RapamycinFungusV1, Main, Exploration, bibRecord, 000E28

Rab1A is an mTORC1 activator and a colorectal oncogene.

Identifieur interne : 000E28 ( Main/Exploration ); précédent : 000E27; suivant : 000E29

Rab1A is an mTORC1 activator and a colorectal oncogene.

Auteurs : Janice D. Thomas [États-Unis] ; Yan-Jie Zhang [République populaire de Chine] ; Yue-Hua Wei [États-Unis] ; Jun-Hung Cho [États-Unis] ; Laura E. Morris [États-Unis] ; Hui-Yun Wang [République populaire de Chine] ; X F Steven Zheng [République populaire de Chine]

Source :

Cancer cell [ 1878-3686 ] ; 2014.

RBID : pubmed:25446900

Descripteurs français

English descriptors

KwdEn :
- Amino Acids (physiology), Animals (MeSH), Antibiotics, Antineoplastic (pharmacology), Cell Line, Tumor (MeSH), Cell Proliferation (MeSH), Colorectal Neoplasms (drug therapy), Colorectal Neoplasms (metabolism), Colorectal Neoplasms (pathology), Female (MeSH), Gene Expression (MeSH), HEK293 Cells (MeSH), Humans (MeSH), MAP Kinase Kinase Kinases (metabolism), Mechanistic Target of Rapamycin Complex 1 (MeSH), Mice (MeSH), Mice, Inbred BALB C (MeSH), Mice, Nude (MeSH), Multiprotein Complexes (metabolism), NIH 3T3 Cells (MeSH), Neoplasm Invasiveness (MeSH), Oncogenes (MeSH), Phosphatidylinositol 3-Kinases (metabolism), Saccharomyces cerevisiae (MeSH), Saccharomyces cerevisiae Proteins (metabolism), Saccharomyces cerevisiae Proteins (physiology), Signal Transduction (MeSH), Sirolimus (pharmacology), TOR Serine-Threonine Kinases (metabolism), Transcription Factors (metabolism), Tumor Burden (drug effects), Xenograft Model Antitumor Assays (MeSH), rab GTP-Binding Proteins (physiology), rab1 GTP-Binding Proteins (physiology).
MESH :
- chemical , metabolism : MAP Kinase Kinase Kinases, Multiprotein Complexes, Phosphatidylinositol 3-Kinases, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases, Transcription Factors.
- chemical , pharmacology : Antibiotics, Antineoplastic, Sirolimus.
- chemical , physiology : Amino Acids, Saccharomyces cerevisiae Proteins, rab GTP-Binding Proteins, rab1 GTP-Binding Proteins.
- drug effects : Tumor Burden.
- drug therapy : Colorectal Neoplasms.
- metabolism : Colorectal Neoplasms.
- pathology : Colorectal Neoplasms.
- Animals, Cell Line, Tumor, Cell Proliferation, Female, Gene Expression, HEK293 Cells, Humans, Mechanistic Target of Rapamycin Complex 1, Mice, Mice, Inbred BALB C, Mice, Nude, NIH 3T3 Cells, Neoplasm Invasiveness, Oncogenes, Saccharomyces cerevisiae, Signal Transduction, Xenograft Model Antitumor Assays.

Abstract

Amino acid (AA) is a potent mitogen that controls growth and metabolism. Here we describe the identification of Rab1 as a conserved regulator of AA signaling to mTORC1. AA stimulates Rab1A GTP binding and interaction with mTORC1 and Rheb-mTORC1 interaction in the Golgi. Rab1A overexpression promotes mTORC1 signaling and oncogenic growth in an AA- and mTORC1-dependent manner. Conversely, Rab1A knockdown selectively attenuates oncogenic growth of Rab1-overexpressing cancer cells. Moreover, Rab1A is overexpressed in colorectal cancer (CRC), which is correlated with elevated mTORC1 signaling, tumor invasion, progression, and poor prognosis. Our results demonstrate that Rab1 is an mTORC1 activator and an oncogene and that hyperactive AA signaling through Rab1A overexpression drives oncogenesis and renders cancer cells prone to mTORC1-targeted therapy.

DOI: 10.1016/j.ccell.2014.09.008
PubMed: 25446900
PubMed Central: PMC4288827

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000D48
to stream Main, to step Curation: 000D48

Le document en format XML

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<term>Animals (MeSH)</term>
<term>Antibiotics, Antineoplastic (pharmacology)</term>
<term>Cell Line, Tumor (MeSH)</term>
<term>Cell Proliferation (MeSH)</term>
<term>Colorectal Neoplasms (drug therapy)</term>
<term>Colorectal Neoplasms (metabolism)</term>
<term>Colorectal Neoplasms (pathology)</term>
<term>Female (MeSH)</term>
<term>Gene Expression (MeSH)</term>
<term>HEK293 Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>MAP Kinase Kinase Kinases (metabolism)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term>
<term>Mice (MeSH)</term>
<term>Mice, Inbred BALB C (MeSH)</term>
<term>Mice, Nude (MeSH)</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>NIH 3T3 Cells (MeSH)</term>
<term>Neoplasm Invasiveness (MeSH)</term>
<term>Oncogenes (MeSH)</term>
<term>Phosphatidylinositol 3-Kinases (metabolism)</term>
<term>Saccharomyces cerevisiae (MeSH)</term>
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<term>Saccharomyces cerevisiae Proteins (physiology)</term>
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<term>TOR Serine-Threonine Kinases (metabolism)</term>
<term>Transcription Factors (metabolism)</term>
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<term>rab1 GTP-Binding Proteins (physiology)</term>
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<term>Cellules NIH 3T3 (MeSH)</term>
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<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (physiologie)</term>
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<term>Souris (MeSH)</term>
<term>Souris de lignée BALB C (MeSH)</term>
<term>Souris nude (MeSH)</term>
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<term>Transduction du signal (MeSH)</term>
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<term>Tumeurs colorectales (métabolisme)</term>
<term>Tumeurs colorectales (traitement médicamenteux)</term>
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<term>Phosphatidylinositol 3-Kinases</term>
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<term>Female</term>
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<term>Oncogenes</term>
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<term>Xenograft Model Antitumor Assays</term>
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<term>Cellules NIH 3T3</term>
<term>Complexe-1 cible mécanistique de la rapamycine</term>
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<term>Souris de lignée BALB C</term>
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<front><div type="abstract" xml:lang="en">Amino acid (AA) is a potent mitogen that controls growth and metabolism. Here we describe the identification of Rab1 as a conserved regulator of AA signaling to mTORC1. AA stimulates Rab1A GTP binding and interaction with mTORC1 and Rheb-mTORC1 interaction in the Golgi. Rab1A overexpression promotes mTORC1 signaling and oncogenic growth in an AA- and mTORC1-dependent manner. Conversely, Rab1A knockdown selectively attenuates oncogenic growth of Rab1-overexpressing cancer cells. Moreover, Rab1A is overexpressed in colorectal cancer (CRC), which is correlated with elevated mTORC1 signaling, tumor invasion, progression, and poor prognosis. Our results demonstrate that Rab1 is an mTORC1 activator and an oncogene and that hyperactive AA signaling through Rab1A overexpression drives oncogenesis and renders cancer cells prone to mTORC1-targeted therapy. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25446900</PMID>
<DateCompleted><Year>2015</Year>
<Month>02</Month>
<Day>09</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1878-3686</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>26</Volume>
<Issue>5</Issue>
<PubDate><Year>2014</Year>
<Month>Nov</Month>
<Day>10</Day>
</PubDate>
</JournalIssue>
<Title>Cancer cell</Title>
<ISOAbbreviation>Cancer Cell</ISOAbbreviation>
</Journal>
<ArticleTitle>Rab1A is an mTORC1 activator and a colorectal oncogene.</ArticleTitle>
<Pagination><MedlinePgn>754-69</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ccell.2014.09.008</ELocationID>
<ELocationID EIdType="pii" ValidYN="Y">S1535-6108(14)00371-7</ELocationID>
<Abstract><AbstractText>Amino acid (AA) is a potent mitogen that controls growth and metabolism. Here we describe the identification of Rab1 as a conserved regulator of AA signaling to mTORC1. AA stimulates Rab1A GTP binding and interaction with mTORC1 and Rheb-mTORC1 interaction in the Golgi. Rab1A overexpression promotes mTORC1 signaling and oncogenic growth in an AA- and mTORC1-dependent manner. Conversely, Rab1A knockdown selectively attenuates oncogenic growth of Rab1-overexpressing cancer cells. Moreover, Rab1A is overexpressed in colorectal cancer (CRC), which is correlated with elevated mTORC1 signaling, tumor invasion, progression, and poor prognosis. Our results demonstrate that Rab1 is an mTORC1 activator and an oncogene and that hyperactive AA signaling through Rab1A overexpression drives oncogenesis and renders cancer cells prone to mTORC1-targeted therapy. </AbstractText>
<CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Thomas</LastName>
<ForeName>Janice D</ForeName>
<Initials>JD</Initials>
<AffiliationInfo><Affiliation>Rutgers Cancer Institute of New Jersey, Rutgers, The State University of New Jersey, 195 Little Albany Street, New Brunswick, NJ 08903, USA; Department of Pharmacology, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, 675 Hoes Lane, Piscataway, NJ 08854, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Yan-Jie</ForeName>
<Initials>YJ</Initials>
<AffiliationInfo><Affiliation>Rutgers Cancer Institute of New Jersey, Rutgers, The State University of New Jersey, 195 Little Albany Street, New Brunswick, NJ 08903, USA; Department of Pharmacology, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, 675 Hoes Lane, Piscataway, NJ 08854, USA; Department of Gastroenterology, No. 3 People's Hospital Affiliated to Shanghai Jiaotong University School of Medicine, Shanghai 201900, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wei</LastName>
<ForeName>Yue-Hua</ForeName>
<Initials>YH</Initials>
<AffiliationInfo><Affiliation>Cellular and Molecular Pharmacology Graduate Program, Rutgers, The State University of New Jersey, 675 Hoes Lane, Piscataway, NJ 08854, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cho</LastName>
<ForeName>Jun-Hung</ForeName>
<Initials>JH</Initials>
<AffiliationInfo><Affiliation>Cellular and Molecular Pharmacology Graduate Program, Rutgers, The State University of New Jersey, 675 Hoes Lane, Piscataway, NJ 08854, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Morris</LastName>
<ForeName>Laura E</ForeName>
<Initials>LE</Initials>
<AffiliationInfo><Affiliation>Cellular and Molecular Pharmacology Graduate Program, Rutgers, The State University of New Jersey, 675 Hoes Lane, Piscataway, NJ 08854, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Hui-Yun</ForeName>
<Initials>HY</Initials>
<AffiliationInfo><Affiliation>Rutgers Cancer Institute of New Jersey, Rutgers, The State University of New Jersey, 195 Little Albany Street, New Brunswick, NJ 08903, USA; Department of Pharmacology, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, 675 Hoes Lane, Piscataway, NJ 08854, USA; Sun Yat-Sen University Cancer Center, National Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Guangzhou 510060, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zheng</LastName>
<ForeName>X F Steven</ForeName>
<Initials>XF</Initials>
<AffiliationInfo><Affiliation>Rutgers Cancer Institute of New Jersey, Rutgers, The State University of New Jersey, 195 Little Albany Street, New Brunswick, NJ 08903, USA; Department of Pharmacology, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, 675 Hoes Lane, Piscataway, NJ 08854, USA; Sun Yat-Sen University Cancer Center, National Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Guangzhou 510060, China. Electronic address: zhengst@cinj.rutgers.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 CA173519</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 CA166575</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>CA173519</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>P30 CA072720</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>CA123391</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 CA123391</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI 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>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2014</Year>
<Month>10</Month>
<Day>23</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Cancer Cell</MedlineTA>
<NlmUniqueID>101130617</NlmUniqueID>
<ISSNLinking>1535-6108</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000903">Antibiotics, Antineoplastic</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C561842">TORC1 protein complex, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber>
<NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</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 2.7.11.25</RegistryNumber>
<NameOfSubstance UI="D020930">MAP Kinase Kinase Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber>
<NameOfSubstance UI="C060755">YPT1 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber>
<NameOfSubstance UI="D020691">rab GTP-Binding Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber>
<NameOfSubstance UI="D020761">rab1 GTP-Binding Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber>
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<CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Cancer Cell. 2014 Nov 10;26(5):601-3</RefSource>
<PMID Version="1">25517745</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="ErratumIn"><RefSource>Cancer Cell. 2016 Jul 11;30(1):181-182</RefSource>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000903" MajorTopicYN="N">Antibiotics, Antineoplastic</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D049109" MajorTopicYN="N">Cell Proliferation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015179" MajorTopicYN="N">Colorectal Neoplasms</DescriptorName>
<QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020930" MajorTopicYN="N">MAP Kinase Kinase Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008807" MajorTopicYN="N">Mice, Inbred BALB C</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008819" MajorTopicYN="N">Mice, Nude</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D041681" MajorTopicYN="N">NIH 3T3 Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009361" MajorTopicYN="N">Neoplasm Invasiveness</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009857" MajorTopicYN="N">Oncogenes</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
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<MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName>
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<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
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<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
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<MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D047368" MajorTopicYN="N">Tumor Burden</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D023041" MajorTopicYN="N">Xenograft Model Antitumor Assays</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020691" MajorTopicYN="N">rab GTP-Binding Proteins</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
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<MeshHeading><DescriptorName UI="D020761" MajorTopicYN="N">rab1 GTP-Binding Proteins</DescriptorName>
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Rab1A is an mTORC1 activator and a colorectal oncogene.

Rab1A is an mTORC1 activator and a colorectal oncogene.

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