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LLP1 is a pyrophosphatase involved in homeostasis/quality control of dolichol-linked oligosaccharide. LLP1是一种热磷酸酶，参与醇联寡糖的稳态/质量控制。
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-29 DOI: 10.1083/jcb.202501239
Sheng-Tao Li,Katsuhiko Kamada,Akinobu Honda,Junichi Seino,Tsugiyo Matsuda,Takehiro Suzuki,Naoshi Dohmae,Yuichi Shichino,Shintaro Iwasaki,Yoichi Noda,Michael Costanzo,Charles Boone,Tadashi Suzuki
{"title":"LLP1 is a pyrophosphatase involved in homeostasis/quality control of dolichol-linked oligosaccharide.","authors":"Sheng-Tao Li,Katsuhiko Kamada,Akinobu Honda,Junichi Seino,Tsugiyo Matsuda,Takehiro Suzuki,Naoshi Dohmae,Yuichi Shichino,Shintaro Iwasaki,Yoichi Noda,Michael Costanzo,Charles Boone,Tadashi Suzuki","doi":"10.1083/jcb.202501239","DOIUrl":"https://doi.org/10.1083/jcb.202501239","url":null,"abstract":"Dolichol-linked oligosaccharide (DLO) is the precursor for asparagine (N)-linked protein glycosylation. DLO synthesis can be impaired by genetic and environmental factors, leading to the accumulation of various immature DLO intermediates that are subsequently cleaved into phosphorylated oligosaccharides (POSs). Despite the fact that its activity has been known since the 1970s, the identity of the enzyme has not been clarified. Here, we identified a Saccharomyces cerevisiae gene encoding a DLO-pyrophosphatase (Llp1), which converts DLO to POSs. Intriguingly, LLP1 mRNA was translated through a programmed +1 translational frameshifting. LLP1 orthologs encode members of VanZ family proteins, which are found in various bacteria and fungi. Llp1 and its substrate DLO are likely to be localized in the Golgi, and when LLP1 was knocked out, abnormal DLO modified by Golgi mannosyltransferases accumulated, which is consistent with a role in DLO homeostasis/quality control. This study provides insights into how the cellular levels and quality of DLOs are maintained in eukaryotes.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"27 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145182731","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
JIP4 and RILPL1 utilize opposing motor force to dynamically regulate lysosomal tubulation. JIP4和RILPL1利用相反的运动力动态调节溶酶体管化。
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-24 DOI: 10.1083/jcb.202404018
Luis Bonet-Ponce,Tsion Tegicho,Nuria Fernandez-Martinez,Irene A Rozenberg,Mia Ashriem,Alexandra Beilina,Jillian H Kluss,Yan Li,Mark R Cookson
{"title":"JIP4 and RILPL1 utilize opposing motor force to dynamically regulate lysosomal tubulation.","authors":"Luis Bonet-Ponce,Tsion Tegicho,Nuria Fernandez-Martinez,Irene A Rozenberg,Mia Ashriem,Alexandra Beilina,Jillian H Kluss,Yan Li,Mark R Cookson","doi":"10.1083/jcb.202404018","DOIUrl":"https://doi.org/10.1083/jcb.202404018","url":null,"abstract":"Lysosomes are dynamic organelles that remodel their membrane in response to stimuli. We previously uncovered a process we term LYsosomal Tubulation/sorting driven by LRRK2 (LYTL), wherein damaged lysosomes generate tubules sorted into vesicles. LYTL is orchestrated by the Parkinson's disease kinase LRRK2 that recruits the motor adaptor protein and RHD family member JIP4 to lysosomes. JIP4 enhances LYTL tubule extension toward the plus-end of microtubules. To identify new players involved in LYTL, we mapped the lysosomal proteome after LRRK2 kinase inhibition. We found that RILPL1 is recruited to dysfunctional lysosomes in an LRRK2 kinase activity-dependent manner, facilitated by pRAB proteins. Unlike JIP4, RILPL1 induces retraction of LYTL tubules by binding to p150Glued, thereby moving lysosomal tubules toward the minus-end of microtubules. Our findings emphasize the dynamic regulation of LYTL tubules by two distinct RHD proteins and pRAB effectors, acting as opposing motor adaptor proteins. These opposing forces create a metastable lysosomal membrane deformation, enabling dynamic tubulation events.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"1 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145127025","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
All roads lead to TDP43: Convergent mechanisms of TDP43 autoregulation. 条条大路通TDP43: TDP43自动调节的趋同机制
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-23 DOI: 10.1083/jcb.202508101
Morgan R Miller,Sami J Barmada
{"title":"All roads lead to TDP43: Convergent mechanisms of TDP43 autoregulation.","authors":"Morgan R Miller,Sami J Barmada","doi":"10.1083/jcb.202508101","DOIUrl":"https://doi.org/10.1083/jcb.202508101","url":null,"abstract":"TDP43 is an essential RNA-binding protein with fundamental ties to neurodegenerative disorders. In this issue, Hasegawa-Ogawa and colleagues (https://doi.org/10.1083/jcb.202406097) describe a new mechanism for regulating TDP43 function, involving alternatively spliced variants that inhibit TDP43 via dominant-negative activity.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"88 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145117043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Patterning in motion: Cell interfaces guide mesenchymal collective migration and morphogenesis. 运动中的模式：细胞界面引导间充质集体迁移和形态发生。
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-23 DOI: 10.1083/jcb.202505198
Maik C Bischoff,Roberto Mayor
{"title":"Patterning in motion: Cell interfaces guide mesenchymal collective migration and morphogenesis.","authors":"Maik C Bischoff,Roberto Mayor","doi":"10.1083/jcb.202505198","DOIUrl":"https://doi.org/10.1083/jcb.202505198","url":null,"abstract":"Collective cell migration is a fundamental process in development, wound healing, and cancer. The best-characterized modes of collective migration typically involve cells that retain an epithelial architecture. However, in this review, we explore less well-understood modes of migration driven by cells with a more mesenchymal phenotype. To better understand and compare contact-dependent collective cell behaviors, we propose envisioning each cell as a structure made up of smaller dynamic parts and inferring how these parts behave to understand the overall collective behavior. By examining how local cell shapes influence single-cell behaviors, we can gain insight into how swarm-like behaviors emerge through cell-cell contact. Through this lens, we compare key processes such as contact inhibition of locomotion, mesenchymal cell intercalation, and more complex heterotypic swarm behaviors. Finally, we discuss the emerging concept of contact-mediated rules that regulate motility and have the potential to encode blueprints for complex patterns and even organ shapes.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"16 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145117041","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
How do trypanosome IFT trains choose special tracks? 锥虫型IFT列车如何选择专用轨道？
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-16 DOI: 10.1083/jcb.202508054
Yameng Huang,Cynthia Y He
{"title":"How do trypanosome IFT trains choose special tracks?","authors":"Yameng Huang,Cynthia Y He","doi":"10.1083/jcb.202508054","DOIUrl":"https://doi.org/10.1083/jcb.202508054","url":null,"abstract":"Intraflagellar transport trains in Trypanosoma brucei are known to selectively associate with a subset of axonemal doublet microtubules. In this issue, Araujo Alves et al. (https://doi.org/10.1083/jcb.202501088) aim to elucidate the mechanisms underlying this selective association using high-resolution microscopy approaches.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"35 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145068363","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
ATG16L strikes again! New findings link lysosome stress and physiology. ATG16L又来了！新发现将溶酶体应激与生理联系起来。
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-16 DOI: 10.1083/jcb.202509030
Alison D Klein,Michael Overholtzer
{"title":"ATG16L strikes again! New findings link lysosome stress and physiology.","authors":"Alison D Klein,Michael Overholtzer","doi":"10.1083/jcb.202509030","DOIUrl":"https://doi.org/10.1083/jcb.202509030","url":null,"abstract":"Lysosome stress responses are emerging, but their connections to normal physiology are not well understood. In this issue, Duque et al. (https://doi.org/10.1083/jcb.202503166) discover that the autophagy protein ATG16L, a mediator of a stress response called CASM, also regulates normal lysosome function.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"22 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145068365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The purification of biomolecular condensates: Bottlenecks and strategies. 生物分子凝聚物的纯化：瓶颈与策略。
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-12 DOI: 10.1083/jcb.202504081
Sylvain Tartier,Jihane Basbous,Séverine Boulon,Céline Verheggen,Edouard Bertrand
{"title":"The purification of biomolecular condensates: Bottlenecks and strategies.","authors":"Sylvain Tartier,Jihane Basbous,Séverine Boulon,Céline Verheggen,Edouard Bertrand","doi":"10.1083/jcb.202504081","DOIUrl":"https://doi.org/10.1083/jcb.202504081","url":null,"abstract":"Biomolecular condensates are large assemblies of proteins and nucleic acids that form distinct compartments inside the cell without being surrounded by a membrane. They form through multivalent interactions, are not stereospecifically defined, and can scale with component addition. By concentrating specific biomolecules at specific times and cellular locations, condensates play key roles in many processes, such as transcription, RNP assembly, cell cycle, DNA repair, and stress responses. Condensate biology greatly benefited from systematic analyses of their composition. However, condensates often have heterogenous sizes and are built on interaction networks that include stable and labile components. They also have highly variable compositions and dynamics. Their purification thus represents a significant challenge, and it necessitates extensive testing and adaptation of techniques originally designed for other applications. This article aims to synthesize the existing empirical knowledge on the extraction and purification of cellular condensates and analyze the challenges inherent to this field.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"164 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145035692","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Lipid droplets: Open questions and conceptual advances around a unique organelle. 脂滴：围绕独特细胞器的开放性问题和概念进展。
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-11 DOI: 10.1083/jcb.202406019
W Mike Henne,Emma Reynolds,William A Prinz
{"title":"Lipid droplets: Open questions and conceptual advances around a unique organelle.","authors":"W Mike Henne,Emma Reynolds,William A Prinz","doi":"10.1083/jcb.202406019","DOIUrl":"https://doi.org/10.1083/jcb.202406019","url":null,"abstract":"Once viewed as mere lipid inclusions, the past four decades have witnessed an explosion of research into lipid droplet (LD) biogenesis and function. Pioneering cell biology, biochemical, genetics, and lipidomic studies now reveal LDs as active players in lipid metabolism and cellular homeostasis. Here, we discuss some of the major findings that defined LDs as bona fide organelles. However, despite what is known, much needs to be discovered. We highlight five enduring questions that continue to challenge the LD field and discuss a few misconceptions about this remarkable organelle.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"59 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145032173","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
ATG16L1 controls mammalian vacuolar proton ATPase. ATG16L1控制哺乳动物液泡质子atp酶。
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-09 DOI: 10.1083/jcb.202503166
Thabata L A Duque,Masroor Paddar,Einar Trosdal,Ruheena Javed,Lee Allers,Michal H Mudd,Prithvi Akepati,Soumya R Mishra,Michelle Salemi,Brett Phinney,Shawn B Bratton,Thomas Wileman,Vojo Deretic
{"title":"ATG16L1 controls mammalian vacuolar proton ATPase.","authors":"Thabata L A Duque,Masroor Paddar,Einar Trosdal,Ruheena Javed,Lee Allers,Michal H Mudd,Prithvi Akepati,Soumya R Mishra,Michelle Salemi,Brett Phinney,Shawn B Bratton,Thomas Wileman,Vojo Deretic","doi":"10.1083/jcb.202503166","DOIUrl":"https://doi.org/10.1083/jcb.202503166","url":null,"abstract":"The mechanisms governing mammalian proton pump V-ATPase function are of fundamental and medical interest. The assembly and disassembly of cytoplasmic V1 domain with the membrane-embedded V0 domain of V-ATPase is a key aspect of V-ATPase localization and function. Here, we show that the mammalian protein ATG16L1, primarily appreciated for its role in canonical autophagy and in noncanonical membrane atg8ylation processes, controls V-ATPase. ATG16L1 knockout elevated V-ATPase activity, increased V1 presence on endomembranes, and increased the number of acidified intracellular compartments. ATG16L1's ability to efficiently bind V-ATPase was required for its inhibitory role in endolysosomal acidification and for control of Mycobacterium tuberculosis infection in mice. These findings uncover a hitherto unappreciated role of ATG16L1 in regulating V-ATPase, a key pump governing acidification and functionality of the endolysosomal system along with its physiological roles.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"13 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145018262","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
PI(3)P coordinates SNX17- and SNX27-dependent protein recycling for long-term synaptic plasticity. PI(3)P协调SNX17-和snx27依赖蛋白的长期突触可塑性循环。
IF 7.8 1区 生物学
Journal of Cell Biology Pub Date : 2025-09-08 DOI: 10.1083/jcb.202411198
Pilar Rivero-Ríos,Tunahan Uygun,Garrett D Chavis,Hankyu Lee,Bo Duan,Michael A Sutton,Lois S Weisman
{"title":"PI(3)P coordinates SNX17- and SNX27-dependent protein recycling for long-term synaptic plasticity.","authors":"Pilar Rivero-Ríos,Tunahan Uygun,Garrett D Chavis,Hankyu Lee,Bo Duan,Michael A Sutton,Lois S Weisman","doi":"10.1083/jcb.202411198","DOIUrl":"https://doi.org/10.1083/jcb.202411198","url":null,"abstract":"Two major protein recycling pathways have emerged as key regulators of enduring forms of synaptic plasticity, such as long-term potentiation (LTP), yet how these pathways are recruited during plasticity is unknown. Phosphatidylinositol-3-phosphate (PI(3)P) is a key regulator of endosomal trafficking and alterations in this lipid have been linked to neurodegeneration. Here, using primary hippocampal neurons, we demonstrate dynamic PI(3)P synthesis during chemical induction of LTP (cLTP), which drives coordinate recruitment of the SNX17-Retriever and SNX27-Retromer pathways to endosomes and synaptic sites. Both pathways are necessary for the cLTP-dependent structural enlargement of dendritic spines and act in parallel by recycling distinct sets of cell surface proteins at synapses. Importantly, preventing PI(3)P synthesis blocks synaptic recruitment of SNX17 and SNX27, decreases cargo recycling, and blocks LTP in cultured neurons and hippocampal slices. These findings provide mechanistic insights into the regulation of endocytic recycling at synapses and define a role for dynamic PI(3)P synthesis in synaptic plasticity.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"51 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145008860","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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