Sensors for the mTORC1 pathway regulated by amino acids.
Identifieur interne : 000165 ( Main/Exploration ); précédent : 000164; suivant : 000166Sensors for the mTORC1 pathway regulated by amino acids.
Auteurs : Xiu-Zhi Li [République populaire de Chine] ; Xiang-Hua Yan [République populaire de Chine]Source :
- Journal of Zhejiang University. Science. B [ 1862-1783 ]
Descripteurs français
- KwdFr :
- Acides aminés (composition chimique), Adémétionine (composition chimique), Animaux (MeSH), Appareil de Golgi (métabolisme), Arginine (composition chimique), Complexe-1 cible mécanistique de la rapamycine (métabolisme), Humains (MeSH), Leucine (composition chimique), Lysosomes (métabolisme), Membrane cellulaire (métabolisme), Méthionine (composition chimique), Régulation de l'expression des gènes (MeSH), Sérine-thréonine kinases TOR (métabolisme), Transduction du signal (MeSH), dGTPases (métabolisme).
- MESH :
- composition chimique : Acides aminés, Adémétionine, Arginine, Leucine, Méthionine.
- métabolisme : Appareil de Golgi, Complexe-1 cible mécanistique de la rapamycine, Lysosomes, Membrane cellulaire, Sérine-thréonine kinases TOR, dGTPases.
- Animaux, Humains, Régulation de l'expression des gènes, Transduction du signal.
English descriptors
- KwdEn :
- Amino Acids (chemistry), Animals (MeSH), Arginine (chemistry), Cell Membrane (metabolism), GTP Phosphohydrolases (metabolism), Gene Expression Regulation (MeSH), Golgi Apparatus (metabolism), Humans (MeSH), Leucine (chemistry), Lysosomes (metabolism), Mechanistic Target of Rapamycin Complex 1 (metabolism), Methionine (chemistry), S-Adenosylmethionine (chemistry), Signal Transduction (MeSH), TOR Serine-Threonine Kinases (metabolism).
- MESH :
- chemical , chemistry : Amino Acids, Arginine, Leucine, Methionine, S-Adenosylmethionine.
- metabolism : Cell Membrane, GTP Phosphohydrolases, Golgi Apparatus, Lysosomes, Mechanistic Target of Rapamycin Complex 1, TOR Serine-Threonine Kinases.
- Animals, Gene Expression Regulation, Humans, Signal Transduction.
Abstract
The mechanistic target of rapamycin complex 1 (mTORC1) controls cell growth and metabolism in response to various environmental inputs, especially amino acids. In fact, the activity of mTORC1 is highly sensitive to changes in amino acid levels. Over past decades, a variety of proteins have been identified as participating in the mTORC1 pathway regulated by amino acids. Classically, the Rag guanosine triphosphatases (GTPases), which reside on the lysosome, transmit amino acid availability to the mTORC1 pathway and recruit mTORC1 to the lysosome upon amino acid sufficiency. Recently, several sensors of leucine, arginine, and S-adenosylmethionine for the amino acid-stimulated mTORC1 pathway have been coming to light. Characterization of these sensors is requisite for understanding how cells adjust amino acid sensing pathways to their different needs. In this review, we summarize recent advances in amino acid sensing mechanisms that regulate mTORC1 activity and highlight these identified sensors that accurately transmit specific amino acid signals to the mTORC1 pathway.
DOI: 10.1631/jzus.B1900181
PubMed: 31379141
PubMed Central: PMC6700350
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070</wicri:regionArea><placeName><settlement type="city">Wuhan</settlement><region type="région">Hubei</region></placeName></affiliation><affiliation wicri:level="1"><nlm:affiliation>Hubei Provincial Engineering Laboratory for Pig Precision Feeding and Feed Safety Technology, Wuhan 430070, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Hubei Provincial Engineering Laboratory for Pig Precision Feeding and Feed Safety Technology, Wuhan 430070</wicri:regionArea><placeName><settlement type="city">Wuhan</settlement><region type="région">Hubei</region></placeName></affiliation></author><author><name sortKey="Yan, Xiang Hua" sort="Yan, Xiang Hua" uniqKey="Yan X" first="Xiang-Hua" last="Yan">Xiang-Hua Yan</name><affiliation wicri:level="1"><nlm:affiliation>State Key Laboratory of Agricultural Microbiology, College of Animal Sciences and Technology, Huazhong Agricultural University, Wuhan 430070, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>State Key Laboratory of Agricultural Microbiology, College of Animal Sciences and Technology, Huazhong Agricultural University, Wuhan 430070</wicri:regionArea><placeName><settlement type="city">Wuhan</settlement><region type="région">Hubei</region></placeName></affiliation><affiliation wicri:level="1"><nlm:affiliation>The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070</wicri:regionArea><placeName><settlement type="city">Wuhan</settlement><region type="région">Hubei</region></placeName></affiliation><affiliation 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Science. B</title><idno type="eISSN">1862-1783</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acids (chemistry)</term><term>Animals (MeSH)</term><term>Arginine (chemistry)</term><term>Cell Membrane (metabolism)</term><term>GTP Phosphohydrolases (metabolism)</term><term>Gene Expression Regulation (MeSH)</term><term>Golgi Apparatus (metabolism)</term><term>Humans (MeSH)</term><term>Leucine (chemistry)</term><term>Lysosomes (metabolism)</term><term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term><term>Methionine (chemistry)</term><term>S-Adenosylmethionine (chemistry)</term><term>Signal Transduction (MeSH)</term><term>TOR Serine-Threonine Kinases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (composition chimique)</term><term>Adémétionine (composition chimique)</term><term>Animaux (MeSH)</term><term>Appareil de Golgi (métabolisme)</term><term>Arginine (composition chimique)</term><term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term><term>Humains (MeSH)</term><term>Leucine (composition chimique)</term><term>Lysosomes (métabolisme)</term><term>Membrane cellulaire (métabolisme)</term><term>Méthionine (composition chimique)</term><term>Régulation de l'expression des gènes (MeSH)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term><term>Transduction du signal (MeSH)</term><term>dGTPases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term><term>Arginine</term><term>Leucine</term><term>Methionine</term><term>S-Adenosylmethionine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acides aminés</term><term>Adémétionine</term><term>Arginine</term><term>Leucine</term><term>Méthionine</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>GTP Phosphohydrolases</term><term>Golgi Apparatus</term><term>Lysosomes</term><term>Mechanistic Target of Rapamycin Complex 1</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil de Golgi</term><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Lysosomes</term><term>Membrane cellulaire</term><term>Sérine-thréonine kinases TOR</term><term>dGTPases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Gene Expression Regulation</term><term>Humans</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Régulation de l'expression des gènes</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The mechanistic target of rapamycin complex 1 (mTORC1) controls cell growth and metabolism in response to various environmental inputs, especially amino acids. In fact, the activity of mTORC1 is highly sensitive to changes in amino acid levels. Over past decades, a variety of proteins have been identified as participating in the mTORC1 pathway regulated by amino acids. Classically, the Rag guanosine triphosphatases (GTPases), which reside on the lysosome, transmit amino acid availability to the mTORC1 pathway and recruit mTORC1 to the lysosome upon amino acid sufficiency. Recently, several sensors of leucine, arginine, and S-adenosylmethionine for the amino acid-stimulated mTORC1 pathway have been coming to light. Characterization of these sensors is requisite for understanding how cells adjust amino acid sensing pathways to their different needs. In this review, we summarize recent advances in amino acid sensing mechanisms that regulate mTORC1 activity and highlight these identified sensors that accurately transmit specific amino acid signals to the mTORC1 pathway.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31379141</PMID><DateCompleted><Year>2020</Year><Month>02</Month><Day>20</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1862-1783</ISSN><JournalIssue CitedMedium="Internet"><Volume>20</Volume><Issue>9</Issue><PubDate><MedlineDate>2019 Sept.</MedlineDate></PubDate></JournalIssue><Title>Journal of Zhejiang University. Science. B</Title><ISOAbbreviation>J Zhejiang Univ Sci B</ISOAbbreviation></Journal><ArticleTitle>Sensors for the mTORC1 pathway regulated by amino acids.</ArticleTitle><Pagination><MedlinePgn>699-712</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1631/jzus.B1900181</ELocationID><Abstract><AbstractText>The mechanistic target of rapamycin complex 1 (mTORC1) controls cell growth and metabolism in response to various environmental inputs, especially amino acids. In fact, the activity of mTORC1 is highly sensitive to changes in amino acid levels. Over past decades, a variety of proteins have been identified as participating in the mTORC1 pathway regulated by amino acids. Classically, the Rag guanosine triphosphatases (GTPases), which reside on the lysosome, transmit amino acid availability to the mTORC1 pathway and recruit mTORC1 to the lysosome upon amino acid sufficiency. Recently, several sensors of leucine, arginine, and S-adenosylmethionine for the amino acid-stimulated mTORC1 pathway have been coming to light. Characterization of these sensors is requisite for understanding how cells adjust amino acid sensing pathways to their different needs. In this review, we summarize recent advances in amino acid sensing mechanisms that regulate mTORC1 activity and highlight these identified sensors that accurately transmit specific amino acid signals to the mTORC1 pathway.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Xiu-Zhi</ForeName><Initials>XZ</Initials><AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Animal Sciences and Technology, Huazhong Agricultural University, Wuhan 430070, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Hubei Provincial Engineering Laboratory for Pig Precision Feeding and Feed Safety Technology, Wuhan 430070, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yan</LastName><ForeName>Xiang-Hua</ForeName><Initials>XH</Initials><AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Animal Sciences and Technology, Huazhong Agricultural University, Wuhan 430070, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Hubei Provincial Engineering Laboratory for Pig Precision Feeding and Feed Safety Technology, Wuhan 430070, China.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>China</Country><MedlineTA>J Zhejiang Univ Sci B</MedlineTA><NlmUniqueID>101236535</NlmUniqueID><ISSNLinking>1673-1581</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>7LP2MPO46S</RegistryNumber><NameOfSubstance UI="D012436">S-Adenosylmethionine</NameOfSubstance></Chemical><Chemical><RegistryNumber>94ZLA3W45F</RegistryNumber><NameOfSubstance UI="D001120">Arginine</NameOfSubstance></Chemical><Chemical><RegistryNumber>AE28F7PNPL</RegistryNumber><NameOfSubstance UI="D008715">Methionine</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 3.6.1.-</RegistryNumber><NameOfSubstance UI="D020558">GTP Phosphohydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GMW67QNF9C</RegistryNumber><NameOfSubstance UI="D007930">Leucine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001120" MajorTopicYN="N">Arginine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020558" MajorTopicYN="N">GTP Phosphohydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006056" MajorTopicYN="N">Golgi Apparatus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007930" MajorTopicYN="N">Leucine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008247" MajorTopicYN="N">Lysosomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008715" MajorTopicYN="N">Methionine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012436" MajorTopicYN="N">S-Adenosylmethionine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Mechanistic target of rapamycin complex 1 (mTORC1); Amino acid; Sensor; Lysosome; Rag GTPases</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate 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