Molecular Biology of the Cell最新文献_第5页

Loss of intermicrovillar adhesion factor CDHR2 impairs basolateral junctional complexes in transporting epithelia. 失去微绒毛间粘附因子 CDHR2 会损害运输上皮的基底侧连接复合体。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 Epub Date: 2024-09-18 DOI: 10.1091/mbc.E24-03-0113

Caroline S Cencer, Kianna L Robinson, Matthew J Tyska

{"title":"Loss of intermicrovillar adhesion factor CDHR2 impairs basolateral junctional complexes in transporting epithelia.","authors":"Caroline S Cencer, Kianna L Robinson, Matthew J Tyska","doi":"10.1091/mbc.E24-03-0113","DOIUrl":"10.1091/mbc.E24-03-0113","url":null,"abstract":"Transporting epithelial cells in the gut and kidney rely on protocadherin-based apical adhesion complexes to organize microvilli that extend into luminal space. In these systems, CDHR2 and CDHR5 localize to the distal ends of microvilli, where they form an intermicrovillar adhesion complex (IMAC) that links the tips of these structures, promotes the formation of a well-ordered array of protrusions, and thus maximizes apical membrane surface area. Recently, we discovered that IMACs can also form between microvilli that extend from neighboring cells, across cell-cell junctions. As an additional point of physical contact between cells, transjunctional IMACs are well positioned to impact the integrity of canonical tight and adherens junctions that form more basolaterally. To begin to test this idea, we examined cell culture and mouse models that lacked CDHR2 expression and were unable to form IMACs. CDHR2 knockout perturbed cell and junction morphology, reduced key components from tight and adherens junctions, impaired barrier function, and increased the motility of single cells within established monolayers. These results support the hypothesis that, in addition to organizing apical microvilli, IMACs provide a layer of cell-cell contact that functions in parallel with canonical tight and adherens junctions to promote epithelial functions.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"br21"},"PeriodicalIF":3.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11617098/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142291466","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}

引用次数: 0

Diversity, equity, and inclusion in a polarized world: Navigating challenges and opportunities in STEMM. 两极分化世界中的多样性、公平性和包容性：驾驭科学、技术、工程和数学领域的挑战与机遇。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 DOI: 10.1091/mbc.E24-06-0264

Vijayvardhan Kamalumpundi, Kit Neikirk, Debora Kamin Mukaz, Zer Vue, Neng Vue, Sulema Perales, Antentor Hinton

引用次数: 0

Endosomal actin branching, fission, and receptor recycling require FCHSD2 recruitment by MICAL-L1. 内体肌动蛋白分支、裂变和受体再循环需要 MICAL-L1 招募 FCHSD2。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 Epub Date: 2024-10-09 DOI: 10.1091/mbc.E24-07-0324

Devin Frisby, Ajay B Murakonda, Bazella Ashraf, Kanika Dhawan, Leonardo Almeida-Souza, Naava Naslavsky, Steve Caplan

{"title":"Endosomal actin branching, fission, and receptor recycling require FCHSD2 recruitment by MICAL-L1.","authors":"Devin Frisby, Ajay B Murakonda, Bazella Ashraf, Kanika Dhawan, Leonardo Almeida-Souza, Naava Naslavsky, Steve Caplan","doi":"10.1091/mbc.E24-07-0324","DOIUrl":"10.1091/mbc.E24-07-0324","url":null,"abstract":"Endosome fission is required for the release of carrier vesicles and the recycling of receptors to the plasma membrane. Early events in endosome budding and fission rely on actin branching to constrict the endosomal membrane, ultimately leading to nucleotide hydrolysis and enzymatic fission. However, our current understanding of this process is limited, particularly regarding the coordination between the early and late steps of endosomal fission. Here we have identified a novel interaction between the endosomal scaffolding protein, MICAL-L1, and the human homologue of the Drosophila Nervous Wreck (Nwk) protein, FCH and double SH3 domains protein 2 (FCHSD2). We demonstrate that MICAL-L1 recruits FCHSD2 to the endosomal membrane, where it is required for ARP2/3-mediated generation of branched actin, endosome fission and receptor recycling to the plasma membrane. Because MICAL-L1 first recruits FCHSD2 to the endosomal membrane, and is subsequently responsible for recruitment of the ATPase and fission protein EHD1 to endosomes, our findings support a model in which MICAL-L1 orchestrates endosomal fission by connecting between the early actin-driven and subsequent nucleotide hydrolysis steps of the process.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar144"},"PeriodicalIF":3.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11617095/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142391840","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}

引用次数: 0

The rat bladder umbrella cell keratin network: Organization, dependence on the plectin cytolinker, and responses to bladder filling. 大鼠膀胱伞细胞角蛋白网络：组织、对 plectin 细胞连接蛋白的依赖以及对膀胱充盈的反应。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 Epub Date: 2024-10-02 DOI: 10.1091/mbc.E24-06-0262

Wily G Ruiz, Dennis R Clayton, Tanmay Parakala-Jain, Marianela G Dalghi, Jonathan Franks, Gerard Apodaca

{"title":"The rat bladder umbrella cell keratin network: Organization, dependence on the plectin cytolinker, and responses to bladder filling.","authors":"Wily G Ruiz, Dennis R Clayton, Tanmay Parakala-Jain, Marianela G Dalghi, Jonathan Franks, Gerard Apodaca","doi":"10.1091/mbc.E24-06-0262","DOIUrl":"10.1091/mbc.E24-06-0262","url":null,"abstract":"The keratin cytoskeleton and associated desmosomes contribute to the mechanical stability of epithelial tissues, but their organization in native bladder umbrella cells and their responses to bladder filling are poorly understood. Using whole rat bladders in conjunction with confocal microscopy, super-resolution image processing, three-dimensional image reconstruction, and platinum replica electron microscopy, we identified a cortical cytoskeleton network in umbrella cells that was organized as a dense tile-like mesh comprised of tesserae bordered by cortical actin filaments, filled with keratin filaments, and cross-linked by plectin. Below these tesserae, keratin formed a subapical meshwork and at the cell periphery a band of keratin was linked via plectin to the junction-associated actin ring. Disruption of plectin led to focal keratin network dissolution, loss of the junction-associated keratin, and defects in cell-cell adhesion. During bladder filling, a junction-localized necklace of desmosomes expanded, and a subjacent girded layer formed linking the keratin network to desmosomes, including those at the umbrella cell-intermediate cell interface. Our studies reveal a novel tile- and mesh-like organization of the umbrella cell keratin network that is dependent on plectin, that reorganizes in response to bladder filling, and that likely serves to maintain umbrella cell continuity in the face of mechanical distension.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar139"},"PeriodicalIF":3.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11617100/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142365799","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}

引用次数: 0

FAP20 is required for flagellum assembly in Trypanosoma brucei. 布氏锥虫的鞭毛组装需要 FAP20。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 Epub Date: 2024-10-09 DOI: 10.1091/mbc.E23-12-0497

Michelle M Shimogawa, Keya Jonnalagadda, Kent L Hill

{"title":"FAP20 is required for flagellum assembly in Trypanosoma brucei.","authors":"Michelle M Shimogawa, Keya Jonnalagadda, Kent L Hill","doi":"10.1091/mbc.E23-12-0497","DOIUrl":"10.1091/mbc.E23-12-0497","url":null,"abstract":"Trypanosoma brucei is a human and animal pathogen that depends on flagellar motility for transmission and infection. The trypanosome flagellum is built around a canonical \"9+2\" axoneme, containing nine doublet microtubules (DMTs) surrounding two singlet microtubules. Each DMT contains a 13-protofilament A-tubule and a 10-protofilament B-tubule, connected to the A-tubule by a conserved, non-tubulin inner junction (IJ) filament made up of alternating PACRG and FAP20 subunits. Here we investigate FAP20 in procyclic form T. brucei. A FAP20-NeonGreen fusion protein localized to the axoneme as expected. Surprisingly, FAP20 knockdown led to a catastrophic failure in flagellum assembly and concomitant lethality. This differs from other organisms, where FAP20 is required for normal flagellum motility, but generally dispensable for flagellum assembly and viability. Transmission electron microscopy demonstrates failed flagellum assembly in FAP20 mutants is associated with a range of DMT defects and defective assembly of the paraflagellar rod, a lineage-specific flagellum filament that attaches to DMT 4-7 in trypanosomes. Our studies reveal a lineage-specific requirement for FAP20 in trypanosomes, offering insight into adaptations for flagellum stability and motility in these parasites and highlighting pathogen versus host differences that might be considered for therapeutic intervention in trypanosome diseases.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"br22"},"PeriodicalIF":3.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11617092/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142391841","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}

引用次数: 0

Cyclin A/Cdk1 promotes chromosome alignment and timely mitotic progression. Cyclin A/Cdk1 可促进染色体排列和有丝分裂的及时进行。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 Epub Date: 2024-10-02 DOI: 10.1091/mbc.E23-12-0479

Sarah Y Valles, Shrea Bural, Kristina M Godek, Duane A Compton

{"title":"Cyclin A/Cdk1 promotes chromosome alignment and timely mitotic progression.","authors":"Sarah Y Valles, Shrea Bural, Kristina M Godek, Duane A Compton","doi":"10.1091/mbc.E23-12-0479","DOIUrl":"10.1091/mbc.E23-12-0479","url":null,"abstract":"To ensure genomic fidelity, a series of spatially and temporally coordinated events is executed during prometaphase of mitosis, including bipolar spindle formation, chromosome attachment to spindle microtubules at kinetochores, the correction of erroneous kinetochore-microtubule (k-MT) attachments, and chromosome congression to the spindle equator. Cyclin A/Cdk1 kinase plays a key role in destabilizing k-MT attachments during prometaphase to promote correction of erroneous k-MT attachments. However, it is unknown whether Cyclin A/Cdk1 kinase regulates other events during prometaphase. Here, we investigate additional roles of Cyclin A/Cdk1 in prometaphase by using an siRNA knockdown strategy to deplete endogenous Cyclin A from human cells. We find that depleting Cyclin A significantly extends mitotic duration, specifically prometaphase, because chromosome alignment is delayed. Unaligned chromosomes display erroneous monotelic, syntelic, or lateral k-MT attachments suggesting that bioriented k-MT attachment formation is delayed in the absence of Cyclin A. Mechanistically, chromosome alignment is likely impaired because the localization of the kinetochore proteins BUB1 kinase, KNL1, and MPS1 kinase are reduced in Cyclin A-depleted cells. Moreover, we find that Cyclin A promotes BUB1 kinetochore localization independently of its role in destabilizing k-MT attachments. Thus, Cyclin A/Cdk1 facilitates chromosome alignment during prometaphase to support timely mitotic progression.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar141"},"PeriodicalIF":3.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11617097/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142365797","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}

引用次数: 0

Polymer dynamics of Alp7A reveals how two critical concentrations govern assembly of dynamically unstable actin-like proteins. Alp7A 的聚合物动力学揭示了两个临界浓度如何控制动态不稳定的类肌动蛋白的组装。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 Epub Date: 2024-09-25 DOI: 10.1091/mbc.E23-11-0440

Natalie A Petek-Seoane, Johnny Rodriguez, Alan I Derman, Siobhan G Royal, Samuel J Lord, Rosalie Lawrence, Joe Pogliano, R Dyche Mullins

{"title":"Polymer dynamics of Alp7A reveals how two critical concentrations govern assembly of dynamically unstable actin-like proteins.","authors":"Natalie A Petek-Seoane, Johnny Rodriguez, Alan I Derman, Siobhan G Royal, Samuel J Lord, Rosalie Lawrence, Joe Pogliano, R Dyche Mullins","doi":"10.1091/mbc.E23-11-0440","DOIUrl":"10.1091/mbc.E23-11-0440","url":null,"abstract":"Dynamically unstable polymers capture and move cellular cargos in bacteria and eukaryotes, but regulation of their assembly remains poorly understood. Here we describe polymerization of Alp7A, a bacterial actin-like protein (ALP) that distributes copies of plasmid pLS20 among daughter cells in Bacillus subtilis. Purified ATP-Alp7A forms dynamically unstable polymers with a high critical concentration for net assembly (ccN = 10.3 µM), but a much lower critical concentration for filament elongation (ccE = 0.6 µM). Rapid nucleation and stabilization of Alp7A polymers by the accessory factor, Alp7R, decrease ccN into the physiological range. Stable populations of Alp7A filaments appear under two conditions: (i) when Alp7R slows catastrophe rates or (ii) when Alp7A concentrations are high enough to promote filament bundling. These results reveal how dynamic instability maintains high steady-state concentrations of monomeric Alp7A, and how accessory factors regulate Alp7A assembly by modulating ccN independently of ccE.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar145"},"PeriodicalIF":3.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11617094/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142350263","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}

引用次数: 0

Med13 is required for efficient P-body recruitment and autophagic degradation of Edc3 following nitrogen starvation. 氮饥饿后，Edc3 的高效 P 体招募和自噬降解需要 Med13。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 Epub Date: 2024-09-25 DOI: 10.1091/mbc.E23-12-0470

Sara E Hanley, Stephen D Willis, Brittany Friedson, Katrina F Cooper

{"title":"Med13 is required for efficient P-body recruitment and autophagic degradation of Edc3 following nitrogen starvation.","authors":"Sara E Hanley, Stephen D Willis, Brittany Friedson, Katrina F Cooper","doi":"10.1091/mbc.E23-12-0470","DOIUrl":"10.1091/mbc.E23-12-0470","url":null,"abstract":"The Cdk8 kinase module (CKM), a conserved, detachable unit of the Mediator complex, plays a vital role in regulating transcription and communicating stress signals from the nucleus to other organelles. Here, we describe a new transcription-independent role for Med13, a CKM scaffold protein, following nitrogen starvation. In Saccharomyces cerevisiae, nitrogen starvation triggers Med13 to translocate to the cytoplasm. This stress also induces the assembly of conserved membraneless condensates called processing bodies (P-bodies) that dynamically sequester translationally inactive messenger ribonucleoprotein particles. Cytosolic Med13 colocalizes with P-bodies, where it helps recruit Edc3, a highly conserved decapping activator and P-body assembly factor, into these conserved ribonucleoprotein granules. Moreover, Med13 orchestrates the autophagic degradation of Edc3 through a selective cargo-hitchhiking autophagy pathway that utilizes Ksp1 as its autophagic receptor protein. In contrast, the autophagic degradation of Xrn1, another conserved P-body assembly factor, is Med13 independent. These results place Med13 as a new player in P-body assembly and regulation following nitrogen starvation. They support a model in which Med13 acts as a conduit between P-bodies and phagophores, two condensates that use liquid-liquid phase separation in their assembly.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar142"},"PeriodicalIF":3.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11617093/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142350261","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}

引用次数: 0

Nuclear basket proteins regulate the distribution and mobility of nuclear pore complexes in budding yeast. 核篮蛋白调节芽殖酵母中核孔复合体的分布和流动性。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 Epub Date: 2024-09-25 DOI: 10.1091/mbc.E24-08-0371

Janka Zsok, Francois Simon, Göksu Bayrak, Luljeta Isaki, Nina Kerff, Yoana Kicheva, Amy Wolstenholme, Lucien E Weiss, Elisa Dultz

{"title":"Nuclear basket proteins regulate the distribution and mobility of nuclear pore complexes in budding yeast.","authors":"Janka Zsok, Francois Simon, Göksu Bayrak, Luljeta Isaki, Nina Kerff, Yoana Kicheva, Amy Wolstenholme, Lucien E Weiss, Elisa Dultz","doi":"10.1091/mbc.E24-08-0371","DOIUrl":"10.1091/mbc.E24-08-0371","url":null,"abstract":"Nuclear pore complexes (NPCs) mediate all traffic between the nucleus and the cytoplasm and are among the most stable protein assemblies in cells. Budding yeast cells carry two variants of NPCs which differ in the presence or absence of the nuclear basket proteins Mlp1, Mlp2, and Pml39. The binding of these basket proteins occurs very late in NPC assembly and Mlp-positive NPCs are excluded from the region of the nuclear envelope that borders the nucleolus. Here, we use recombination-induced tag exchange to investigate the stability of all the NPC subcomplexes within individual NPCs. We show that the nuclear basket proteins Mlp1, Mlp2, and Pml39 remain stably associated with NPCs through multiple cell-division cycles, and that Mlp1/2 are responsible for the exclusion of NPCs from the nucleolar territory. In addition, we demonstrate that binding of the FG-nucleoporins Nup1 and Nup2 depletes also Mlp-negative NPCs from this region by an independent pathway. We develop a method for single NPC tracking in budding yeast and observe that NPCs exhibit increased mobility in the absence of nuclear basket components. Our data suggest that the distribution of NPCs on the nucleus is governed by multiple interaction of nuclear basket proteins with the nuclear interior.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar143"},"PeriodicalIF":3.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11617099/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142350262","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}

引用次数: 0

G3BP isoforms differentially affect stress granule assembly and gene expression during cellular stress. 在细胞应激过程中，G3BP 同工酶会对应激颗粒的组装和基因表达产生不同影响。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2024-11-01 Epub Date: 2024-10-02 DOI: 10.1091/mbc.E24-02-0062

José M Liboy-Lugo, Carla A Espinoza, Jessica Sheu-Gruttadauria, Jesslyn E Park, Albert Xu, Ziad Jowhar, Angela L Gao, José A Carmona-Negrón, Torsten Wittmann, Natalia Jura, Stephen N Floor

{"title":"G3BP isoforms differentially affect stress granule assembly and gene expression during cellular stress.","authors":"José M Liboy-Lugo, Carla A Espinoza, Jessica Sheu-Gruttadauria, Jesslyn E Park, Albert Xu, Ziad Jowhar, Angela L Gao, José A Carmona-Negrón, Torsten Wittmann, Natalia Jura, Stephen N Floor","doi":"10.1091/mbc.E24-02-0062","DOIUrl":"10.1091/mbc.E24-02-0062","url":null,"abstract":"Stress granules (SGs) are macromolecular assemblies that form under cellular stress. Formation of these membraneless organelles is driven by the condensation of RNA and RNA-binding proteins such as G3BPs. G3BPs form SGs following stress-induced translational arrest. Three G3BP paralogues (G3BP1, G3BP2A, and G3BP2B) have been identified in vertebrates. However, the contribution of different G3BP paralogues to SG formation and gene expression changes is incompletely understood. Here, we probed the functions of G3BPs by identifying important residues for SG assembly at their N-terminal domain such as V11. This conserved amino acid is required for formation of the G3BP-Caprin-1 complex, hence promoting SG assembly. Total RNA sequencing and ribosome profiling revealed that a G3BPV11A mutant leads to changes in mRNA levels and ribosome engagement during the integrated stress response (ISR). Moreover, we found that G3BP2B preferentially forms SGs and promotes changes in mRNA expression under endoplasmic reticulum (ER) stress. Furthermore, our work is a resource for researchers to study gene expression changes under cellular stress. Together, this work suggests that perturbing protein-protein interactions mediated by G3BPs affect SG assembly and gene expression during the ISR, and such functions are differentially regulated by G3BP paralogues under ER stress.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar140"},"PeriodicalIF":3.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11617104/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142365798","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}

引用次数: 0