Hongfei Xu, Fei Chang, Shweta Jain, B. A. Heller, Xu Han, Yongjian Liu, R. Edwards
The endosomal adaptor protein AP-3 assembles the membrane proteins of dense core vesicles (DCVs). Sorting nexin 5 targets the vesicular monoamine transporter (VMAT) to DCVs by retrograde transport from endosomes to the trans-Golgi network (TGN), thereby revealing a novel role for AP-3 at the TGN.
{"title":"SNX5 targets a monoamine transporter to the TGN for assembly into dense core vesicles by AP-3","authors":"Hongfei Xu, Fei Chang, Shweta Jain, B. A. Heller, Xu Han, Yongjian Liu, R. Edwards","doi":"10.1083/jcb.202106083","DOIUrl":"https://doi.org/10.1083/jcb.202106083","url":null,"abstract":"The endosomal adaptor protein AP-3 assembles the membrane proteins of dense core vesicles (DCVs). Sorting nexin 5 targets the vesicular monoamine transporter (VMAT) to DCVs by retrograde transport from endosomes to the trans-Golgi network (TGN), thereby revealing a novel role for AP-3 at the TGN.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"50 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":"126573448","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}
Haiping Liu, Wei Lin, Spencer R Leibow, Alexander J Morateck, Malini Ahuja, S. Muallem
PI(4,5)P2, a key lipid at ER/PM junctions, has multiple roles in regulating TRPC channels, which includes recruitment of the channel to the junctions to facilitate activation by receptor stimulation, channel pore opening, and channel ionic selectivity.
{"title":"TRPC3 channel gating by lipids requires localization at the ER/PM junctions defined by STIM1","authors":"Haiping Liu, Wei Lin, Spencer R Leibow, Alexander J Morateck, Malini Ahuja, S. Muallem","doi":"10.1083/jcb.202107120","DOIUrl":"https://doi.org/10.1083/jcb.202107120","url":null,"abstract":"PI(4,5)P2, a key lipid at ER/PM junctions, has multiple roles in regulating TRPC channels, which includes recruitment of the channel to the junctions to facilitate activation by receptor stimulation, channel pore opening, and channel ionic selectivity.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"427-429 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"124029925","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}
Jieqiong Gao, Raffaele Nicastro, Marie-Pierre Péli-Gulli, Sophie Grziwa, Zilei Chen, Rainer Kurre, J. Piehler, C. De Virgilio, F. Fröhlich, C. Ungermann
Gao et al. show that an endosomal population carrying the TORC1 signaling complex, which they term signaling endosomes (SEs), requires the HOPS tethering complex and MVB biogenesis for their formation and identity and for efficient TORC1 signaling.
{"title":"The HOPS tethering complex is required to maintain signaling endosome identity and TORC1 activity","authors":"Jieqiong Gao, Raffaele Nicastro, Marie-Pierre Péli-Gulli, Sophie Grziwa, Zilei Chen, Rainer Kurre, J. Piehler, C. De Virgilio, F. Fröhlich, C. Ungermann","doi":"10.1083/jcb.202109084","DOIUrl":"https://doi.org/10.1083/jcb.202109084","url":null,"abstract":"Gao et al. show that an endosomal population carrying the TORC1 signaling complex, which they term signaling endosomes (SEs), requires the HOPS tethering complex and MVB biogenesis for their formation and identity and for efficient TORC1 signaling.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"112 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"127312509","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}
A. Vásquez-Limeta, Kimberly Lukasik, Dong Kong, Catherine Sullenberger, Delgermaa Luvsanjav, Natalie Sahabandu, R. Chari, J. Loncarek
Vasquez-Limeta et al. use human cells engineered for fast degradation of centrosomal protein CPAP. Using superresolution microscopy, they show that CPAP insufficiency leads to centrioles with incomplete microtubule triplets that convert to centrosomes and duplicate, but fragment owing to loss of cohesion between microtubule blades.
{"title":"CPAP insufficiency leads to incomplete centrioles that duplicate but fragment","authors":"A. Vásquez-Limeta, Kimberly Lukasik, Dong Kong, Catherine Sullenberger, Delgermaa Luvsanjav, Natalie Sahabandu, R. Chari, J. Loncarek","doi":"10.1083/jcb.202108018","DOIUrl":"https://doi.org/10.1083/jcb.202108018","url":null,"abstract":"Vasquez-Limeta et al. use human cells engineered for fast degradation of centrosomal protein CPAP. Using superresolution microscopy, they show that CPAP insufficiency leads to centrioles with incomplete microtubule triplets that convert to centrosomes and duplicate, but fragment owing to loss of cohesion between microtubule blades.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"36 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"128003599","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}
Marivin et al. show how association of the protein DAPLE with PAR polarity complexes at cell–cell junctions maintains an apical cytoskeletal network in epithelial cells by simultaneously activating heterotrimeric G proteins and recruiting the actin-stabilizing protein CD2AP.
{"title":"DAPLE orchestrates apical actomyosin assembly from junctional polarity complexes","authors":"A. Marivin, R. Ho, M. Garcia-Marcos","doi":"10.1083/jcb.202111002","DOIUrl":"https://doi.org/10.1083/jcb.202111002","url":null,"abstract":"Marivin et al. show how association of the protein DAPLE with PAR polarity complexes at cell–cell junctions maintains an apical cytoskeletal network in epithelial cells by simultaneously activating heterotrimeric G proteins and recruiting the actin-stabilizing protein CD2AP.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"82 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"117057897","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}
V. Pande, N. Mitra, S. Bagde, R. Srinivasan, P. Gayathri
Through the characterization of Spiroplasma MreB5, Pande et al. show that MreB5 exhibits a nucleotide-dependent allosteric effect on filament dynamics and membrane binding. The results highlight the conserved and distinct features of MreBs in shape determination, independent of peptidoglycan synthesis machinery.
{"title":"Filament organization of the bacterial actin MreB is dependent on the nucleotide state","authors":"V. Pande, N. Mitra, S. Bagde, R. Srinivasan, P. Gayathri","doi":"10.1083/jcb.202106092","DOIUrl":"https://doi.org/10.1083/jcb.202106092","url":null,"abstract":"Through the characterization of Spiroplasma MreB5, Pande et al. show that MreB5 exhibits a nucleotide-dependent allosteric effect on filament dynamics and membrane binding. The results highlight the conserved and distinct features of MreBs in shape determination, independent of peptidoglycan synthesis machinery.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"1068 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132751189","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}
Rachel L. Flores, Zach Peterson, A. Zelter, Michael Riffle, C. Asbury, T. Davis
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.
{"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
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.
{"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}
Pub Date : 2022-03-12DOI: 10.1101/2022.03.11.484024
J. Adlakha, Zhouping Hong, PeiQi Li, K. Reinisch
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.
{"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}
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.
{"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}
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