Modulation of autophagy by RTN-1C: role in autophagosome biogenesis
The endoplasmic reticulum (ER) is a key organelle fundamental for the maintenance of cellular homeostasis and to determine the cell’s fate under stress conditions. Among the known proteins that regulate ER structure and function there is Reticulon-1C (RTN-1C), a member of the reticulon family locali...
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| Veröffentlicht in: | Cell death & disease 2019-11, Vol.10 (12), p.868-14, Article 868 |
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| creator | D’ Eletto, Manuela Risuglia, Anna Oliverio, Serafina Mehdawy, Bisan Nardacci, Roberta Bordi, Matteo Di Sano, Federica |
| description | The endoplasmic reticulum (ER) is a key organelle fundamental for the maintenance of cellular homeostasis and to determine the cell’s fate under stress conditions. Among the known proteins that regulate ER structure and function there is Reticulon-1C (RTN-1C), a member of the reticulon family localized primarily on the ER membrane. We previously demonstrated that RTN-1C expression affects ER function and stress condition. ER is an essential site for the regulation of apoptotic pathways and it has also been recently recognized as an important component of autophagic signaling. Based on these evidences, we have investigated the impact of RTN-1C modulation on autophagy induction. Interestingly we found that reticulon overexpression is able to activate autophagic machinery and its silencing results in a significative inhibition of both basal and induced autophagic response. Using different experimental approaches we demonstrated that RTN-1C colocalizes with ATG16L and LC3II on the autophagosomes. Considering the key role of reticulon proteins in the control of ER membrane shaping and homeostasis, our data suggest the participation of RTN-1C in the autophagic vesicle biogenesis at the level of the ER compartment. Our data indicate a new mechanism by which this structural ER protein modulates cellular stress, that is at the basis of different autophagy-related pathologies. |
| doi_str_mv | 10.1038/s41419-019-2099-7 |
| format | Article |
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Among the known proteins that regulate ER structure and function there is Reticulon-1C (RTN-1C), a member of the reticulon family localized primarily on the ER membrane. We previously demonstrated that RTN-1C expression affects ER function and stress condition. ER is an essential site for the regulation of apoptotic pathways and it has also been recently recognized as an important component of autophagic signaling. Based on these evidences, we have investigated the impact of RTN-1C modulation on autophagy induction. Interestingly we found that reticulon overexpression is able to activate autophagic machinery and its silencing results in a significative inhibition of both basal and induced autophagic response. Using different experimental approaches we demonstrated that RTN-1C colocalizes with ATG16L and LC3II on the autophagosomes. Considering the key role of reticulon proteins in the control of ER membrane shaping and homeostasis, our data suggest the participation of RTN-1C in the autophagic vesicle biogenesis at the level of the ER compartment. Our data indicate a new mechanism by which this structural ER protein modulates cellular stress, that is at the basis of different autophagy-related pathologies.</description><identifier>ISSN: 2041-4889</identifier><identifier>EISSN: 2041-4889</identifier><identifier>DOI: 10.1038/s41419-019-2099-7</identifier><identifier>PMID: 31740665</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13/106 ; 13/89 ; 14/19 ; 14/28 ; 631/80/39 ; 631/80/39/2346 ; 82/29 ; 96/31 ; Antibodies ; Apoptosis ; Autophagosomes - metabolism ; Autophagy ; Autophagy - physiology ; Biochemistry ; Biomedical and Life Sciences ; Biosynthesis ; Cell Biology ; Cell Culture ; Cellular stress response ; Endoplasmic reticulum ; Endoplasmic Reticulum - metabolism ; Homeostasis ; Humans ; Immunology ; Life Sciences ; Nerve Tissue Proteins - genetics ; Organelle Biogenesis ; Phagocytosis ; Phagosomes ; Structure-function relationships</subject><ispartof>Cell death & disease, 2019-11, Vol.10 (12), p.868-14, Article 868</ispartof><rights>The Author(s) 2019</rights><rights>2019. 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Among the known proteins that regulate ER structure and function there is Reticulon-1C (RTN-1C), a member of the reticulon family localized primarily on the ER membrane. We previously demonstrated that RTN-1C expression affects ER function and stress condition. ER is an essential site for the regulation of apoptotic pathways and it has also been recently recognized as an important component of autophagic signaling. Based on these evidences, we have investigated the impact of RTN-1C modulation on autophagy induction. Interestingly we found that reticulon overexpression is able to activate autophagic machinery and its silencing results in a significative inhibition of both basal and induced autophagic response. Using different experimental approaches we demonstrated that RTN-1C colocalizes with ATG16L and LC3II on the autophagosomes. Considering the key role of reticulon proteins in the control of ER membrane shaping and homeostasis, our data suggest the participation of RTN-1C in the autophagic vesicle biogenesis at the level of the ER compartment. 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metabolism</topic><topic>Autophagy</topic><topic>Autophagy - physiology</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Cell Biology</topic><topic>Cell Culture</topic><topic>Cellular stress response</topic><topic>Endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Immunology</topic><topic>Life Sciences</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Organelle Biogenesis</topic><topic>Phagocytosis</topic><topic>Phagosomes</topic><topic>Structure-function relationships</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>D’ Eletto, Manuela</creatorcontrib><creatorcontrib>Risuglia, Anna</creatorcontrib><creatorcontrib>Oliverio, Serafina</creatorcontrib><creatorcontrib>Mehdawy, Bisan</creatorcontrib><creatorcontrib>Nardacci, Roberta</creatorcontrib><creatorcontrib>Bordi, Matteo</creatorcontrib><creatorcontrib>Di Sano, Federica</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>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</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 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>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</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>Science Database</collection><collection>Biological Science Database</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell death & disease</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>D’ Eletto, Manuela</au><au>Risuglia, Anna</au><au>Oliverio, Serafina</au><au>Mehdawy, Bisan</au><au>Nardacci, Roberta</au><au>Bordi, Matteo</au><au>Di Sano, Federica</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modulation of autophagy by RTN-1C: role in autophagosome biogenesis</atitle><jtitle>Cell death & disease</jtitle><stitle>Cell Death Dis</stitle><addtitle>Cell Death Dis</addtitle><date>2019-11-18</date><risdate>2019</risdate><volume>10</volume><issue>12</issue><spage>868</spage><epage>14</epage><pages>868-14</pages><artnum>868</artnum><issn>2041-4889</issn><eissn>2041-4889</eissn><abstract>The endoplasmic reticulum (ER) is a key organelle fundamental for the maintenance of cellular homeostasis and to determine the cell’s fate under stress conditions. Among the known proteins that regulate ER structure and function there is Reticulon-1C (RTN-1C), a member of the reticulon family localized primarily on the ER membrane. We previously demonstrated that RTN-1C expression affects ER function and stress condition. ER is an essential site for the regulation of apoptotic pathways and it has also been recently recognized as an important component of autophagic signaling. Based on these evidences, we have investigated the impact of RTN-1C modulation on autophagy induction. Interestingly we found that reticulon overexpression is able to activate autophagic machinery and its silencing results in a significative inhibition of both basal and induced autophagic response. Using different experimental approaches we demonstrated that RTN-1C colocalizes with ATG16L and LC3II on the autophagosomes. Considering the key role of reticulon proteins in the control of ER membrane shaping and homeostasis, our data suggest the participation of RTN-1C in the autophagic vesicle biogenesis at the level of the ER compartment. Our data indicate a new mechanism by which this structural ER protein modulates cellular stress, that is at the basis of different autophagy-related pathologies.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>31740665</pmid><doi>10.1038/s41419-019-2099-7</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 13/106 13/89 14/19 14/28 631/80/39 631/80/39/2346 82/29 96/31 Antibodies Apoptosis Autophagosomes - metabolism Autophagy Autophagy - physiology Biochemistry Biomedical and Life Sciences Biosynthesis Cell Biology Cell Culture Cellular stress response Endoplasmic reticulum Endoplasmic Reticulum - metabolism Homeostasis Humans Immunology Life Sciences Nerve Tissue Proteins - genetics Organelle Biogenesis Phagocytosis Phagosomes Structure-function relationships |
| title | Modulation of autophagy by RTN-1C: role in autophagosome biogenesis |
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