Mingming Ji, Meng Li, Long Sun, Hongyu Zhao, Ying Li, Lulu Zhou, Zhenni Yang, Xin Zhao, Wenyan Qu, Hanbing Xue, Ze Zheng, Yiming Li, H. Deng, Yan G Zhao
Ji et al. show that the autophagy proteins VMP1 and TMEM41B are required for β-coronavirus infection, and they function at different steps during DMV biogenesis. TMEM41B is involved in nsp3/4 binding and ER zippering, while VMP1 is essential for bending the paired ER into DMVs.
{"title":"VMP1 and TMEM41B are essential for DMV formation during β-coronavirus infection","authors":"Mingming Ji, Meng Li, Long Sun, Hongyu Zhao, Ying Li, Lulu Zhou, Zhenni Yang, Xin Zhao, Wenyan Qu, Hanbing Xue, Ze Zheng, Yiming Li, H. Deng, Yan G Zhao","doi":"10.1083/jcb.202112081","DOIUrl":"https://doi.org/10.1083/jcb.202112081","url":null,"abstract":"Ji et al. show that the autophagy proteins VMP1 and TMEM41B are required for β-coronavirus infection, and they function at different steps during DMV biogenesis. TMEM41B is involved in nsp3/4 binding and ER zippering, while VMP1 is essential for bending the paired ER into DMVs.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"83 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"114856729","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
K. Hooper, E. Jacquin, Taoyingnan Li, Jonathan M Goodwin, J. Brumell, J. Durgan, O. Florey
Hooper et al. report on the role and regulation of V-ATPase in the activation of non-canonical autophagy, including LC3-associated phagocytosis. They reveal new insights into how V-ATPase V0-V1 engagement recruits the autophagy protein ATG16L1 to direct the conjugation of ATG8 to single membranes.
{"title":"V-ATPase is a universal regulator of LC3-associated phagocytosis and non-canonical autophagy","authors":"K. Hooper, E. Jacquin, Taoyingnan Li, Jonathan M Goodwin, J. Brumell, J. Durgan, O. Florey","doi":"10.1083/jcb.202105112","DOIUrl":"https://doi.org/10.1083/jcb.202105112","url":null,"abstract":"Hooper et al. report on the role and regulation of V-ATPase in the activation of non-canonical autophagy, including LC3-associated phagocytosis. They reveal new insights into how V-ATPase V0-V1 engagement recruits the autophagy protein ATG16L1 to direct the conjugation of ATG8 to single membranes.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"785 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"124066609","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Kuo Liu, Hengwei Jin, Muxue Tang, Shaohua Zhang, Xueying Tian, Mingjun Zhang, Ximeng Han, Xiuxiu Liu, Juan Tang, Wenjuan Pu, Yan Li, Lingjuan He, Zhongzhou Yang, K. O. Lui, Bin Zhou
Liu et al. reassess the cellular origin of tissue-resident macrophages in the developing heart. By generating new genetic tools, they reveal that cardiac macrophages are mainly derived from the hemogenic endothelium of yolk sac and aorta-gonad-mesonephros but not from the endocardium.
{"title":"Lineage tracing clarifies the cellular origin of tissue-resident macrophages in the developing heart","authors":"Kuo Liu, Hengwei Jin, Muxue Tang, Shaohua Zhang, Xueying Tian, Mingjun Zhang, Ximeng Han, Xiuxiu Liu, Juan Tang, Wenjuan Pu, Yan Li, Lingjuan He, Zhongzhou Yang, K. O. Lui, Bin Zhou","doi":"10.1083/jcb.202108093","DOIUrl":"https://doi.org/10.1083/jcb.202108093","url":null,"abstract":"Liu et al. reassess the cellular origin of tissue-resident macrophages in the developing heart. By generating new genetic tools, they reveal that cardiac macrophages are mainly derived from the hemogenic endothelium of yolk sac and aorta-gonad-mesonephros but not from the endocardium.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"4 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"124086663","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Tie et al. developed a side-averaging method to visualize the Golgi cisternal organization. They observed the progressive intra-Golgi transport of a synchronized cargo wave. Their data suggest that constitutive cargos might exit at the trans-Golgi instead of the TGN.
{"title":"Visualizing intra-Golgi localization and transport by side-averaging Golgi ministacks","authors":"H. Tie, Divyanshu Mahajan, Lei Lu","doi":"10.1083/jcb.202109114","DOIUrl":"https://doi.org/10.1083/jcb.202109114","url":null,"abstract":"Tie et al. developed a side-averaging method to visualize the Golgi cisternal organization. They observed the progressive intra-Golgi transport of a synchronized cargo wave. Their data suggest that constitutive cargos might exit at the trans-Golgi instead of the TGN.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"49 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"122009799","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Tzu-Jing Yang, Tian-Neng Li, Rih-Sheng Huang, Maxwell Pan, Shu-Yu Lin, Steven Lin, Kuen-Phon Wu, L. Wang, S. Hsu
Yang et al. unravel the molecular mechanism by which the tumor suppressor BAP1 is shuttled into the nucleus by TNPO1. TNPO1 sterically competes with UBE2O for monoubiquitination sites within the nuclear localization sequence of BAP1 to prevent its cytoplasmic retention.
{"title":"Tumor suppressor BAP1 nuclear import is governed by transportin-1","authors":"Tzu-Jing Yang, Tian-Neng Li, Rih-Sheng Huang, Maxwell Pan, Shu-Yu Lin, Steven Lin, Kuen-Phon Wu, L. Wang, S. Hsu","doi":"10.1083/jcb.202201094","DOIUrl":"https://doi.org/10.1083/jcb.202201094","url":null,"abstract":"Yang et al. unravel the molecular mechanism by which the tumor suppressor BAP1 is shuttled into the nucleus by TNPO1. TNPO1 sterically competes with UBE2O for monoubiquitination sites within the nuclear localization sequence of BAP1 to prevent its cytoplasmic retention.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"7 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"114171344","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ofer Guttman, Adrien Le Thomas, S. Marsters, D. Lawrence, Lauren M. Gutgesell, Iratxe Zuazo-Gaztelu, J. Harnoss, S. M. Haag, A. Murthy, G. Strasser, Z. Modrušan, Thomas Wu, I. Mellman, A. Ashkenazi
Antigen cross-presenting dendritic cells (DCs) activate the ER stress sensor IRE1α without ER stress. Guttman et al. show that antigen-derived ER-imported peptides can directly engage IRE1α. Regulated IRE1α-dependent MHC-I mRNA decay curbs DC cross-presentation, while IRE1α inhibition augments antitumor immunity.
{"title":"Antigen-derived peptides engage the ER stress sensor IRE1α to curb dendritic cell cross-presentation","authors":"Ofer Guttman, Adrien Le Thomas, S. Marsters, D. Lawrence, Lauren M. Gutgesell, Iratxe Zuazo-Gaztelu, J. Harnoss, S. M. Haag, A. Murthy, G. Strasser, Z. Modrušan, Thomas Wu, I. Mellman, A. Ashkenazi","doi":"10.1083/jcb.202111068","DOIUrl":"https://doi.org/10.1083/jcb.202111068","url":null,"abstract":"Antigen cross-presenting dendritic cells (DCs) activate the ER stress sensor IRE1α without ER stress. Guttman et al. show that antigen-derived ER-imported peptides can directly engage IRE1α. Regulated IRE1α-dependent MHC-I mRNA decay curbs DC cross-presentation, while IRE1α inhibition augments antitumor immunity.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"20 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"116744650","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
T. Solvik, Tan A Nguyen, Yu-Hsiu Tony Lin, Timothy Marsh, E. Huang, A. Wiita, Jayanta Debnath, Andrew M. Leidal
Solvik et al. reveal that the autophagy machinery facilitates the secretion of autophagy cargo receptors and other cellular components via extracellular vesicles and particles in response to lysosome inhibition or impaired autophagosome maturation.
{"title":"Secretory autophagy maintains proteostasis upon lysosome inhibition","authors":"T. Solvik, Tan A Nguyen, Yu-Hsiu Tony Lin, Timothy Marsh, E. Huang, A. Wiita, Jayanta Debnath, Andrew M. Leidal","doi":"10.1083/jcb.202110151","DOIUrl":"https://doi.org/10.1083/jcb.202110151","url":null,"abstract":"Solvik et al. reveal that the autophagy machinery facilitates the secretion of autophagy cargo receptors and other cellular components via extracellular vesicles and particles in response to lysosome inhibition or impaired autophagosome maturation.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"211 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"122420069","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
S. Matsumoto, S. Ono, Saori Shinoda, Chika Kakuta, S. Okada, Takashi Ito, T. Numata, T. Endo
Tail-anchored (TA) membrane proteins mistargeted to mitochondria are extracted by Msp1 and then transferred to the ER for further quality control. Matsumoto, Ono, et al. show that this retransfer of mistargeted TA proteins requires the operation of the GET system.
{"title":"GET pathway mediates transfer of mislocalized tail-anchored proteins from mitochondria to the ER","authors":"S. Matsumoto, S. Ono, Saori Shinoda, Chika Kakuta, S. Okada, Takashi Ito, T. Numata, T. Endo","doi":"10.1083/jcb.202104076","DOIUrl":"https://doi.org/10.1083/jcb.202104076","url":null,"abstract":"Tail-anchored (TA) membrane proteins mistargeted to mitochondria are extracted by Msp1 and then transferred to the ER for further quality control. Matsumoto, Ono, et al. show that this retransfer of mistargeted TA proteins requires the operation of the GET system.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"25 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"131657106","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Lena Ho studies small ORF-encoded peptides (SEPs; also known as micropeptides), with a particular focus on mitochondrial SEPs, and their role in vascular biology and immunometabolism.
Lena Ho研究小orf编码肽(sep);也称为微肽)，特别关注线粒体sep及其在血管生物学和免疫代谢中的作用。
{"title":"Lena Ho: Micropeptides under the spotlight","authors":"Lucia Morgado-Palacin","doi":"10.1083/jcb.202204038","DOIUrl":"https://doi.org/10.1083/jcb.202204038","url":null,"abstract":"Lena Ho studies small ORF-encoded peptides (SEPs; also known as micropeptides), with a particular focus on mitochondrial SEPs, and their role in vascular biology and immunometabolism.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"44 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"124801394","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-04-15DOI: 10.1101/2022.04.14.488376
Grant A. King, Rahel Wettstein, Joseph M. Varberg, Keerthana Chetlapalli, M. E. Walsh, Ludovic C. Gillet, Claudia Hernandez-Armenta, P. Beltrão, R. Aebersold, S. Jaspersen, Joao Matos, E. Ünal
Nuclear pore complexes (NPCs) are large proteinaceous assemblies that mediate nuclear compartmentalization. NPCs undergo largescale structural rearrangements during mitosis in metazoans and some fungi. However, our understanding of NPC remodeling beyond mitosis remains limited. Using time-lapse fluorescence microscopy, we discovered that NPCs undergo two mechanistically-separable remodeling events during budding yeast meiosis whereby parts or all of the nuclear basket transiently dissociate from the NPC core during meiosis I and II, respectively. Meiosis I detachment, observed for Nup60 and Nup2, is driven by Polo kinase-mediated phosphorylation of Nup60 at its interface with the Y-complex. Subsequent reattachment of Nup60-Nup2 to the NPC core is mediated by a lipid-binding amphipathic helix in Nup60. Preventing Nup60-Nup2 reattachment causes misorganization of the entire nuclear basket in gametes. Strikingly, meiotic nuclear basket remodeling also occurs in the distantly related fission yeast, Schizosaccharomyces pombe. Our study reveals a conserved and developmentally programmed aspect of NPC plasticity, providing key mechanistic insights into nuclear basket organization. SUMMARY King and Wettstein et al. reveal that nuclear pore complexes undergo two distinct remodeling events during budding yeast meiosis: partial and full nuclear basket detachment. By dissecting the regulation of these events, the study provides mechanistic insights into NPC organization.
{"title":"Meiotic nuclear pore complex remodeling provides key insights into nuclear basket organization","authors":"Grant A. King, Rahel Wettstein, Joseph M. Varberg, Keerthana Chetlapalli, M. E. Walsh, Ludovic C. Gillet, Claudia Hernandez-Armenta, P. Beltrão, R. Aebersold, S. Jaspersen, Joao Matos, E. Ünal","doi":"10.1101/2022.04.14.488376","DOIUrl":"https://doi.org/10.1101/2022.04.14.488376","url":null,"abstract":"Nuclear pore complexes (NPCs) are large proteinaceous assemblies that mediate nuclear compartmentalization. NPCs undergo largescale structural rearrangements during mitosis in metazoans and some fungi. However, our understanding of NPC remodeling beyond mitosis remains limited. Using time-lapse fluorescence microscopy, we discovered that NPCs undergo two mechanistically-separable remodeling events during budding yeast meiosis whereby parts or all of the nuclear basket transiently dissociate from the NPC core during meiosis I and II, respectively. Meiosis I detachment, observed for Nup60 and Nup2, is driven by Polo kinase-mediated phosphorylation of Nup60 at its interface with the Y-complex. Subsequent reattachment of Nup60-Nup2 to the NPC core is mediated by a lipid-binding amphipathic helix in Nup60. Preventing Nup60-Nup2 reattachment causes misorganization of the entire nuclear basket in gametes. Strikingly, meiotic nuclear basket remodeling also occurs in the distantly related fission yeast, Schizosaccharomyces pombe. Our study reveals a conserved and developmentally programmed aspect of NPC plasticity, providing key mechanistic insights into nuclear basket organization. SUMMARY King and Wettstein et al. reveal that nuclear pore complexes undergo two distinct remodeling events during budding yeast meiosis: partial and full nuclear basket detachment. By dissecting the regulation of these events, the study provides mechanistic insights into NPC organization.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"81 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"121080202","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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