Constitutive Tor2 Activity Promotes Retention of the Amino Acid Transporter Agp3 at Trans-Golgi/Endosomes in Fission Yeast.
Identifieur interne : 000B68 ( Main/Corpus ); précédent : 000B67; suivant : 000B69Constitutive Tor2 Activity Promotes Retention of the Amino Acid Transporter Agp3 at Trans-Golgi/Endosomes in Fission Yeast.
Auteurs : Qingbin Liu ; Yan Ma ; Xin Zhou ; Tomoyuki FuruyashikiSource :
- PloS one [ 1932-6203 ] ; 2015.
English descriptors
- KwdEn :
- Amino Acid Transport Systems (metabolism), Endosomes (metabolism), Golgi Apparatus (metabolism), Nitrogen (metabolism), Phosphatidylinositol 3-Kinases (metabolism), Protein Transport (MeSH), Schizosaccharomyces (cytology), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (metabolism).
- MESH :
- chemical , metabolism : Amino Acid Transport Systems, Nitrogen, Phosphatidylinositol 3-Kinases, Schizosaccharomyces pombe Proteins.
- cytology : Schizosaccharomyces.
- metabolism : Endosomes, Golgi Apparatus, Schizosaccharomyces.
- Protein Transport.
Abstract
Amino acid transporters are located at specific subcellular compartments, and their localizations are regulated by the extracellular availability of amino acids. In yeast, target of rapamycin (TOR) activation induces the internalization of amino acid transporters located at the plasma membrane. However, whether and how TOR signaling regulates other amino acid transporters located at intracellular compartments remains unknown. Here, we demonstrate that in the fission yeast, the TOR inhibitor Torin-1 induces the transfer of several yellow fluorescent protein (YFP)-fused intracellular amino acid transporters, including Agp3, Isp5, Aat1, and Put4, from trans-Golgi/endosomes into the vacuoles. By contrast, the localizations of YFP-fused Can1, Fnx1, and Fnx2 transporter proteins were unaffected upon Torin-1 treatment. There are two TOR isoforms in fission yeast, Tor1 and Tor2. Whereas tor1 deletion did not affect the Torin-1-induced transfer of Agp3-YFP, Tor2 inhibition using a temperature-sensitive mutant induced the transfer of Agp3-YFP to the vacuolar lumen, similar to the effects of Torin-1 treatment. Tor2 inhibition also induced the transfer of the YFP-fused Isp5, Aat1, and Put4 transporter proteins to the vacuoles, although only partial transfer of the latter two transporters was observed. Under nitrogen depletion accompanied by reduced Tor2 activity, Agp3-YFP was transferred from the trans-Golgi/endosomes to the plasma membrane and then to the vacuoles, where it was degraded by the vacuolar proteases Isp6 and Psp3. Mutants with constitutively active Tor2 showed delayed transfer of Agp3-YFP to the plasma membrane upon nitrogen depletion. Cells lacking Tsc2, a negative regulator of Tor2, also showed a delay in this process in a Tor2-dependent manner. Taken together, these findings suggest that constitutive Tor2 activity is critical for the retention of amino acid transporters at trans-Golgi/endosomes. Moreover, nitrogen depletion suppresses Tor2 activity through Tsc2, thereby promoting the surface expression of these transporters.
DOI: 10.1371/journal.pone.0139045
PubMed: 26447710
PubMed Central: PMC4598100
Links to Exploration step
pubmed:26447710Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Constitutive Tor2 Activity Promotes Retention of the Amino Acid Transporter Agp3 at Trans-Golgi/Endosomes in Fission Yeast.</title><author><name sortKey="Liu, Qingbin" sort="Liu, Qingbin" uniqKey="Liu Q" first="Qingbin" last="Liu">Qingbin Liu</name><affiliation><nlm:affiliation>Division of Pharmacology, Kobe University Graduate School of Medicine, Kobe, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Ma, Yan" sort="Ma, Yan" uniqKey="Ma Y" first="Yan" last="Ma">Yan Ma</name><affiliation><nlm:affiliation>Division of Pharmacology, Kobe University Graduate School of Medicine, Kobe, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Xin" sort="Zhou, Xin" uniqKey="Zhou X" first="Xin" last="Zhou">Xin Zhou</name><affiliation><nlm:affiliation>Department of Oncology, the First Affiliated Hospital of Liaoning Medical University, Jinzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Furuyashiki, Tomoyuki" sort="Furuyashiki, Tomoyuki" uniqKey="Furuyashiki T" first="Tomoyuki" last="Furuyashiki">Tomoyuki Furuyashiki</name><affiliation><nlm:affiliation>Division of Pharmacology, Kobe University Graduate School of Medicine, Kobe, Japan.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26447710</idno><idno type="pmid">26447710</idno><idno type="doi">10.1371/journal.pone.0139045</idno><idno type="pmc">PMC4598100</idno><idno type="wicri:Area/Main/Corpus">000B68</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B68</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Constitutive Tor2 Activity Promotes Retention of the Amino Acid Transporter Agp3 at Trans-Golgi/Endosomes in Fission Yeast.</title><author><name sortKey="Liu, Qingbin" sort="Liu, Qingbin" uniqKey="Liu Q" first="Qingbin" last="Liu">Qingbin Liu</name><affiliation><nlm:affiliation>Division of Pharmacology, Kobe University Graduate School of Medicine, Kobe, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Ma, Yan" sort="Ma, Yan" uniqKey="Ma Y" first="Yan" last="Ma">Yan Ma</name><affiliation><nlm:affiliation>Division of Pharmacology, Kobe University Graduate School of Medicine, Kobe, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Xin" sort="Zhou, Xin" uniqKey="Zhou X" first="Xin" last="Zhou">Xin Zhou</name><affiliation><nlm:affiliation>Department of Oncology, the First Affiliated Hospital of Liaoning Medical University, Jinzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Furuyashiki, Tomoyuki" sort="Furuyashiki, Tomoyuki" uniqKey="Furuyashiki T" first="Tomoyuki" last="Furuyashiki">Tomoyuki Furuyashiki</name><affiliation><nlm:affiliation>Division of Pharmacology, Kobe University Graduate School of Medicine, Kobe, Japan.</nlm:affiliation></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Transport Systems (metabolism)</term><term>Endosomes (metabolism)</term><term>Golgi Apparatus (metabolism)</term><term>Nitrogen (metabolism)</term><term>Phosphatidylinositol 3-Kinases (metabolism)</term><term>Protein Transport (MeSH)</term><term>Schizosaccharomyces (cytology)</term><term>Schizosaccharomyces (metabolism)</term><term>Schizosaccharomyces pombe Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acid Transport Systems</term><term>Nitrogen</term><term>Phosphatidylinositol 3-Kinases</term><term>Schizosaccharomyces pombe Proteins</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endosomes</term><term>Golgi Apparatus</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Transport</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Amino acid transporters are located at specific subcellular compartments, and their localizations are regulated by the extracellular availability of amino acids. In yeast, target of rapamycin (TOR) activation induces the internalization of amino acid transporters located at the plasma membrane. However, whether and how TOR signaling regulates other amino acid transporters located at intracellular compartments remains unknown. Here, we demonstrate that in the fission yeast, the TOR inhibitor Torin-1 induces the transfer of several yellow fluorescent protein (YFP)-fused intracellular amino acid transporters, including Agp3, Isp5, Aat1, and Put4, from trans-Golgi/endosomes into the vacuoles. By contrast, the localizations of YFP-fused Can1, Fnx1, and Fnx2 transporter proteins were unaffected upon Torin-1 treatment. There are two TOR isoforms in fission yeast, Tor1 and Tor2. Whereas tor1 deletion did not affect the Torin-1-induced transfer of Agp3-YFP, Tor2 inhibition using a temperature-sensitive mutant induced the transfer of Agp3-YFP to the vacuolar lumen, similar to the effects of Torin-1 treatment. Tor2 inhibition also induced the transfer of the YFP-fused Isp5, Aat1, and Put4 transporter proteins to the vacuoles, although only partial transfer of the latter two transporters was observed. Under nitrogen depletion accompanied by reduced Tor2 activity, Agp3-YFP was transferred from the trans-Golgi/endosomes to the plasma membrane and then to the vacuoles, where it was degraded by the vacuolar proteases Isp6 and Psp3. Mutants with constitutively active Tor2 showed delayed transfer of Agp3-YFP to the plasma membrane upon nitrogen depletion. Cells lacking Tsc2, a negative regulator of Tor2, also showed a delay in this process in a Tor2-dependent manner. Taken together, these findings suggest that constitutive Tor2 activity is critical for the retention of amino acid transporters at trans-Golgi/endosomes. Moreover, nitrogen depletion suppresses Tor2 activity through Tsc2, thereby promoting the surface expression of these transporters. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26447710</PMID><DateCompleted><Year>2016</Year><Month>06</Month><Day>07</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>10</Issue><PubDate><Year>2015</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Constitutive Tor2 Activity Promotes Retention of the Amino Acid Transporter Agp3 at Trans-Golgi/Endosomes in Fission Yeast.</ArticleTitle><Pagination><MedlinePgn>e0139045</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0139045</ELocationID><Abstract><AbstractText>Amino acid transporters are located at specific subcellular compartments, and their localizations are regulated by the extracellular availability of amino acids. In yeast, target of rapamycin (TOR) activation induces the internalization of amino acid transporters located at the plasma membrane. However, whether and how TOR signaling regulates other amino acid transporters located at intracellular compartments remains unknown. Here, we demonstrate that in the fission yeast, the TOR inhibitor Torin-1 induces the transfer of several yellow fluorescent protein (YFP)-fused intracellular amino acid transporters, including Agp3, Isp5, Aat1, and Put4, from trans-Golgi/endosomes into the vacuoles. By contrast, the localizations of YFP-fused Can1, Fnx1, and Fnx2 transporter proteins were unaffected upon Torin-1 treatment. There are two TOR isoforms in fission yeast, Tor1 and Tor2. Whereas tor1 deletion did not affect the Torin-1-induced transfer of Agp3-YFP, Tor2 inhibition using a temperature-sensitive mutant induced the transfer of Agp3-YFP to the vacuolar lumen, similar to the effects of Torin-1 treatment. Tor2 inhibition also induced the transfer of the YFP-fused Isp5, Aat1, and Put4 transporter proteins to the vacuoles, although only partial transfer of the latter two transporters was observed. Under nitrogen depletion accompanied by reduced Tor2 activity, Agp3-YFP was transferred from the trans-Golgi/endosomes to the plasma membrane and then to the vacuoles, where it was degraded by the vacuolar proteases Isp6 and Psp3. Mutants with constitutively active Tor2 showed delayed transfer of Agp3-YFP to the plasma membrane upon nitrogen depletion. Cells lacking Tsc2, a negative regulator of Tor2, also showed a delay in this process in a Tor2-dependent manner. Taken together, these findings suggest that constitutive Tor2 activity is critical for the retention of amino acid transporters at trans-Golgi/endosomes. Moreover, nitrogen depletion suppresses Tor2 activity through Tsc2, thereby promoting the surface expression of these transporters. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Qingbin</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Division of Pharmacology, Kobe University Graduate School of Medicine, Kobe, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Yan</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Division of Pharmacology, Kobe University Graduate School of Medicine, Kobe, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhou</LastName><ForeName>Xin</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Department of Oncology, the First Affiliated Hospital of Liaoning Medical University, Jinzhou, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Furuyashiki</LastName><ForeName>Tomoyuki</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Division of Pharmacology, Kobe University Graduate School of Medicine, Kobe, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>10</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000608141">Agp3 protein, S pombe</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026905">Amino Acid Transport 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