Nature Cell Biology最新文献_第5页

Coupling of cell shape, matrix and tissue dynamics ensures embryonic patterning robustness

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-18 DOI: 10.1038/s41556-025-01618-9

Prachiti Moghe, Roman Belousov, Takafumi Ichikawa, Chizuru Iwatani, Tomoyuki Tsukiyama, Anna Erzberger, Takashi Hiiragi

{"title":"Coupling of cell shape, matrix and tissue dynamics ensures embryonic patterning robustness","authors":"Prachiti Moghe, Roman Belousov, Takafumi Ichikawa, Chizuru Iwatani, Tomoyuki Tsukiyama, Anna Erzberger, Takashi Hiiragi","doi":"10.1038/s41556-025-01618-9","DOIUrl":"10.1038/s41556-025-01618-9","url":null,"abstract":"Tissue patterning coordinates morphogenesis, cell dynamics and fate specification. Understanding how precision in patterning is robustly achieved despite inherent developmental variability during mammalian embryogenesis remains a challenge. Here, based on cell dynamics quantification and simulation, we show how salt-and-pepper epiblast and primitive endoderm (PrE) cells pattern the inner cell mass of mouse blastocysts. Coupling cell fate and dynamics, PrE cells form apical polarity-dependent actin protrusions required for RAC1-dependent migration towards the surface of the fluid cavity, where PrE cells are trapped due to decreased tension. Concomitantly, PrE cells deposit an extracellular matrix gradient, presumably breaking the tissue-level symmetry and collectively guiding their own migration. Tissue size perturbations of mouse embryos and their comparison with monkey and human blastocysts further demonstrate that the fixed proportion of PrE/epiblast cells is optimal with respect to embryo size and tissue geometry and, despite variability, ensures patterning robustness during early mammalian development. Moghe et al. show that mouse embryonic primitive endoderm cells migrate towards the inner cell mass-cavity interface, depositing an extracellular matrix gradient that may guide migration. Primitive endoderm to epiblast ratios may enable robust patterning across embryos and sizes.","PeriodicalId":18977,"journal":{"name":"Nature Cell Biology","volume":"27 3","pages":"408-423"},"PeriodicalIF":17.3,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.com/articles/s41556-025-01618-9.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143435026","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Author Correction: Genome-wide CRISPR screens identify ILF3 as a mediator of mTORC1-dependent amino acid sensing

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-17 DOI: 10.1038/s41556-025-01633-w

Guokai Yan, Jinxin Yang, Wen Li, Ao Guo, Jialiang Guan, Ying Liu

引用次数: 0

Mesoderm FN1 shaping the heart

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-13 DOI: 10.1038/s41556-025-01630-z

Daryl J. V. David

引用次数: 0

Enhancers activate from afar

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-13 DOI: 10.1038/s41556-025-01628-7

Sabrya Carim

引用次数: 0

Restoring placental methylome

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-13 DOI: 10.1038/s41556-025-01631-y

Stylianos Lefkopoulos

引用次数: 0

Ribophagy relies on Rpl12

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-11 DOI: 10.1038/s41556-024-01594-6

Katarzyna Tutak, Katrin Karbstein

引用次数: 0

Rpl12 is a conserved ribophagy receptor

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-11 DOI: 10.1038/s41556-024-01598-2

Yuting Chen, Jiaxin Hu, Pengwei Zhao, Jie Fang, Yingqi Kuang, Zhaojie Liu, Shuling Dong, Weijing Yao, Yuanyuan Ding, Xinhui Wang, Yibin Pan, Jianbin Wu, Jingwei Zhao, Jing Yang, Zhenzhong Xu, Xiaodi Liu, Yi Zhang, Choufei Wu, Liqin Zhang, Mingzhu Fan, Shan Feng, Zhi Hong, Zhangming Yan, Hongguang Xia, Kaiyue Tang, Bing Yang, Wei Liu, Qiming Sun, Kunrong Mei, Wei Zou, Yunpeng Huang, Du Feng, Cong Yi

{"title":"Rpl12 is a conserved ribophagy receptor","authors":"Yuting Chen, Jiaxin Hu, Pengwei Zhao, Jie Fang, Yingqi Kuang, Zhaojie Liu, Shuling Dong, Weijing Yao, Yuanyuan Ding, Xinhui Wang, Yibin Pan, Jianbin Wu, Jingwei Zhao, Jing Yang, Zhenzhong Xu, Xiaodi Liu, Yi Zhang, Choufei Wu, Liqin Zhang, Mingzhu Fan, Shan Feng, Zhi Hong, Zhangming Yan, Hongguang Xia, Kaiyue Tang, Bing Yang, Wei Liu, Qiming Sun, Kunrong Mei, Wei Zou, Yunpeng Huang, Du Feng, Cong Yi","doi":"10.1038/s41556-024-01598-2","DOIUrl":"10.1038/s41556-024-01598-2","url":null,"abstract":"Ribophagy is a selective autophagic process that regulates ribosome turnover. Although NUFIP1 has been identified as a mammalian receptor for ribophagy, its homologues do not exist in yeast and nematodes. Here we demonstrate that Rpl12, a ribosomal large subunit protein, functions as a conserved ribophagy receptor in multiple organisms. Disruption of Rpl12–Atg8s binding leads to significant accumulation of ribosomal proteins and rRNA, while Atg1-mediated Rpl12 phosphorylation enhances its association with Atg11, thus triggering ribophagy during starvation. Ribophagy deficiency accelerates cell death induced by starvation and pathogen infection, leading to impaired growth and development and a shortened lifespan in both Caenorhabditis elegans and Drosophila melanogaster. Moreover, ribophagy deficiency results in motor impairments associated with ageing, while the overexpression of RPL12 significantly improves movement defects induced by starvation, ageing and Aβ accumulation in fly models. Our findings suggest that Rpl12 functions as a conserved ribophagy receptor vital for ribosome metabolism and cellular homeostasis. Chen, Hu, Zhao, Fang and colleagues show that the ribosomal large subunit protein Rpl12 functions as a conserved ribophagy receptor in multiple organisms.","PeriodicalId":18977,"journal":{"name":"Nature Cell Biology","volume":"27 3","pages":"477-492"},"PeriodicalIF":17.3,"publicationDate":"2025-02-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143385076","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

A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-07 DOI: 10.1038/s41556-025-01612-1

Philip J. Mannino, Andrew Perun, Ivan V. Surovtsev, Nicholas R. Ader, Lin Shao, Elisa C. Rodriguez, Thomas J. Melia, Megan C. King, C. Patrick Lusk

{"title":"A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope","authors":"Philip J. Mannino, Andrew Perun, Ivan V. Surovtsev, Nicholas R. Ader, Lin Shao, Elisa C. Rodriguez, Thomas J. Melia, Megan C. King, C. Patrick Lusk","doi":"10.1038/s41556-025-01612-1","DOIUrl":"10.1038/s41556-025-01612-1","url":null,"abstract":"Autophagic mechanisms that maintain nuclear envelope homoeostasis are bulwarks to ageing and disease. Here we define a quantitative and ultrastructural timeline of nuclear macroautophagy (nucleophagy) in yeast by leveraging four-dimensional lattice light sheet microscopy and correlative light and electron tomography. Nucleophagy begins with a rapid accumulation of the selective autophagy receptor Atg39 at the nuclear envelope and finishes in ~300 s with Atg39-cargo delivery to the vacuole. Although there are several routes to the vacuole, at least one pathway incorporates two consecutive membrane fission steps: inner nuclear membrane (INM) fission to generate an INM-derived vesicle in the perinuclear space and outer nuclear membrane fission to liberate a double-membraned vesicle to the cytosol. Outer nuclear membrane fission occurs independently of phagophore engagement and instead relies surprisingly on dynamin-like protein 1 (Dnm1), which is recruited to sites of Atg39 accumulation by Atg11. Loss of Dnm1 compromises nucleophagic flux by stalling nucleophagy after INM fission. Our findings reveal how nuclear and INM cargo are removed from an intact nucleus without compromising its integrity, achieved in part by a non-canonical role for Dnm1 in nuclear envelope remodelling. Mannino et al. provide a quantitative and ultrastructural timeline of nucleophagy in yeast with lattice light sheet microscopy and correlative light and electron tomography. They identify a role for dynamin-like protein 1 in outer nuclear membrane fission.","PeriodicalId":18977,"journal":{"name":"Nature Cell Biology","volume":"27 3","pages":"464-476"},"PeriodicalIF":17.3,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143257838","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

Regulating MYC translation in cancer

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-07 DOI: 10.1038/s41556-024-01589-3

Zainab Hussain, Mara H. Sherman

引用次数: 0

Time for lipid cell biology

IF 17.3 1区生物学

Nature Cell Biology Pub Date : 2025-02-05 DOI: 10.1038/s41556-025-01609-w

Xiao-Wei Chen, Anthony S. Don, Maria Fedorova, Takeshi Harayama, Natalie Krahmer, Shigekazu Nagata, Priyanka Narayan, Dequina Nicholas, Sara M. Nowinski, Yasunori Saheki, Clay F. Semenkovich, Xiaoai Zhao, Yilong Zou

引用次数: 0