Regulation of mATG9 trafficking by Src- and ULK1-mediated phosphorylation in basal and starvation-induced autophagy
Autophagy requires diverse membrane sources and involves membrane trafficking of mATG9, the only membrane protein in the ATG family. However, the molecular regulation of mATG9 trafficking for autophagy initiation remains unclear. Here we identified two conserved classic adaptor protein sorting signa...
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| Veröffentlicht in: | Cell research 2017-02, Vol.27 (2), p.184-201 |
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| creator | Zhou, Changqian Ma, Kaili Gao, Ruize Mu, Chenglong Chen, Linbo Liu, Qiangqiang Luo, Qian Feng, Du Zhu, Yushan Chen, Quan |
| description | Autophagy requires diverse membrane sources and involves membrane trafficking of mATG9, the only membrane protein in the ATG family. However, the molecular regulation of mATG9 trafficking for autophagy initiation remains unclear. Here we identified two conserved classic adaptor protein sorting signals within the cytosolic N-terminus of mATG9, which mediate trafficking of mATG9 from the plasma membrane and trans-Golgi network (TGN) via interaction with the AP1/2 complex. Src phosphorylates mATG9 at Tyr8 to maintain its endocytic and constitutive trafficking in unstressed conditions. In response to starvation, phosphorylation of mATG9 at Tyr8 by Src and at Ser14 by ULK1 functionally cooperate to promote interactions between mATG9 and the AP1/2 complex, leading to redistribution of mATG9 from the plasma membrane and juxta-nuclear region to the peripheral pool for autophagy initiation. Our findings uncover novel mechanisms of mATG9 trafficking and suggest a coordination of basal and stress-induced autophagy. |
| doi_str_mv | 10.1038/cr.2016.146 |
| format | Article |
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However, the molecular regulation of mATG9 trafficking for autophagy initiation remains unclear. Here we identified two conserved classic adaptor protein sorting signals within the cytosolic N-terminus of mATG9, which mediate trafficking of mATG9 from the plasma membrane and trans-Golgi network (TGN) via interaction with the AP1/2 complex. Src phosphorylates mATG9 at Tyr8 to maintain its endocytic and constitutive trafficking in unstressed conditions. In response to starvation, phosphorylation of mATG9 at Tyr8 by Src and at Ser14 by ULK1 functionally cooperate to promote interactions between mATG9 and the AP1/2 complex, leading to redistribution of mATG9 from the plasma membrane and juxta-nuclear region to the peripheral pool for autophagy initiation. Our findings uncover novel mechanisms of mATG9 trafficking and suggest a coordination of basal and stress-induced autophagy.</description><identifier>ISSN: 1001-0602</identifier><identifier>EISSN: 1748-7838</identifier><identifier>DOI: 10.1038/cr.2016.146</identifier><identifier>PMID: 27934868</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/80/313 ; 631/80/458/1733 ; 631/80/82/39 ; 631/80/86 ; Amino Acid Sequence ; Autophagy - drug effects ; Autophagy-Related Protein-1 Homolog - metabolism ; Autophagy-Related Proteins - chemistry ; Autophagy-Related Proteins - metabolism ; Biomedical and Life Sciences ; Cell Biology ; Cell Membrane - metabolism ; Conserved Sequence ; Epidermal Growth Factor - pharmacology ; HEK293 Cells ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins - metabolism ; Life Sciences ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Membranes ; Original ; original-article ; Phosphorylation - drug effects ; Phosphotyrosine - metabolism ; Protein Transport - drug effects ; src-Family Kinases - metabolism ; Starvation - metabolism ; Starvation - pathology ; Stress, Physiological - drug effects ; Vesicular Transport Proteins - chemistry ; Vesicular Transport Proteins - metabolism</subject><ispartof>Cell research, 2017-02, Vol.27 (2), p.184-201</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group Feb 2017</rights><rights>Copyright © 2016 Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences 2016 Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c545t-6d38175e177b4787cdcc591be53cf9ecc08517177a601892def53861c19770bf3</citedby><cites>FETCH-LOGICAL-c545t-6d38175e177b4787cdcc591be53cf9ecc08517177a601892def53861c19770bf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5339848/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5339848/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,41464,42533,51294,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27934868$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhou, Changqian</creatorcontrib><creatorcontrib>Ma, Kaili</creatorcontrib><creatorcontrib>Gao, Ruize</creatorcontrib><creatorcontrib>Mu, Chenglong</creatorcontrib><creatorcontrib>Chen, Linbo</creatorcontrib><creatorcontrib>Liu, Qiangqiang</creatorcontrib><creatorcontrib>Luo, Qian</creatorcontrib><creatorcontrib>Feng, Du</creatorcontrib><creatorcontrib>Zhu, Yushan</creatorcontrib><creatorcontrib>Chen, Quan</creatorcontrib><title>Regulation of mATG9 trafficking by Src- and ULK1-mediated phosphorylation in basal and starvation-induced autophagy</title><title>Cell research</title><addtitle>Cell Res</addtitle><addtitle>Cell Res</addtitle><description>Autophagy requires diverse membrane sources and involves membrane trafficking of mATG9, the only membrane protein in the ATG family. However, the molecular regulation of mATG9 trafficking for autophagy initiation remains unclear. Here we identified two conserved classic adaptor protein sorting signals within the cytosolic N-terminus of mATG9, which mediate trafficking of mATG9 from the plasma membrane and trans-Golgi network (TGN) via interaction with the AP1/2 complex. Src phosphorylates mATG9 at Tyr8 to maintain its endocytic and constitutive trafficking in unstressed conditions. In response to starvation, phosphorylation of mATG9 at Tyr8 by Src and at Ser14 by ULK1 functionally cooperate to promote interactions between mATG9 and the AP1/2 complex, leading to redistribution of mATG9 from the plasma membrane and juxta-nuclear region to the peripheral pool for autophagy initiation. Our findings uncover novel mechanisms of mATG9 trafficking and suggest a coordination of basal and stress-induced autophagy.</description><subject>631/80/313</subject><subject>631/80/458/1733</subject><subject>631/80/82/39</subject><subject>631/80/86</subject><subject>Amino Acid Sequence</subject><subject>Autophagy - drug effects</subject><subject>Autophagy-Related Protein-1 Homolog - metabolism</subject><subject>Autophagy-Related Proteins - chemistry</subject><subject>Autophagy-Related Proteins - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Cell Membrane - metabolism</subject><subject>Conserved Sequence</subject><subject>Epidermal Growth Factor - pharmacology</subject><subject>HEK293 Cells</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins - metabolism</subject><subject>Life Sciences</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>Original</subject><subject>original-article</subject><subject>Phosphorylation - drug effects</subject><subject>Phosphotyrosine - metabolism</subject><subject>Protein Transport - drug effects</subject><subject>src-Family Kinases - metabolism</subject><subject>Starvation - metabolism</subject><subject>Starvation - pathology</subject><subject>Stress, Physiological - drug effects</subject><subject>Vesicular Transport Proteins - chemistry</subject><subject>Vesicular Transport Proteins - metabolism</subject><issn>1001-0602</issn><issn>1748-7838</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNptkd1r2zAUxUXpWLp2T30vgr4UNme6lm3JL4MStrYsUFibZyHLsqPWkTLJDuS_r_Kx0JY-CAndn849VwehcyBjIJT_UH6cEijGkBVH6ARYxhPGKT-OZ0IgIQVJR-hLCE-EpHmWw2c0SllJM17wExT-6nboZG-cxa7Bi-vHmxL3XjaNUc_Gtrha4wevEixtjWfTP5AsdG1kr2u8nLsQl1_vnxuLKxlkt0VDL_1qe58YWw8q8nLo3XIu2_UZ-tTILuiv-_0UzX7_epzcJtP7m7vJ9TRR0WafFDXlwHINjFUZ40zVSuUlVDqnqim1UoTnwGJVFgR4mda6ySkvQEHJGKkaeop-7nSXQxVdK23jYJ1YerOQfi2cNOJtxZq5aN1K5JSWPONR4Gov4N2_QYdeLExQuuuk1W4IAuIXUpqSkkT08h365AZv43gbKss4B7qhvu0o5V0IXjcHM0DEJkyhvNiEKWKYkb547f_A_k8vAt93QIgl22r_qukHei9Kz6ls</recordid><startdate>20170201</startdate><enddate>20170201</enddate><creator>Zhou, Changqian</creator><creator>Ma, Kaili</creator><creator>Gao, Ruize</creator><creator>Mu, Chenglong</creator><creator>Chen, Linbo</creator><creator>Liu, Qiangqiang</creator><creator>Luo, Qian</creator><creator>Feng, Du</creator><creator>Zhu, Yushan</creator><creator>Chen, Quan</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20170201</creationdate><title>Regulation of mATG9 trafficking by Src- and ULK1-mediated phosphorylation in basal and starvation-induced autophagy</title><author>Zhou, Changqian ; Ma, Kaili ; Gao, Ruize ; Mu, Chenglong ; Chen, Linbo ; Liu, Qiangqiang ; Luo, Qian ; Feng, Du ; Zhu, Yushan ; Chen, Quan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c545t-6d38175e177b4787cdcc591be53cf9ecc08517177a601892def53861c19770bf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>631/80/313</topic><topic>631/80/458/1733</topic><topic>631/80/82/39</topic><topic>631/80/86</topic><topic>Amino Acid Sequence</topic><topic>Autophagy - 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drug effects</topic><topic>Vesicular Transport Proteins - chemistry</topic><topic>Vesicular Transport Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhou, Changqian</creatorcontrib><creatorcontrib>Ma, Kaili</creatorcontrib><creatorcontrib>Gao, Ruize</creatorcontrib><creatorcontrib>Mu, Chenglong</creatorcontrib><creatorcontrib>Chen, Linbo</creatorcontrib><creatorcontrib>Liu, Qiangqiang</creatorcontrib><creatorcontrib>Luo, Qian</creatorcontrib><creatorcontrib>Feng, Du</creatorcontrib><creatorcontrib>Zhu, Yushan</creatorcontrib><creatorcontrib>Chen, Quan</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhou, Changqian</au><au>Ma, Kaili</au><au>Gao, Ruize</au><au>Mu, Chenglong</au><au>Chen, Linbo</au><au>Liu, Qiangqiang</au><au>Luo, Qian</au><au>Feng, Du</au><au>Zhu, Yushan</au><au>Chen, Quan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of mATG9 trafficking by Src- and ULK1-mediated phosphorylation in basal and starvation-induced autophagy</atitle><jtitle>Cell research</jtitle><stitle>Cell Res</stitle><addtitle>Cell Res</addtitle><date>2017-02-01</date><risdate>2017</risdate><volume>27</volume><issue>2</issue><spage>184</spage><epage>201</epage><pages>184-201</pages><issn>1001-0602</issn><eissn>1748-7838</eissn><abstract>Autophagy requires diverse membrane sources and involves membrane trafficking of mATG9, the only membrane protein in the ATG family. However, the molecular regulation of mATG9 trafficking for autophagy initiation remains unclear. Here we identified two conserved classic adaptor protein sorting signals within the cytosolic N-terminus of mATG9, which mediate trafficking of mATG9 from the plasma membrane and trans-Golgi network (TGN) via interaction with the AP1/2 complex. Src phosphorylates mATG9 at Tyr8 to maintain its endocytic and constitutive trafficking in unstressed conditions. In response to starvation, phosphorylation of mATG9 at Tyr8 by Src and at Ser14 by ULK1 functionally cooperate to promote interactions between mATG9 and the AP1/2 complex, leading to redistribution of mATG9 from the plasma membrane and juxta-nuclear region to the peripheral pool for autophagy initiation. Our findings uncover novel mechanisms of mATG9 trafficking and suggest a coordination of basal and stress-induced autophagy.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>27934868</pmid><doi>10.1038/cr.2016.146</doi><tpages>18</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/80/313 631/80/458/1733 631/80/82/39 631/80/86 Amino Acid Sequence Autophagy - drug effects Autophagy-Related Protein-1 Homolog - metabolism Autophagy-Related Proteins - chemistry Autophagy-Related Proteins - metabolism Biomedical and Life Sciences Cell Biology Cell Membrane - metabolism Conserved Sequence Epidermal Growth Factor - pharmacology HEK293 Cells HeLa Cells Humans Intracellular Signaling Peptides and Proteins - metabolism Life Sciences Membrane Proteins - chemistry Membrane Proteins - metabolism Membranes Original original-article Phosphorylation - drug effects Phosphotyrosine - metabolism Protein Transport - drug effects src-Family Kinases - metabolism Starvation - metabolism Starvation - pathology Stress, Physiological - drug effects Vesicular Transport Proteins - chemistry Vesicular Transport Proteins - metabolism |
| title | Regulation of mATG9 trafficking by Src- and ULK1-mediated phosphorylation in basal and starvation-induced autophagy |
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