Molecular Biology of the Cell最新文献

Isoform-specific phosphorylation of axonemal dynein heavy chains. 轴突动力蛋白重链的异构体特异性磷酸化。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-04-23 DOI: 10.1091/mbc.E25-03-0116

Miho Sakato-Antoku, Ramila S Patel-King, Kazuo Inaba, Jeremy L Balsbaugh, Stephen M King

{"title":"Isoform-specific phosphorylation of axonemal dynein heavy chains.","authors":"Miho Sakato-Antoku, Ramila S Patel-King, Kazuo Inaba, Jeremy L Balsbaugh, Stephen M King","doi":"10.1091/mbc.E25-03-0116","DOIUrl":"10.1091/mbc.E25-03-0116","url":null,"abstract":"Axonemal dyneins power ciliary motility and phosphorylation of key intermediate and light chain components affects the regulation and properties of these motors in very distantly related organisms. It is also known that many axonemal dynein heavy chains are subject to this posttranslational modification although this has been little studied. Here we examine axonemal dynein heavy chains from a broad range of ciliated eukaryotes and identify phosphorylated sites embedded within various kinase recognition motifs such as those for protein kinase A, protein kinase C, and casein kinase II. Mapping these sites onto discrete heavy chain types reveals class-specific locations apparently mediated by different kinases. For example, we find that all Chlamydomonas α heavy chain phosphorylation sites are in an extended loop derived from AAA5 that arches over the coiled-coil buttress which in turn interacts with the microtubule-binding stalk. In contrast, most sites in the monomeric inner arm dyneins occur very close to the N-terminus and may be involved in assembly processes. In Chlamydomonas, the two cilia (termed cis and trans) exhibit different intrinsic beat frequencies and we identify cilium-specific phosphorylation patterns on both the α heavy chain and outer arm docking complex consistent with differential regulation of these motors in the two organelles.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":"36 6","pages":"ar67"},"PeriodicalIF":3.1,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144028398","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}

引用次数: 0

Inducible FAK loss but not FAK inhibition in endothelial cells of PYK2-null mice activates p53 tumor suppressor to prevent tumor growth. pyk2缺失小鼠内皮细胞诱导FAK缺失而非FAK抑制激活p53肿瘤抑制因子，阻止肿瘤生长。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-04-09 DOI: 10.1091/mbc.E24-12-0562

Xiao Lei Chen, Marjaana Ojalill, Christine Jean, Isabelle Tancioni, Shulin Jiang, Antonia Boyer, Duygu Ozmadenci, Sean Uryu, David Tarin, Joseph Schlessinger, Dwayne G Stupack, David D Schlaepfer

{"title":"Inducible FAK loss but not FAK inhibition in endothelial cells of PYK2-null mice activates p53 tumor suppressor to prevent tumor growth.","authors":"Xiao Lei Chen, Marjaana Ojalill, Christine Jean, Isabelle Tancioni, Shulin Jiang, Antonia Boyer, Duygu Ozmadenci, Sean Uryu, David Tarin, Joseph Schlessinger, Dwayne G Stupack, David D Schlaepfer","doi":"10.1091/mbc.E24-12-0562","DOIUrl":"10.1091/mbc.E24-12-0562","url":null,"abstract":"Focal adhesion kinase (FAK) and the related tyrosine kinase PYK2 are signaling and scaffolding proteins co-expressed in endothelial cells (ECs) that regulate blood vessel function and tumor growth. As FAK-PYK2 share overlapping cellular roles, we generated PYK2-/- FAKfl/fl mice with tamoxifen-inducible EC-specific Cre expression. EC FAK inactivation in PYK2-/- but not PYK2+/+ mice led to increased heart and lung mass, vascular leakage, and created a tumor microenvironment that was repressive to syngeneic melanoma, breast, and lung carcinoma implanted tumor growth. Tumor suppression was associated with defective vessel sprouting, enhanced p53 tumor suppressor and p21CIP1 protein expression in ECs, elevated markers of DNA damage, and altered blood cytokine levels in tumor-bearing mice. However, EC-specific hemizygous kinase-defective (KD) FAK expression in EC FAK-/KD PYK2-/- mice was not associated with elevated p53 levels. Instead, EC FAK-/KD PYK2-/- mice supported primary tumor growth but prevented metastasis, implicating EC FAK activity in tumor spread. In vitro, combined genetic or small molecule FAK-PYK2 knockdown in ECs or tumor cells elevated p21CIP1 and prevented cell proliferation in a p53-dependent manner, highlighting a linkage between EC FAK-PYK2 loss and p53 activation in tumor regulation.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":"36 6","pages":"ar64"},"PeriodicalIF":3.1,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144028358","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}

引用次数: 0

Hsp70 chaperones, Ssa1 and Ssa2, limit poly(A) binding protein aggregation. Hsp70伴侣，Ssa1和Ssa2，限制聚(A)结合蛋白聚集。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-04-09 DOI: 10.1091/mbc.E25-01-0027

Hannah E Buchholz, Sean A Martin, Jane E Dorweiler, Claire M Radtke, Adam S Knier, Natalia B Beans, Anita L Manogaran

{"title":"Hsp70 chaperones, Ssa1 and Ssa2, limit poly(A) binding protein aggregation.","authors":"Hannah E Buchholz, Sean A Martin, Jane E Dorweiler, Claire M Radtke, Adam S Knier, Natalia B Beans, Anita L Manogaran","doi":"10.1091/mbc.E25-01-0027","DOIUrl":"10.1091/mbc.E25-01-0027","url":null,"abstract":"Molecular chaperones play a central role in maintaining protein homeostasis. The highly conserved Hsp70 family of chaperones have major functions in folding of nascent peptides, protein refolding, and protein aggregate disassembly. In yeast, loss of two Hsp70 proteins, Ssa1 and Ssa2, is associated with decreased cellular growth and shortened lifespan. While heterologous or mutant temperature-sensitive proteins form anomalous large cytoplasmic inclusions in ssa1Δssa2Δ strains, it is unclear how endogenous wild-type proteins behave and are regulated in the presence of limiting Hsp70s. Using the wild-type yeast Poly A binding protein (Pab1), which is involved in mRNA binding and forms stress granules (SGs) upon heat shock, Pab1 forms large inclusions in approximately half of ssa1Δssa2Δ cells in the absence of stress. Overexpression of Ssa1, Hsp104, and Sis1 almost completely limits the formation of these large inclusions in ssa1Δssa2Δ, suggesting that excess Ssa1, Hsp104, and Sis1 can each compensate for the lower levels of Ssa proteins. Upon heat shock, SGs also form in cells whether large Pab1 inclusions are present or not. Surprisingly, cells containing only SGs disassemble faster than wild type, whereas cells with both large inclusions disassemble slower albeit completely. We suspect that disassembly of these large inclusions is linked to the elevated heat shock response and elevated Hsp104 and Sis1 levels in ssa1Δssa2Δ strains. We also observed that wild-type cultures grown to saturation also form large Pab1-GFP inclusions. These inclusions can be partially rescued by overexpression of Ssa1. Taken together, our data suggest that Hsp70 not only plays a role in limiting unwanted protein aggregation in normal cells, but as cells age, the depletion of active Hsp70 possibly underlies the age-related aggregation of endogenous proteins.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":"36 6","pages":"ar66"},"PeriodicalIF":3.1,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143972190","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}

引用次数: 0

Optimized vectors for genetic engineering of Aureobasidium pullulans. 普鲁兰小孢子菌基因工程载体优化。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-04-09 DOI: 10.1091/mbc.E25-02-0059

Analeigha V Colarusso, Audrey M Williams, Amy S Gladfelter, Alison C E Wirshing, Daniel J Lew

引用次数: 0

Cell confluency affects p53 dynamics in response to DNA damage. 细胞融合影响p53动态响应DNA损伤。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-04-09 DOI: 10.1091/mbc.E24-09-0394

Alina Simerzin, Emily E Ackerman, Kotaro Fujimaki, Rainer H Kohler, Yoshiko Iwamoto, Mathias S Heltberg, Ashwini Jambhekar, Ralph Weissleder, Galit Lahav

{"title":"Cell confluency affects p53 dynamics in response to DNA damage.","authors":"Alina Simerzin, Emily E Ackerman, Kotaro Fujimaki, Rainer H Kohler, Yoshiko Iwamoto, Mathias S Heltberg, Ashwini Jambhekar, Ralph Weissleder, Galit Lahav","doi":"10.1091/mbc.E24-09-0394","DOIUrl":"10.1091/mbc.E24-09-0394","url":null,"abstract":"The tumor suppressor protein p53 plays a key role in the cellular response to DNA damage. In response to DNA double-strand breaks (DSB), cultured cells exhibit oscillations of p53 levels, which impact gene expression and cell fate. The dynamics of p53 in vivo have only been studied in fixed tissues or using reporters for p53's transcriptional activity. Here we established breast tumors expressing a fluorescent reporter for p53 levels and employed intravital imaging to quantify its dynamics in response to DSB in vivo. Our findings revealed large heterogeneity among individual cells, with most cells exhibiting a single prolonged pulse. We then tested how p53 dynamics might change under high cell confluency, one factor that differs between cell culture and tissues. We revealed that highly confluent cultured breast cancer cells also show one broad p53 pulse instead of oscillations. Through mathematical modeling, sensitivity analysis, and live-cell imaging, we identified low levels of the phosphatase Wip1, a transcriptional target and negative regulator of p53, as a key contributor to these dynamics. Because high cell confluency better reflects the microenvironment of tissues, the impact of cell confluency on p53 dynamics may have important consequences for cancerous tissues responding to DNA damage-inducing therapies.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":"36 6","pages":"br16"},"PeriodicalIF":3.1,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144027286","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}

引用次数: 0

M phase-specific generation of supernumerary centrioles in cancer cells. 癌细胞中多余中心粒的阶段性特异性产生。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-04-23 DOI: 10.1091/mbc.E24-08-0386

Byungho Shin, Myungse Kim, Yejoo Lee, Kunsoo Rhee

引用次数: 0

Deep learning-driven imaging of cell division and cell growth across an entire eukaryotic life cycle. 在整个真核生物生命周期中细胞分裂和细胞生长的深度学习驱动成像。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-05-06 DOI: 10.1091/mbc.E25-01-0009

Taylor Kennedy, Berk Yalcinkaya, Shreya Ramakanth, Sandhya Neupane, Nika Tadić, Nicolas E Buchler, Orlando Argüello-Miranda

{"title":"Deep learning-driven imaging of cell division and cell growth across an entire eukaryotic life cycle.","authors":"Taylor Kennedy, Berk Yalcinkaya, Shreya Ramakanth, Sandhya Neupane, Nika Tadić, Nicolas E Buchler, Orlando Argüello-Miranda","doi":"10.1091/mbc.E25-01-0009","DOIUrl":"10.1091/mbc.E25-01-0009","url":null,"abstract":"The life cycle of eukaryotic microorganisms involves complex transitions between states such as dormancy, mating, meiosis, and cell division, which are often studied independently from each other. Therefore, most microbial life cycles are theoretical reconstructions from partial observations of cellular states. Here we show that complete microbial life cycles can be directly and continuously studied by combining microfluidic culturing, life cycle stage-specific segmentation of micrographs, and a novel cell tracking algorithm, FIEST, based on deep learning video frame interpolation. As proof of principle, we quantitatively imaged and compared cell growth and the activity state of the cell division kinase, Cdk1, across the life cycle of Saccharomyces cerevisiae for up to three sexually reproducing generations. Our analysis of S. cerevisiae's life cycle provided the following new insights: 1) the accumulation of cell cycle regulators, such as Whi5, is tailored to each life cycle stage; 2) cell growth always preceded exit from nonproliferative states in our conditions; 3) the temporal coordination of meiotic events is the same across sexually reproducing populations when each generation is exposed to same conditions; 4) information such as cell size and morphology resets after each sexual reproduction cycle. Image processing and tracking algorithms are available as the Python package Yeastvision, which could be used study pathogens such as Candida glabrata, Cryptococcus neoformans, Colletotrichum acutatum, and other unicellular systems.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar74"},"PeriodicalIF":3.1,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144004303","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}

引用次数: 0

The Kinesin-14 tail: Dual microtubule binding domains drive spindle morphogenesis through tight microtubule cross-linking and robust sliding. Kinesin-14尾部：双微管结合域通过紧密的微管交联和稳健的滑动驱动纺锤体形态发生。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-05-06 DOI: 10.1091/mbc.E25-02-0083

Stephanie C Ems-McClung, MacKenzie Cassity, Anjaly Prasannajith, Claire E Walczak

{"title":"The Kinesin-14 tail: Dual microtubule binding domains drive spindle morphogenesis through tight microtubule cross-linking and robust sliding.","authors":"Stephanie C Ems-McClung, MacKenzie Cassity, Anjaly Prasannajith, Claire E Walczak","doi":"10.1091/mbc.E25-02-0083","DOIUrl":"10.1091/mbc.E25-02-0083","url":null,"abstract":"Proper spindle assembly requires the Kinesin-14 (K-14) family of motors to organize microtubules (MT) into the bipolar spindle by cross-linking and sliding antiparallel and parallel MTs through their motor and tail domains. How they mediate these different activities is unclear. We identified two MT-binding domains (MBD1 and MBD2) within the Xenopus K-14 XCTK2 tail and found that MBD1 MT affinity was weaker than MBD2. Comparable with full-length GFP-XCTK2 wild-type protein (GX-WT), GFP-XCTK2 containing the MBD1 mutations (GX-MBD1mut) stimulated spindle assembly, localized moderately on the spindle, and formed narrow spindles. In contrast, GX-MBD2mut only partially stimulated spindle assembly, localized weakly on the spindle, and formed shorter spindles. Biochemical reconstitution of MT cross-linking and sliding demonstrated that GX-MBD2mut slid antiparallel MTs faster than GX-WT and GX-MBD1mut. However, GX-WT and GX-MBD1mut statically cross-linked the majority of parallel MTs, whereas GX-MBD2mut equally slid and statically cross-linked parallel MTs without affecting their sliding velocity. These results provide a mechanism by which the two different MBDs in the K-14 tail balance antiparallel MT sliding velocity (MBD1) and tight parallel MT cross-linking (MBD2), which are important for spindle assembly and localization, and provide a basis for characterizing how molecular motors organize MTs within the spindle.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar72"},"PeriodicalIF":3.1,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144028037","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}

引用次数: 0

M. tuberculosis surface sulfoglycolipid SL-1 activates the mechanosensitive channel TRPV4 to enhance lysosomal biogenesis and exocytosis in macrophages. 结核分枝杆菌表面巯基糖脂SL-1激活机械敏感通道TRPV4，促进巨噬细胞溶酶体生物生成和胞吐。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-04-30 DOI: 10.1091/mbc.E24-12-0560

Ibrahim Umar, Shah-E-Jahan Gulzar, Varadharajan Sundaramurthy

{"title":"M. tuberculosis surface sulfoglycolipid SL-1 activates the mechanosensitive channel TRPV4 to enhance lysosomal biogenesis and exocytosis in macrophages.","authors":"Ibrahim Umar, Shah-E-Jahan Gulzar, Varadharajan Sundaramurthy","doi":"10.1091/mbc.E24-12-0560","DOIUrl":"10.1091/mbc.E24-12-0560","url":null,"abstract":"Intracellular pathogens manipulate host cellular pathways to ensure their survival. Mycobacterium tuberculosis (Mtb) disrupts phagosomal trafficking to prevent fusion with lysosomes. Beyond this localized effect, Mtb globally remodels the host lysosomal system, predominantly through its virulence-associated surface lipid, sulfolipid-1 (SL-1). SL-1 enhances lysosomal biogenesis via the mTORC1-TFEB axis; however, the upstream mediators remain unknown. Here, we show that SL-1 induces calcium influx into macrophages and identify the mechanosensitive calcium channel transient receptor potential vanilloid subtype 4 (TRPV4) as a crucial upstream mediator of SL-1-induced lysosomal remodeling. TRPV4 influences multiple aspects of lysosomal function, including biogenesis, acidification, enzymatic activity, phagosome maturation, and lysosomal exocytosis. These effects are recapitulated during Mtb infection, underscoring the relevance of SL-1- and TRPV4-dependent lysosomal remodeling in an infection context. TRPV4 expression is upregulated during Mtb infection and partially localizes to both lysosomes and the Mtb-containing vacuole. Remarkably, TRPV4 activation, independent of SL-1, is sufficient to enhance lysosomal biogenesis, identifying TRPV4 as a key regulator of lysosomal homeostasis. Together, these findings uncover a novel mechanism of lysosomal remodeling driven by a pathogen lipid virulence factor and reveal a previously unrecognized role for TRPV4 in modulating lysosomal homeostasis in macrophages.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":" ","pages":"ar76"},"PeriodicalIF":3.1,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144033753","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}

引用次数: 0

New insights into nuclear import and nucleolar localization of yeast RNA exosome subunits. 酵母RNA外泌体亚基核输入和核仁定位的新见解。

IF 3.1 3区生物学

Molecular Biology of the Cell Pub Date : 2025-06-01 Epub Date: 2025-04-23 DOI: 10.1091/mbc.E25-02-0078

Valdir Gomes Neto, Leidy Paola P Cepeda, Bruno R S Queiroz, Sylvain Cantaloube, Isabelle Leger-Silvestre, Thomas Mangeat, Benjamin Albert, Olivier Gadal, Carla C Oliveira

{"title":"New insights into nuclear import and nucleolar localization of yeast RNA exosome subunits.","authors":"Valdir Gomes Neto, Leidy Paola P Cepeda, Bruno R S Queiroz, Sylvain Cantaloube, Isabelle Leger-Silvestre, Thomas Mangeat, Benjamin Albert, Olivier Gadal, Carla C Oliveira","doi":"10.1091/mbc.E25-02-0078","DOIUrl":"10.1091/mbc.E25-02-0078","url":null,"abstract":"The RNA exosome is a multiprotein complex essential for RNA maturation and degradation. In budding yeast, a nine-subunit protein core (Exo9) associated with Rrp44 forms a 10-subunit complex (Exo10) in the cytoplasm and, in complex with Rrp6, Exo11 in the nucleus. Depending on its subcellular localization, the exosome interacts with different cofactors and RNA substrates. In the cytoplasm, Exo10 associates with the SKI complex via Ski7, while in the nucleus, Exo11 interacts with the TRAMP complex. Within the nucleolus, the exosome participates in rRNA processing, facilitated by Mtr4-dependent adaptors Utp18 and Nop53. In this article, we have performed a comprehensive study that addresses the targeting mechanism and precise subcellular localization of all members of the Exo11 complex. We observed a high concentration of all Exo11 subunits in the nucleolus and identified the importins Srp1 (α) and Kap95 (β) as responsible for the nuclear import of Exo9 subunits. Notably, Exo9 subunits localization was not significantly disrupted in the simultaneous absence of NLS-containing subunits Rrp6 and Rrp44, suggesting redundant nuclear import pathways for Exo9. Additionally, we show evidence that Ski7 may play a role in the Exo9 retention in the cytoplasm. To explore the exosome subnucleolar localization, we compared Rrp43 with nuclear exosome cofactors and show that it is enriched in the same nucleolar region as Mtr4 and Nop53. In conclusion, our findings provide a detailed characterization of Exo11 distribution, highlight the primary nuclear import mechanisms for Exo9, and reveal the specific localization of the exosome within the granular component of the yeast nucleolus, suggesting a spatial regulation of the RNA-processing pathway.","PeriodicalId":18735,"journal":{"name":"Molecular Biology of the Cell","volume":"36 6","pages":"ar69"},"PeriodicalIF":3.1,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144023649","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}

引用次数: 0