The Birt-Hogg-Dube and tuberous sclerosis complex homologs have opposing roles in amino acid homeostasis in Schizosaccharomyces pombe.
Identifieur interne : 001671 ( Main/Exploration ); précédent : 001670; suivant : 001672The Birt-Hogg-Dube and tuberous sclerosis complex homologs have opposing roles in amino acid homeostasis in Schizosaccharomyces pombe.
Auteurs : Marjon Van Slegtenhorst [États-Unis] ; Damir Khabibullin ; Tiffiney R. Hartman ; Emmanuelle Nicolas ; Warren D. Kruger ; Elizabeth Petri HenskeSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2007.
Descripteurs français
- KwdFr :
- Acides aminés (métabolisme), Allèles (MeSH), Animaux (MeSH), Canavanine (pharmacologie), Données de séquences moléculaires (MeSH), Humains (MeSH), Modèles biologiques (MeSH), Phénotype (MeSH), Protéine-1 du complexe de la sclérose tubéreuse (MeSH), Protéines (génétique), Protéines de Schizosaccharomyces pombe (génétique), Protéines de Schizosaccharomyces pombe (physiologie), Protéines proto-oncogènes (génétique), Protéines suppresseurs de tumeurs (génétique), Protéines suppresseurs de tumeurs (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Schizosaccharomyces (génétique), Schizosaccharomyces (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Éthionine (pharmacologie).
- MESH :
- génétique : Protéines, Protéines de Schizosaccharomyces pombe, Protéines proto-oncogènes, Protéines suppresseurs de tumeurs, Schizosaccharomyces.
- métabolisme : Acides aminés, Protéines suppresseurs de tumeurs, Schizosaccharomyces.
- pharmacologie : Canavanine, Éthionine.
- physiologie : Protéines de Schizosaccharomyces pombe.
- Allèles, Animaux, Données de séquences moléculaires, Humains, Modèles biologiques, Phénotype, Protéine-1 du complexe de la sclérose tubéreuse, Régulation de l'expression des gènes fongiques, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Alleles (MeSH), Amino Acid Sequence (MeSH), Amino Acids (metabolism), Animals (MeSH), Canavanine (pharmacology), Ethionine (pharmacology), Gene Expression Regulation, Fungal (MeSH), Humans (MeSH), Models, Biological (MeSH), Molecular Sequence Data (MeSH), Phenotype (MeSH), Proteins (genetics), Proto-Oncogene Proteins (genetics), Schizosaccharomyces (genetics), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (physiology), Sequence Homology, Amino Acid (MeSH), Tuberous Sclerosis Complex 1 Protein (MeSH), Tumor Suppressor Proteins (genetics), Tumor Suppressor Proteins (metabolism).
- MESH :
- chemical , genetics : Proteins, Proto-Oncogene Proteins, Schizosaccharomyces pombe Proteins, Tumor Suppressor Proteins.
- chemical , metabolism : Amino Acids, Tumor Suppressor Proteins.
- chemical , pharmacology : Canavanine, Ethionine.
- genetics : Schizosaccharomyces.
- metabolism : Schizosaccharomyces.
- chemical , physiology : Schizosaccharomyces pombe Proteins.
- Alleles, Amino Acid Sequence, Animals, Gene Expression Regulation, Fungal, Humans, Models, Biological, Molecular Sequence Data, Phenotype, Sequence Homology, Amino Acid, Tuberous Sclerosis Complex 1 Protein.
Abstract
Birt-Hogg-Dube (BHD) is a tumor suppressor gene disorder characterized by skin hamartomas, cystic lung disease, and renal cell carcinoma. The fact that hamartomas, lung cysts, and renal cell carcinoma can also occur in tuberous sclerosis complex (TSC) suggests that the BHD and TSC proteins may function within a common pathway. To evaluate this hypothesis, we deleted the BHD homolog in Schizosaccharomyces pombe. Expression profiling revealed that six permease and transporter genes, known to be down-regulated in Deltatsc1 and Deltatsc2, were up-regulated in Deltabhd, and levels of specific intracellular amino acids known to be low in Deltatsc1 and Deltatsc2 were elevated in Deltabhd. This "opposite" profile was unexpected, given the overlapping clinical phenotypes. The TSC1/2 proteins inhibit Rheb in mammals, and Tsc1/Tsc2 inhibit Rhb1 in S. pombe. Expression of a hypomorphic allele of rhb1(+) dramatically increased permease expression levels in Deltabhd but not in wild-type yeast. Loss of Bhd sensitized yeast to rapamycin-induced increases in permease expression levels, and rapamycin induced lethality in Deltabhd yeast expressing the hypomorphic Rhb1 allele. In S. pombe, it is known that Rhb1 binds Tor2, and Tor2 inhibition leads to up-regulation of permeases including those that are regulated by Bhd. Our data, therefore, suggest that Bhd activates Tor2. If the mammalian BHD protein, folliculin, similarly activates mammalian target of rapamycin, it will be of great interest to determine how mammalian target of rapamycin inhibition in BHD patients and mammalian target of rapamycin activation in TSC patients lead to overlapping clinical phenotypes.
DOI: 10.1074/jbc.M700857200
PubMed: 17556368
Affiliations:
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Le document en format XML
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The fact that hamartomas, lung cysts, and renal cell carcinoma can also occur in tuberous sclerosis complex (TSC) suggests that the BHD and TSC proteins may function within a common pathway. To evaluate this hypothesis, we deleted the BHD homolog in Schizosaccharomyces pombe. Expression profiling revealed that six permease and transporter genes, known to be down-regulated in Deltatsc1 and Deltatsc2, were up-regulated in Deltabhd, and levels of specific intracellular amino acids known to be low in Deltatsc1 and Deltatsc2 were elevated in Deltabhd. This "opposite" profile was unexpected, given the overlapping clinical phenotypes. The TSC1/2 proteins inhibit Rheb in mammals, and Tsc1/Tsc2 inhibit Rhb1 in S. pombe. Expression of a hypomorphic allele of rhb1(+) dramatically increased permease expression levels in Deltabhd but not in wild-type yeast. Loss of Bhd sensitized yeast to rapamycin-induced increases in permease expression levels, and rapamycin induced lethality in Deltabhd yeast expressing the hypomorphic Rhb1 allele. In S. pombe, it is known that Rhb1 binds Tor2, and Tor2 inhibition leads to up-regulation of permeases including those that are regulated by Bhd. Our data, therefore, suggest that Bhd activates Tor2. If the mammalian BHD protein, folliculin, similarly activates mammalian target of rapamycin, it will be of great interest to determine how mammalian target of rapamycin inhibition in BHD patients and mammalian target of rapamycin activation in TSC patients lead to overlapping clinical phenotypes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17556368</PMID><DateCompleted><Year>2007</Year><Month>10</Month><Day>11</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>282</Volume><Issue>34</Issue><PubDate><Year>2007</Year><Month>Aug</Month><Day>24</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>The Birt-Hogg-Dube and tuberous sclerosis complex homologs have opposing roles in amino acid homeostasis in Schizosaccharomyces pombe.</ArticleTitle><Pagination><MedlinePgn>24583-90</MedlinePgn></Pagination><Abstract><AbstractText>Birt-Hogg-Dube (BHD) is a tumor suppressor gene disorder characterized by skin hamartomas, cystic lung disease, and renal cell carcinoma. The fact that hamartomas, lung cysts, and renal cell carcinoma can also occur in tuberous sclerosis complex (TSC) suggests that the BHD and TSC proteins may function within a common pathway. To evaluate this hypothesis, we deleted the BHD homolog in Schizosaccharomyces pombe. Expression profiling revealed that six permease and transporter genes, known to be down-regulated in Deltatsc1 and Deltatsc2, were up-regulated in Deltabhd, and levels of specific intracellular amino acids known to be low in Deltatsc1 and Deltatsc2 were elevated in Deltabhd. This "opposite" profile was unexpected, given the overlapping clinical phenotypes. The TSC1/2 proteins inhibit Rheb in mammals, and Tsc1/Tsc2 inhibit Rhb1 in S. pombe. Expression of a hypomorphic allele of rhb1(+) dramatically increased permease expression levels in Deltabhd but not in wild-type yeast. Loss of Bhd sensitized yeast to rapamycin-induced increases in permease expression levels, and rapamycin induced lethality in Deltabhd yeast expressing the hypomorphic Rhb1 allele. In S. pombe, it is known that Rhb1 binds Tor2, and Tor2 inhibition leads to up-regulation of permeases including those that are regulated by Bhd. Our data, therefore, suggest that Bhd activates Tor2. If the mammalian BHD protein, folliculin, similarly activates mammalian target of rapamycin, it will be of great interest to determine how mammalian target of rapamycin inhibition in BHD patients and mammalian target of rapamycin activation in TSC patients lead to overlapping clinical phenotypes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>van Slegtenhorst</LastName><ForeName>Marjon</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Khabibullin</LastName><ForeName>Damir</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Hartman</LastName><ForeName>Tiffiney R</ForeName><Initials>TR</Initials></Author><Author ValidYN="Y"><LastName>Nicolas</LastName><ForeName>Emmanuelle</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Kruger</LastName><ForeName>Warren D</ForeName><Initials>WD</Initials></Author><Author ValidYN="Y"><LastName>Henske</LastName><ForeName>Elizabeth Petri</ForeName><Initials>EP</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R21 HL82746</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>06</Month><Day>07</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="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C476078">FLCN protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011518">Proto-Oncogene Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029702">Schizosaccharomyces pombe Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000624650">TSC1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000077004">Tuberous Sclerosis Complex 1 Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D025521">Tumor Suppressor Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C523312">bhd1 protein, S pombe</NameOfSubstance></Chemical><Chemical><RegistryNumber>3HZV514J4B</RegistryNumber><NameOfSubstance UI="D002172">Canavanine</NameOfSubstance></Chemical><Chemical><RegistryNumber>WX1BN24WZT</RegistryNumber><NameOfSubstance UI="D005001">Ethionine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000483" MajorTopicYN="N">Alleles</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002172" MajorTopicYN="N">Canavanine</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005001" MajorTopicYN="N">Ethionine</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="Y">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011518" MajorTopicYN="N">Proto-Oncogene Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029702" MajorTopicYN="N">Schizosaccharomyces pombe Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000077004" MajorTopicYN="N">Tuberous Sclerosis Complex 1 Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025521" MajorTopicYN="N">Tumor Suppressor 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