosis, Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein.
Abstract
Tuberous sclerosis complex (TSC) is caused by mutations in the TSC1 and TSC2 tumor suppressor genes. The gene products hamartin and tuberin form the TSC complex that acts as GTPase-activating protein for Rheb and negatively regulates the mammalian target of rapamycin complex 1 (mTORC1). Tuberin contains a RapGAP homology domain responsible for inactivation of Rheb, but functions of other protein domains remain elusive. Here we show that the TSC2 N terminus interacts with the TSC1 C terminus to mediate complex formation. The structure of the TSC2 N-terminal domain from Chaetomium thermophilum and a homology model of the human tuberin N terminus are presented. We characterize the molecular requirements for TSC1-TSC2 interactions and analyze pathological point mutations in tuberin. Many mutations are structural and produce improperly folded protein, explaining their effect in pathology, but we identify one point mutant that abrogates complex formation without affecting protein structure. We provide the first structural information on TSC2/tuberin with novel insight into the molecular function.
DOI: 10.1074/jbc.M116.732446
PubMed: 27493206
PubMed Central: PMC5025687
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(genetics)</term><term>Fungal Proteins (metabolism)</term><term>HEK293 Cells (MeSH)</term><term>Humans (MeSH)</term><term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term><term>Monomeric GTP-Binding Proteins (genetics)</term><term>Monomeric GTP-Binding Proteins (metabolism)</term><term>Multiprotein Complexes (genetics)</term><term>Multiprotein Complexes (metabolism)</term><term>Neuropeptides (genetics)</term><term>Neuropeptides (metabolism)</term><term>Protein Domains (MeSH)</term><term>Ras Homolog Enriched in Brain Protein (MeSH)</term><term>Structural Homology, Protein (MeSH)</term><term>TOR Serine-Threonine Kinases (genetics)</term><term>TOR Serine-Threonine Kinases (metabolism)</term><term>Tuberous Sclerosis (MeSH)</term><term>Tuberous Sclerosis Complex 1 Protein (MeSH)</term><term>Tuberous Sclerosis Complex 2 Protein (MeSH)</term><term>Tumor Suppressor Proteins (chemistry)</term><term>Tumor Suppressor Proteins (genetics)</term><term>Tumor Suppressor Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HEK293 (MeSH)</term><term>Chaetomium (composition chimique)</term><term>Chaetomium (génétique)</term><term>Chaetomium (métabolisme)</term><term>Complexe de la sclérose tubéreuse (MeSH)</term><term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term><term>Complexes multiprotéiques (génétique)</term><term>Complexes multiprotéiques (métabolisme)</term><term>Domaines protéiques (MeSH)</term><term>Humains (MeSH)</term><term>Neuropeptides (génétique)</term><term>Neuropeptides (métabolisme)</term><term>Protéine homologue de Ras enrichie dans le cerveau (MeSH)</term><term>Protéine-1 du complexe de la sclérose tubéreuse (MeSH)</term><term>Protéine-2 du complexe de la sclérose tubéreuse (MeSH)</term><term>Protéines G monomériques (génétique)</term><term>Protéines G monomériques (métabolisme)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines suppresseurs de tumeurs (composition chimique)</term><term>Protéines suppresseurs de tumeurs (génétique)</term><term>Protéines suppresseurs de tumeurs (métabolisme)</term><term>Similitude structurale de protéines (MeSH)</term><term>Sérine-thréonine kinases TOR (génétique)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term><term>Tumor Suppressor Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Chaetomium</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Chaetomium</term><term>Protéines fongiques</term><term>Protéines suppresseurs de tumeurs</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Chaetomium</term><term>Fungal Proteins</term><term>Monomeric GTP-Binding Proteins</term><term>Multiprotein Complexes</term><term>Neuropeptides</term><term>TOR Serine-Threonine Kinases</term><term>Tumor Suppressor Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Chaetomium</term><term>Complexes multiprotéiques</term><term>Neuropeptides</term><term>Protéines G monomériques</term><term>Protéines fongiques</term><term>Protéines suppresseurs de tumeurs</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Chaetomium</term><term>Fungal Proteins</term><term>Monomeric GTP-Binding Proteins</term><term>Multiprotein Complexes</term><term>Neuropeptides</term><term>TOR Serine-Threonine Kinases</term><term>Tumor Suppressor Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chaetomium</term><term>Complexes multiprotéiques</term><term>Neuropeptides</term><term>Protéines G monomériques</term><term>Protéines fongiques</term><term>Protéines suppresseurs de tumeurs</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" xml:lang="en"><term>HEK293 Cells</term><term>Humans</term><term>Mechanistic Target of Rapamycin Complex 1</term><term>Protein Domains</term><term>Ras Homolog Enriched in Brain Protein</term><term>Structural Homology, Protein</term><term>Tuberous Sclerosis</term><term>Tuberous Sclerosis Complex 1 Protein</term><term>Tuberous Sclerosis Complex 2 Protein</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HEK293</term><term>Complexe de la sclérose tubéreuse</term><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Domaines protéiques</term><term>Humains</term><term>Protéine homologue de Ras enrichie dans le cerveau</term><term>Protéine-1 du complexe de la sclérose tubéreuse</term><term>Protéine-2 du complexe de la sclérose tubéreuse</term><term>Similitude structurale de protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Tuberous sclerosis complex (TSC) is caused by mutations in the TSC1 and TSC2 tumor suppressor genes. The gene products hamartin and tuberin form the TSC complex that acts as GTPase-activating protein for Rheb and negatively regulates the mammalian target of rapamycin complex 1 (mTORC1). Tuberin contains a RapGAP homology domain responsible for inactivation of Rheb, but functions of other protein domains remain elusive. Here we show that the TSC2 N terminus interacts with the TSC1 C terminus to mediate complex formation. The structure of the TSC2 N-terminal domain from Chaetomium thermophilum and a homology model of the human tuberin N terminus are presented. We characterize the molecular requirements for TSC1-TSC2 interactions and analyze pathological point mutations in tuberin. Many mutations are structural and produce improperly folded protein, explaining their effect in pathology, but we identify one point mutant that abrogates complex formation without affecting protein structure. We provide the first structural information on TSC2/tuberin with novel insight into the molecular function.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27493206</PMID><DateCompleted><Year>2017</Year><Month>05</Month><Day>12</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>291</Volume><Issue>38</Issue><PubDate><Year>2016</Year><Month>09</Month><Day>16</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Structure of the Tuberous Sclerosis Complex 2 (TSC2) N Terminus Provides Insight into Complex Assembly and Tuberous Sclerosis Pathogenesis.</ArticleTitle><Pagination><MedlinePgn>20008-20</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M116.732446</ELocationID><Abstract><AbstractText>Tuberous sclerosis complex (TSC) is caused by mutations in the TSC1 and TSC2 tumor suppressor genes. The gene products hamartin and tuberin form the TSC complex that acts as GTPase-activating protein for Rheb and negatively regulates the mammalian target of rapamycin complex 1 (mTORC1). Tuberin contains a RapGAP homology domain responsible for inactivation of Rheb, but functions of other protein domains remain elusive. Here we show that the TSC2 N terminus interacts with the TSC1 C terminus to mediate complex formation. The structure of the TSC2 N-terminal domain from Chaetomium thermophilum and a homology model of the human tuberin N terminus are presented. We characterize the molecular requirements for TSC1-TSC2 interactions and analyze pathological point mutations in tuberin. Many mutations are structural and produce improperly folded protein, explaining their effect in pathology, but we identify one point mutant that abrogates complex formation without affecting protein structure. We provide the first structural information on TSC2/tuberin with novel insight into the molecular function.</AbstractText><CopyrightInformation>© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zech</LastName><ForeName>Reinhard</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>From the Structural Biology Section, FB5 Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kiontke</LastName><ForeName>Stephan</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>From the Structural Biology Section, FB5 Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mueller</LastName><ForeName>Uwe</ForeName><Initials>U</Initials><AffiliationInfo><Affiliation>Macromolecular Crystallography (BESSY-MX), Helmholtz-Zentrum Berlin für Materialien und Energie, 12489 Berlin, Germany, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oeckinghaus</LastName><ForeName>Andrea</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institute of Molecular Tumor Biology, Medical Faculty of the WWU Münster, 48149 Münster Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kümmel</LastName><ForeName>Daniel</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>From the Structural Biology Section, FB5 Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany, daniel.kuemmel@uos.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>1XQR</AccessionNumber><AccessionNumber>4KK1</AccessionNumber><AccessionNumber>4UAE</AccessionNumber><AccessionNumber>5HIU</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>08</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009479">Neuropeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C490211">RHEB protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000076205">Ras Homolog Enriched in Brain Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000624650">TSC1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000624653">TSC2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000077004">Tuberous Sclerosis Complex 1 Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000077005">Tuberous Sclerosis Complex 2 Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D025521">Tumor Suppressor Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber><NameOfSubstance UI="D020559">Monomeric GTP-Binding Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002597" MajorTopicYN="N">Chaetomium</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009479" MajorTopicYN="N">Neuropeptides</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein Domains</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000076205" MajorTopicYN="N">Ras Homolog Enriched in Brain Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D040681" MajorTopicYN="N">Structural Homology, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014402" MajorTopicYN="Y">Tuberous 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