Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation
ABSTRACT ATG9 is a membrane protein that is essential for autophagy and is considered to be directly involved in the early steps of autophagosome formation. Yeast Atg9 is mainly localized to small vesicles (Atg9 vesicles), whereas mammalian ATG9A is reportedly localized to the trans‐Golgi network, t...
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| Veröffentlicht in: | The FASEB journal 2017-09, Vol.31 (9), p.3757-3773 |
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| creator | Kakuta, Soichiro Yamaguchi, Junji Suzuki, Chigure Sasaki, Mitsuho Kazuno, Saiko Uchiyama, Yasuo |
| description | ABSTRACT
ATG9 is a membrane protein that is essential for autophagy and is considered to be directly involved in the early steps of autophagosome formation. Yeast Atg9 is mainly localized to small vesicles (Atg9 vesicles), whereas mammalian ATG9A is reportedly localized to the trans‐Golgi network, the endosomal compartment, and other unidentified membrane structures. To dissect the ATG9A‐containing membranes, we examined the subcellular localization of ATG9A and performed immunoisolation of those membranes. ATG9A‐green fluorescent protein in human culture cells was observed as numerous puncta that move rapidly throughout the cytoplasm. We isolated these cytoplasmic membranes and found that they were small vesicles that resemble the yeast Atg9 vesicle. One of the proteins obtained via proteomic analyses of the mammalian ATG9A vesicle was Rab1, a small GTPase that is essential in endoplasmic reticulum‐to‐Golgi vesicle trafficking. Knockdown studies of Rab1B showed a suppression of autophagy. In these Rab1B‐depleted cells, ATG9A accumulated in intermediate membrane structures at autophagosome formation sites. These results indicate that Rab1B is involved in regulating the proper development of autophagosomes.—Kakuta, S., Yamaguchi, J., Suzuki, C., Sasaki, M., Kazuno, S., Uchiyama, Y. Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation. FASEB J. 31, 3757–3773 (2017). www.fasebj.org—Kakuta, Soichiro, Yamaguchi, Junji, Suzuki, Chigure, Sasaki, Mitsuho, Kazuno, Saiko, Uchiyama, Yasuo Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation. FASEB J. 31, 3757–3773 (2017) |
| doi_str_mv | 10.1096/fj.201601052R |
| format | Article |
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ATG9 is a membrane protein that is essential for autophagy and is considered to be directly involved in the early steps of autophagosome formation. Yeast Atg9 is mainly localized to small vesicles (Atg9 vesicles), whereas mammalian ATG9A is reportedly localized to the trans‐Golgi network, the endosomal compartment, and other unidentified membrane structures. To dissect the ATG9A‐containing membranes, we examined the subcellular localization of ATG9A and performed immunoisolation of those membranes. ATG9A‐green fluorescent protein in human culture cells was observed as numerous puncta that move rapidly throughout the cytoplasm. We isolated these cytoplasmic membranes and found that they were small vesicles that resemble the yeast Atg9 vesicle. One of the proteins obtained via proteomic analyses of the mammalian ATG9A vesicle was Rab1, a small GTPase that is essential in endoplasmic reticulum‐to‐Golgi vesicle trafficking. Knockdown studies of Rab1B showed a suppression of autophagy. In these Rab1B‐depleted cells, ATG9A accumulated in intermediate membrane structures at autophagosome formation sites. These results indicate that Rab1B is involved in regulating the proper development of autophagosomes.—Kakuta, S., Yamaguchi, J., Suzuki, C., Sasaki, M., Kazuno, S., Uchiyama, Y. Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation. FASEB J. 31, 3757–3773 (2017). www.fasebj.org—Kakuta, Soichiro, Yamaguchi, Junji, Suzuki, Chigure, Sasaki, Mitsuho, Kazuno, Saiko, Uchiyama, Yasuo Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation. FASEB J. 31, 3757–3773 (2017)</description><identifier>ISSN: 0892-6638</identifier><identifier>EISSN: 1530-6860</identifier><identifier>DOI: 10.1096/fj.201601052R</identifier><identifier>PMID: 28522593</identifier><language>eng</language><publisher>United States: Federation of American Societies for Experimental Biology (FASEB)</publisher><subject>Autophagosomes - physiology ; Autophagy ; Autophagy-Related Proteins - genetics ; Autophagy-Related Proteins - metabolism ; Cell culture ; Cell Membrane - physiology ; Cytoplasm ; Cytoplasmic membranes ; Cytoplasmic Vesicles ; electron microscopy ; Endoplasmic reticulum ; Fluorescence ; Gene Expression Regulation, Enzymologic - physiology ; Golgi apparatus ; Green fluorescent protein ; Guanosine triphosphatases ; HEK293 Cells ; HeLa Cells ; Humans ; Localization ; Mammals ; mass spectrometry ; Membrane proteins ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membrane structures ; Membranes ; Phagocytosis ; Phagosomes ; Protein Transport ; Proteins ; rab1 GTP-Binding Proteins - genetics ; rab1 GTP-Binding Proteins - metabolism ; Vesicles ; Vesicular Transport Proteins - genetics ; Vesicular Transport Proteins - metabolism ; Yeast</subject><ispartof>The FASEB journal, 2017-09, Vol.31 (9), p.3757-3773</ispartof><rights>FASEB</rights><rights>FASEB.</rights><rights>Copyright Federation of American Societies for Experimental Biology (FASEB) Sep 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412R-f1b118486c9a5bd07c98a049e37a199c680d0a262a2400f08dc5471d4410e0513</citedby><cites>FETCH-LOGICAL-c412R-f1b118486c9a5bd07c98a049e37a199c680d0a262a2400f08dc5471d4410e0513</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1096%2Ffj.201601052R$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1096%2Ffj.201601052R$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28522593$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kakuta, Soichiro</creatorcontrib><creatorcontrib>Yamaguchi, Junji</creatorcontrib><creatorcontrib>Suzuki, Chigure</creatorcontrib><creatorcontrib>Sasaki, Mitsuho</creatorcontrib><creatorcontrib>Kazuno, Saiko</creatorcontrib><creatorcontrib>Uchiyama, Yasuo</creatorcontrib><title>Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation</title><title>The FASEB journal</title><addtitle>FASEB J</addtitle><description>ABSTRACT
ATG9 is a membrane protein that is essential for autophagy and is considered to be directly involved in the early steps of autophagosome formation. Yeast Atg9 is mainly localized to small vesicles (Atg9 vesicles), whereas mammalian ATG9A is reportedly localized to the trans‐Golgi network, the endosomal compartment, and other unidentified membrane structures. To dissect the ATG9A‐containing membranes, we examined the subcellular localization of ATG9A and performed immunoisolation of those membranes. ATG9A‐green fluorescent protein in human culture cells was observed as numerous puncta that move rapidly throughout the cytoplasm. We isolated these cytoplasmic membranes and found that they were small vesicles that resemble the yeast Atg9 vesicle. One of the proteins obtained via proteomic analyses of the mammalian ATG9A vesicle was Rab1, a small GTPase that is essential in endoplasmic reticulum‐to‐Golgi vesicle trafficking. Knockdown studies of Rab1B showed a suppression of autophagy. In these Rab1B‐depleted cells, ATG9A accumulated in intermediate membrane structures at autophagosome formation sites. These results indicate that Rab1B is involved in regulating the proper development of autophagosomes.—Kakuta, S., Yamaguchi, J., Suzuki, C., Sasaki, M., Kazuno, S., Uchiyama, Y. Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation. FASEB J. 31, 3757–3773 (2017). www.fasebj.org—Kakuta, Soichiro, Yamaguchi, Junji, Suzuki, Chigure, Sasaki, Mitsuho, Kazuno, Saiko, Uchiyama, Yasuo Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation. FASEB J. 31, 3757–3773 (2017)</description><subject>Autophagosomes - physiology</subject><subject>Autophagy</subject><subject>Autophagy-Related Proteins - genetics</subject><subject>Autophagy-Related Proteins - metabolism</subject><subject>Cell culture</subject><subject>Cell Membrane - physiology</subject><subject>Cytoplasm</subject><subject>Cytoplasmic membranes</subject><subject>Cytoplasmic Vesicles</subject><subject>electron microscopy</subject><subject>Endoplasmic reticulum</subject><subject>Fluorescence</subject><subject>Gene Expression Regulation, Enzymologic - physiology</subject><subject>Golgi apparatus</subject><subject>Green fluorescent protein</subject><subject>Guanosine triphosphatases</subject><subject>HEK293 Cells</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Localization</subject><subject>Mammals</subject><subject>mass spectrometry</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane structures</subject><subject>Membranes</subject><subject>Phagocytosis</subject><subject>Phagosomes</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>rab1 GTP-Binding Proteins - genetics</subject><subject>rab1 GTP-Binding Proteins - metabolism</subject><subject>Vesicles</subject><subject>Vesicular Transport Proteins - genetics</subject><subject>Vesicular Transport Proteins - metabolism</subject><subject>Yeast</subject><issn>0892-6638</issn><issn>1530-6860</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90M9LwzAYxvEgipvTo1cJePFSfd-0zRI8bcNNZaBs8-KlZGm6dbTLbFqH_72R-QsPnkLIhy_hIeQU4RJB8qtsdckAOSDEbLJH2hiHEHDBYZ-0QUgWcB6KFjlybgXgFfJD0mIiZiyWYZs8T0tVFHQ0e1TO0ImaY5_mjirnrM5VbVK6zesl7c1Gskdfjct1YfzzOqWVWTSFF_7W1HazVAvrbGloZqtS1bldH5ODTBXOnHyeHfI0vJkNboPxw-hu0BsHOkI2CTKcI4pIcC1VPE-hq6VQEEkTdhVKqbmAFBTjTLEIIAOR6jjqYhpFCAZiDDvkYtfdVPalMa5OytxpUxRqbWzjEpQAIuxiLDw9_0NXtqnW_ndeiQgEhOFHMNgpXVnnKpMlmyovVfWWICQfoyfZKvkZ3fuzz2ozL036rb9W9uB6B7Z5Yd7-ryXDaZ8N73_l3wEiMYtR</recordid><startdate>201709</startdate><enddate>201709</enddate><creator>Kakuta, Soichiro</creator><creator>Yamaguchi, Junji</creator><creator>Suzuki, Chigure</creator><creator>Sasaki, Mitsuho</creator><creator>Kazuno, Saiko</creator><creator>Uchiyama, Yasuo</creator><general>Federation of American Societies for Experimental Biology (FASEB)</general><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>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>201709</creationdate><title>Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation</title><author>Kakuta, Soichiro ; 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ATG9 is a membrane protein that is essential for autophagy and is considered to be directly involved in the early steps of autophagosome formation. Yeast Atg9 is mainly localized to small vesicles (Atg9 vesicles), whereas mammalian ATG9A is reportedly localized to the trans‐Golgi network, the endosomal compartment, and other unidentified membrane structures. To dissect the ATG9A‐containing membranes, we examined the subcellular localization of ATG9A and performed immunoisolation of those membranes. ATG9A‐green fluorescent protein in human culture cells was observed as numerous puncta that move rapidly throughout the cytoplasm. We isolated these cytoplasmic membranes and found that they were small vesicles that resemble the yeast Atg9 vesicle. One of the proteins obtained via proteomic analyses of the mammalian ATG9A vesicle was Rab1, a small GTPase that is essential in endoplasmic reticulum‐to‐Golgi vesicle trafficking. Knockdown studies of Rab1B showed a suppression of autophagy. In these Rab1B‐depleted cells, ATG9A accumulated in intermediate membrane structures at autophagosome formation sites. These results indicate that Rab1B is involved in regulating the proper development of autophagosomes.—Kakuta, S., Yamaguchi, J., Suzuki, C., Sasaki, M., Kazuno, S., Uchiyama, Y. Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation. FASEB J. 31, 3757–3773 (2017). www.fasebj.org—Kakuta, Soichiro, Yamaguchi, Junji, Suzuki, Chigure, Sasaki, Mitsuho, Kazuno, Saiko, Uchiyama, Yasuo Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation. FASEB J. 31, 3757–3773 (2017)</abstract><cop>United States</cop><pub>Federation of American Societies for Experimental Biology (FASEB)</pub><pmid>28522593</pmid><doi>10.1096/fj.201601052R</doi><tpages>17</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Autophagosomes - physiology Autophagy Autophagy-Related Proteins - genetics Autophagy-Related Proteins - metabolism Cell culture Cell Membrane - physiology Cytoplasm Cytoplasmic membranes Cytoplasmic Vesicles electron microscopy Endoplasmic reticulum Fluorescence Gene Expression Regulation, Enzymologic - physiology Golgi apparatus Green fluorescent protein Guanosine triphosphatases HEK293 Cells HeLa Cells Humans Localization Mammals mass spectrometry Membrane proteins Membrane Proteins - genetics Membrane Proteins - metabolism Membrane structures Membranes Phagocytosis Phagosomes Protein Transport Proteins rab1 GTP-Binding Proteins - genetics rab1 GTP-Binding Proteins - metabolism Vesicles Vesicular Transport Proteins - genetics Vesicular Transport Proteins - metabolism Yeast |
| title | Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation |
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