BioEssaysPub Date : 2024-07-26DOI: 10.1002/bies.202400092
Martin F Pera
{"title":"A brief chronicle of research on human pluripotent stem cells.","authors":"Martin F Pera","doi":"10.1002/bies.202400092","DOIUrl":"https://doi.org/10.1002/bies.202400092","url":null,"abstract":"<p><p>Today, human pluripotent stem cell technologies find widespread application across biomedical research, as models for early human development, as platforms for functional human genomics, as tools for the study of disease, drug screening and toxicology, and as a renewable source of cellular therapeutics for a range of intractable diseases. The foundations of this human pluripotent stem cell revolution rest on advances in a wide range of disciplines, including cancer biology, assisted reproduction, cell culture and organoid technology, somatic cell nuclear transfer, primate embryology, single-cell biology, and gene editing. This review surveys the slow emergence of the study of human pluripotency and the exponential growth of the field during the past several decades.</p>","PeriodicalId":9264,"journal":{"name":"BioEssays","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-07-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141765528","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioEssaysPub Date : 2024-07-23DOI: 10.1002/bies.202400117
Qi Gao, Bram J. A. Vermeulen, Martin Würtz, Hyesu Shin, Dilara Erdogdu, Anjun Zheng, Florian W. Hofer, Annett Neuner, Stefan Pfeffer, Elmar Schiebel
{"title":"The structure of the γ-TuRC at the microtubule minus end – not just one solution","authors":"Qi Gao, Bram J. A. Vermeulen, Martin Würtz, Hyesu Shin, Dilara Erdogdu, Anjun Zheng, Florian W. Hofer, Annett Neuner, Stefan Pfeffer, Elmar Schiebel","doi":"10.1002/bies.202400117","DOIUrl":"10.1002/bies.202400117","url":null,"abstract":"<p>In cells, microtubules (MTs) assemble from α/β-tubulin subunits at nucleation sites containing the γ-tubulin ring complex (γ-TuRC). Within the γ-TuRC, exposed γ-tubulin molecules act as templates for MT assembly by interacting with α/β-tubulin. The vertebrate γ-TuRC is scaffolded by γ-tubulin-interacting proteins GCP2-6 arranged in a specific order. Interestingly, the γ-tubulin molecules in the γ-TuRC deviate from the cylindrical geometry of MTs, raising the question of how the γ-TuRC structure changes during MT nucleation. Recent studies on the structure of the vertebrate γ-TuRC attached to the end of MTs came to varying conclusions. In vitro assembly of MTs, facilitated by an α-tubulin mutant, resulted in a closed, cylindrical γ-TuRC showing canonical interactions between all γ-tubulin molecules and α/β-tubulin subunits. Conversely, native MTs formed in a frog extract were capped by a partially closed γ-TuRC, with some γ-tubulin molecules failing to align with α/β-tubulin. This review discusses these outcomes, along with the broader implications.</p>","PeriodicalId":9264,"journal":{"name":"BioEssays","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-07-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141751162","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioEssaysPub Date : 2024-07-22DOI: 10.1002/bies.202470012
{"title":"BioEssays 8/2024","authors":"","doi":"10.1002/bies.202470012","DOIUrl":"10.1002/bies.202470012","url":null,"abstract":"<p>Eukaryotic chromosome ends are characterized by specialized structures, namely telomeres. Telomeric DNA is usually rich in guanines and is able to form four-stranded G-quadruplexes. In article 2300229, So Young Joo et al. review how dynamic interactions between G-quadruplexes and the tumor suppressor BRCA2 influence telomere replication.\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure>\u0000 </p>","PeriodicalId":9264,"journal":{"name":"BioEssays","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/bies.202470012","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141753935","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioEssaysPub Date : 2024-07-19DOI: 10.1002/bies.202400037
Biswendu Biswas, Stéphan Vagner
{"title":"Genotoxic stress impacts pre-mRNA 3′-end processing","authors":"Biswendu Biswas, Stéphan Vagner","doi":"10.1002/bies.202400037","DOIUrl":"10.1002/bies.202400037","url":null,"abstract":"<p>Genotoxic stress, arising from various environmental sources and endogenous cellular processes, pose a constant threat to genomic stability. Cells have evolved intricate mechanisms to detect and repair DNA damage, orchestrating a robust genotoxic stress response to safeguard the integrity of the genome. Recent research has shed light on the crucial role of co- and post-transcriptional regulatory mechanisms in modulating the cellular response to genotoxic stress. Here we highlight recent advances illustrating the intricate interplay between pre-mRNA processing, with a focus on 3′-end processing, and genotoxic stress response.</p>","PeriodicalId":9264,"journal":{"name":"BioEssays","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-07-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/bies.202400037","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141731004","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioEssaysPub Date : 2024-07-11DOI: 10.1002/bies.202400133
Seth Blackshaw, Jiang Qian, David R. Hyde
{"title":"New pathways to neurogenesis: Insights from injury-induced retinal regeneration","authors":"Seth Blackshaw, Jiang Qian, David R. Hyde","doi":"10.1002/bies.202400133","DOIUrl":"10.1002/bies.202400133","url":null,"abstract":"<p>The vertebrate retina is a tractable system for studying control of cell neurogenesis and cell fate specification. During embryonic development, retinal neurogenesis is under strict temporal regulation, with cell types generated in fixed but overlapping temporal intervals. The temporal sequence and relative numbers of retinal cell types generated during development are robust and show minimal experience-dependent variation. In many cold-blooded vertebrates, acute retinal injury induces a different form of neurogenesis, where Müller glia reprogram into retinal progenitor-like cells that selectively regenerate retinal neurons lost to injury. The extent to which the molecular mechanisms controlling developmental and injury-induced neurogenesis resemble one another has long been unclear. However, a recent study in zebrafish has shed new light on this question, using single-cell multiomic analysis to show that selective loss of different retinal cell types induces the formation of fate-restricted Müller glia-derived progenitors that differ both from one another and from progenitors in developing retina. Here, we discuss the broader implications of these findings, and their possible therapeutic relevance.</p>","PeriodicalId":9264,"journal":{"name":"BioEssays","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141579020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioEssaysPub Date : 2024-07-11DOI: 10.1002/bies.202400026
Laura Zoe Kreplin, Senthil Arumugam
{"title":"The physical basis of analog-to-digital signal processing in the EGFR system—Delving into the role of the endoplasmic reticulum","authors":"Laura Zoe Kreplin, Senthil Arumugam","doi":"10.1002/bies.202400026","DOIUrl":"10.1002/bies.202400026","url":null,"abstract":"<p>Receptor tyrosine kinases exhibit ligand-induced activity and uptake into cells via endocytosis. In the case of epidermal growth factor (EGF) receptor (EGFR), the resulting endosomes are trafficked to the perinuclear region, where dephosphorylation of receptors occurs, which are subsequently directed to degradation. Traveling endosomes bearing phosphorylated EGFRs are subjected to the activity of cytoplasmic phosphatases as well as interactions with the endoplasmic reticulum (ER). The peri-nuclear region harbors ER-embedded phosphatases, a component of the EGFR-bearing endosome-ER contact site. The ER is also emerging as a central player in spatiotemporal control of endosomal motility, positioning, tubulation, and fission. Past studies strongly suggest that the physical interaction between the ER and endosomes forms a reaction “unit” for EGFR dephosphorylation. Independently, endosomes have been implicated to enable quantization of EGFR signals by modulation of the phosphorylation levels. Here, we review the distinct mechanisms by which endosomes form the logistical means for signal quantization and speculate on the role of the ER.</p>","PeriodicalId":9264,"journal":{"name":"BioEssays","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/bies.202400026","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141589671","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioEssaysPub Date : 2024-07-11DOI: 10.1002/bies.202400107
Wei Guo, Stefano Russo, Francesca Tuorto
{"title":"Lost in translation: How neurons cope with tRNA decoding","authors":"Wei Guo, Stefano Russo, Francesca Tuorto","doi":"10.1002/bies.202400107","DOIUrl":"10.1002/bies.202400107","url":null,"abstract":"<p>Post-transcriptional tRNA modifications contribute to the decoding efficiency of tRNAs by supporting codon recognition and tRNA stability. Recent work shows that the molecular and cellular functions of tRNA modifications and tRNA-modifying-enzymes are linked to brain development and neurological disorders. Lack of these modifications affects codon recognition and decoding rate, promoting protein aggregation and translational stress response pathways with toxic consequences to the cell. In this review, we discuss the peculiarity of local translation in neurons, suggesting a role for fine-tuning of translation performed by tRNA modifications. We provide several examples of tRNA modifications involved in physiology and pathology of the nervous system, highlighting their effects on protein translation and discussing underlying mechanisms, like the unfolded protein response (UPR), ribosome quality control (RQC), and no-go mRNA decay (NGD), which could affect neuronal functions. We aim to deepen the understanding of the roles of tRNA modifications and the coordination of these modifications with the protein translation machinery in the nervous system.</p>","PeriodicalId":9264,"journal":{"name":"BioEssays","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/bies.202400107","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141579019","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioEssaysPub Date : 2024-07-11DOI: 10.1002/bies.202300222
Niels Boegholm, Narcis A. Petriman, Niaj M. Tanvir, Esben Lorentzen
{"title":"Architecture of RabL2-associated complexes at the ciliary base: A structural modeling perspective","authors":"Niels Boegholm, Narcis A. Petriman, Niaj M. Tanvir, Esben Lorentzen","doi":"10.1002/bies.202300222","DOIUrl":"10.1002/bies.202300222","url":null,"abstract":"<p>Cilia are slender, micrometer-long organelles present on the surface of eukaryotic cells. They function in signaling and locomotion and are constructed by intraflagellar transport (IFT). The assembly of IFT complexes into so-called IFT trains to initiate ciliary entry at the base of the cilium remains a matter of debate. Here, we use structural modeling to provide an architectural framework for how RabL2 is anchored at the ciliary base via CEP19 before being handed over to IFT trains for ciliary entry. Our models suggest that the N-terminal domain of CEP43 forms a homo-dimer to anchor at the subdistal appendages of cilia through a direct interaction with CEP350. A long linker region separates the N-terminal domain of CEP43 from the C-terminal domain, which captures CEP19 above the subdistal appendages and close to the distal appendages. Furthermore, we present a structural model for how RabL2-CEP19 associates with the IFT-B complex, providing insight into how RabL2 is handed over from CEP19 to the IFT complex. Interestingly, RabL2 association with the IFT-B complex appears to induce a significant conformational change in the IFT complex via a kink in the coiled-coils of the IFT81/74 proteins, which may prime the IFT machinery for entry into cilia.</p>","PeriodicalId":9264,"journal":{"name":"BioEssays","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/bies.202300222","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141589670","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}