Yichen Wang, Lin Jia, Cong Wang, Zhonghua Du, Shilin Zhang, Lei Zhou, Xue Wen, Hui Li, Huiling Chen, Yuanyuan Nie, Dan Li, Shanshan Liu, Daniela Salgado Figueroa, Ferhat Ay, Wei Xu, Songling Zhang, Wei Li, Jiuwei Cui, Andrew R Hoffman, Hui Guo, Ji-Fan Hu
{"title":"Pluripotency exit is guided by the Peln1-mediated disruption of intrachromosomal architecture.","authors":"Yichen Wang, Lin Jia, Cong Wang, Zhonghua Du, Shilin Zhang, Lei Zhou, Xue Wen, Hui Li, Huiling Chen, Yuanyuan Nie, Dan Li, Shanshan Liu, Daniela Salgado Figueroa, Ferhat Ay, Wei Xu, Songling Zhang, Wei Li, Jiuwei Cui, Andrew R Hoffman, Hui Guo, Ji-Fan Hu","doi":"10.1083/jcb.202009134","DOIUrl":"https://doi.org/10.1083/jcb.202009134","url":null,"abstract":"<p><p>The molecular circuitry that causes stem cells to exit from pluripotency remains largely uncharacterized. Using chromatin RNA in situ reverse transcription sequencing, we identified Peln1 as a novel chromatin RNA component in the promoter complex of Oct4, a stem cell master transcription factor gene. Peln1 was negatively associated with pluripotent status during somatic reprogramming. Peln1 overexpression caused E14 cells to exit from pluripotency, while Peln1 downregulation induced robust reprogramming. Mechanistically, we discovered that Peln1 interacted with the Oct4 promoter and recruited the DNA methyltransferase DNMT3A. By de novo altering the epigenotype in the Oct4 promoter, Peln1 dismantled the intrachromosomal loop that is required for the maintenance of pluripotency. Using RNA reverse transcription-associated trap sequencing, we showed that Peln1 targets multiple pathway genes that are associated with stem cell self-renewal. These findings demonstrate that Peln1 can act as a new epigenetic player and use a trans mechanism to induce an exit from the pluripotent state in stem cells.</p>","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2022-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/17/9a/JCB_202009134.PMC8855478.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39928373","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Rajprasad Loganathan, Daniel C Levings, Ji Hoon Kim, Michael B Wells, Hannah Chiu, Yifan Wu, Matthew Slattery, Deborah J Andrew
{"title":"Ribbon boosts ribosomal protein gene expression to coordinate organ form and function.","authors":"Rajprasad Loganathan, Daniel C Levings, Ji Hoon Kim, Michael B Wells, Hannah Chiu, Yifan Wu, Matthew Slattery, Deborah J Andrew","doi":"10.1083/jcb.202110073","DOIUrl":"https://doi.org/10.1083/jcb.202110073","url":null,"abstract":"<p><p>Cell growth is well defined for late (postembryonic) stages of development, but evidence for early (embryonic) cell growth during postmitotic morphogenesis is limited. Here, we report early cell growth as a key characteristic of tubulogenesis in the Drosophila embryonic salivary gland (SG) and trachea. A BTB/POZ domain nuclear factor, Ribbon (Rib), mediates this early cell growth. Rib binds the transcription start site of nearly every SG-expressed ribosomal protein gene (RPG) and is required for full expression of all RPGs tested. Rib binding to RPG promoters in vitro is weak and not sequence specific, suggesting that specificity is achieved through cofactor interactions. Accordingly, we demonstrate Rib's ability to physically interact with each of the three known regulators of RPG transcription. Surprisingly, Rib-dependent early cell growth in another tubular organ, the embryonic trachea, is not mediated by direct RPG transcription. These findings support a model of early cell growth customized by transcriptional regulatory networks to coordinate organ form and function.</p>","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2022-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/9b/f3/JCB_202110073.PMC9237840.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39656900","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sebastian Eising, Bianca Esch, Mike Wälte, Prado Vargas Duarte, Stefan Walter, Christian Ungermann, Maria Bohnert, Florian Fröhlich
{"title":"A lysosomal biogenesis map reveals the cargo spectrum of yeast vacuolar protein targeting pathways.","authors":"Sebastian Eising, Bianca Esch, Mike Wälte, Prado Vargas Duarte, Stefan Walter, Christian Ungermann, Maria Bohnert, Florian Fröhlich","doi":"10.1083/jcb.202107148","DOIUrl":"https://doi.org/10.1083/jcb.202107148","url":null,"abstract":"<p><p>The lysosome is the major catabolic organelle in the cell that has been established as a key metabolic signaling center. Mutations in many lysosomal proteins have catastrophic effects and cause neurodegeneration, cancer, and age-related diseases. The vacuole is the lysosomal analog of Saccharomyces cerevisiae that harbors many evolutionary conserved proteins. Proteins reach vacuoles via the Vps10-dependent endosomal vacuolar protein sorting pathway, via the alkaline phosphatase (ALP or AP-3) pathway, and via the cytosol-to-vacuole transport (CVT) pathway. A systematic understanding of the cargo spectrum of each pathway is completely lacking. Here, we use quantitative proteomics of purified vacuoles to generate the yeast lysosomal biogenesis map. This dataset harbors information on the cargo-receptor relationship of almost all vacuolar proteins. We map binding motifs of Vps10 and the AP-3 complex and identify a novel cargo of the CVT pathway under nutrient-rich conditions. Our data show how organelle purification and quantitative proteomics can uncover fundamental insights into organelle biogenesis.</p>","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2022-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/33/4f/JCB_202107148.PMC8859911.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39931039","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Rachel L. Flores, Zach Peterson, A. Zelter, Michael Riffle, C. Asbury, T. Davis
{"title":"Three interacting regions of the Ndc80 and Dam1 complexes support microtubule tip-coupling under load","authors":"Rachel L. Flores, Zach Peterson, A. Zelter, Michael Riffle, C. Asbury, T. Davis","doi":"10.1083/jcb.202107016","DOIUrl":"https://doi.org/10.1083/jcb.202107016","url":null,"abstract":"Using laser trapping with recombinant Ndc80 and Dam1 kinetochore complexes, Flores et al. show that interactions between three distinct regions of the complexes support strong, stable attachments to dynamic microtubule tips. Phosphorylating two of the regions reduces both attachment strength and stability. Phosphorylating the third region specifically reduces long-term stability.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"8 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-03-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"123797471","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}
Zheng Wang, Di Chen, Dongshi Guan, Xiaobo Liang, Jianfeng Xue, Hongyu Zhao, G. Song, J. Lou, Yan He, Hong Zhang
{"title":"Material properties of phase-separated TFEB condensates regulate the autophagy-lysosome pathway","authors":"Zheng Wang, Di Chen, Dongshi Guan, Xiaobo Liang, Jianfeng Xue, Hongyu Zhao, G. Song, J. Lou, Yan He, Hong Zhang","doi":"10.1083/jcb.202112024","DOIUrl":"https://doi.org/10.1083/jcb.202112024","url":null,"abstract":"Protein condensates possess distinct material properties. Wang et al. show that the material properties of TFEB condensates govern their size and transcriptional activity. These properties can be manipulated to modulate the activity of TFEB in the autophagy-lysosome pathway.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"487 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-03-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"129413954","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}
{"title":"Structural and biochemical insights into lipid transport by VPS13 proteins","authors":"J. Adlakha, Zhouping Hong, PeiQi Li, K. Reinisch","doi":"10.1101/2022.03.11.484024","DOIUrl":"https://doi.org/10.1101/2022.03.11.484024","url":null,"abstract":"VPS13 proteins are proposed to function at contact sites between organelles as bridges for lipids to move directionally and in bulk between organellar membranes. VPS13s are anchored between membranes via interactions with receptors, including both peripheral or integral membrane proteins. Here we present the crystal structure of VPS13s adaptor binding domain (VAB) complexed with a Pro-X-Pro peptide recognition motif present in one such receptor, the integral membrane protein Mcp1p, and show biochemically that other Pro-X-Pro motifs bind the VAB in the same site. We further demonstrate that Mcp1p and another integral membrane protein that interacts directly with human VPS13A, XK, are scramblases. This finding supports an emerging paradigm of a partnership between bulk lipid transport proteins and scramblases. Scramblases can re-equilibrate lipids between membrane leaflets as lipids are removed from or inserted into, respectively, the cytosolic leaflet of donor and acceptor organelles in the course of protein-mediated transport.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"28 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"124911354","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}
{"title":"The multi-factor modulated biogenesis of the mitochondrial multi-span protein Om14","authors":"Jialin Zhou, M. Jung, K. Dimmer, D. Rapaport","doi":"10.1083/jcb.202112030","DOIUrl":"https://doi.org/10.1083/jcb.202112030","url":null,"abstract":"Zhou et al. provide new insights to the biogenesis of mitochondrial outer membrane proteins. They demonstrate that such proteins can follow various routes where both proteinaceous elements and membrane behavior regulate the efficiency and specificity of this process.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"1 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-03-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"131824910","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}
Jacob Malin, Christian Rosa Birriel, Sergio Astigarraga, J. Treisman, V. Hatini
{"title":"Sidekick dynamically rebalances contractile and protrusive forces to control tissue morphogenesis","authors":"Jacob Malin, Christian Rosa Birriel, Sergio Astigarraga, J. Treisman, V. Hatini","doi":"10.1083/jcb.202107035","DOIUrl":"https://doi.org/10.1083/jcb.202107035","url":null,"abstract":"Malin et al. show that the homophilic adhesion molecule Sidekick interacts alternately with the WAVE regulatory complex and with Polychaetoid/Zonula occludence-1 at tricellular adherens junctions to dynamically rebalance opposing protrusive and contractile forces that repeatedly expand and contract cell contacts to maintain cell–cell contacts and ensure proper epithelial remodeling.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"15 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-03-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"117764782","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}
Saranyaraajan Varadarajan, Shahana A Chumki, Rachel E. Stephenson, Eileen Misterovich, Jessica L. Wu, Claire E Dudley, I. Erofeev, A. Goryachev, Ann L. Miller
{"title":"Mechanosensitive calcium flashes promote sustained RhoA activation during tight junction remodeling","authors":"Saranyaraajan Varadarajan, Shahana A Chumki, Rachel E. Stephenson, Eileen Misterovich, Jessica L. Wu, Claire E Dudley, I. Erofeev, A. Goryachev, Ann L. Miller","doi":"10.1083/jcb.202105107","DOIUrl":"https://doi.org/10.1083/jcb.202105107","url":null,"abstract":"Varadarajan et al. find that calcium flashes regulate epithelial barrier function. Using live imaging, optogenetics, and laser-induced tight junction injury, they show that mechanosensitive channel-dependent calcium flashes promote sustained local activation of RhoA, allowing cells to repair tight junction leaks induced by mechanical stimuli.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"18 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"123983006","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}
Rebecca Cabral-Dias, Stefanie Lucarelli, Karolina Zak, Sadia Rahmani, Gurjeet Judge, John Abousawan, Laura F DiGiovanni, Dafne Vural, K. Anderson, Michael G. Sugiyama, G. Genç, W. Hong, R. Botelho, G. Fairn, P. Kim, C. Antonescu
{"title":"Fyn and TOM1L1 are recruited to clathrin-coated pits and regulate Akt signaling","authors":"Rebecca Cabral-Dias, Stefanie Lucarelli, Karolina Zak, Sadia Rahmani, Gurjeet Judge, John Abousawan, Laura F DiGiovanni, Dafne Vural, K. Anderson, Michael G. Sugiyama, G. Genç, W. Hong, R. Botelho, G. Fairn, P. Kim, C. Antonescu","doi":"10.1083/jcb.201808181","DOIUrl":"https://doi.org/10.1083/jcb.201808181","url":null,"abstract":"Ligand binding to EGF receptor (EGFR) triggers signaling and concomitant receptor recruitment to clathrin-coated pits. This study reveals that the signaling adaptor TOM1L1 recruits Fyn to a specialized subset of clathrin-coated pits and is required for SHIP2 recruitment and regulation of Akt signaling by EGFR.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"88 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"121164243","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}