Molecular and Cellular Biology最新文献_第5页

MARBP-lncRNA Complexes Alter Gene Function Through Modulation of Epigenetic Landscape. MARBP-lncRNA复合物通过调控表观遗传景观改变基因功能。

IF 2.7 2区生物学

Molecular and Cellular Biology Pub Date : 2025-01-01 Epub Date: 2025-07-03 DOI: 10.1080/10985549.2025.2519156

Nilanjana Maji, Anindya Dutta, Animesh Anand, Subhrangsu Chatterjee, Samit Chattopadhyay

引用次数: 0

Molecular Function of Midnolin and Its Relevance to Parkinson's Disease. Midnolin的分子功能及其与帕金森病的相关性。

IF 2.7 2区生物学

Molecular and Cellular Biology Pub Date : 2025-01-01 Epub Date: 2025-07-22 DOI: 10.1080/10985549.2025.2535666

Yutaro Obara, Ayano Chiba

{"title":"Molecular Function of Midnolin and Its Relevance to Parkinson's Disease.","authors":"Yutaro Obara, Ayano Chiba","doi":"10.1080/10985549.2025.2535666","DOIUrl":"10.1080/10985549.2025.2535666","url":null,"abstract":"Midnolin (Midn) was originally discovered as a gene expressed specifically in the mouse midbrain at the embryonic developmental stage; MIDN was localized in the nucleus/nucleolus. Although the pathophysiological roles of MIDN remained largely unknown for many years after its discovery, its molecular functions and relevance to diseases have gradually become clearer. In PC12 cells, a rat neuronal model cell line, liquidity factors that are necessary for neurite outgrowth are reported to induce Midn gene expression. In addition, MIDN is required for E3 ubiquitin-protein ligase parkin expression, suggesting that MIDN is important for the development and maintenance of neuronal functions. Notably, it was recently reported that MIDN plays fundamental roles in the ubiquitin-independent proteasomal degradation of various nuclear proteins and transcription factors. Regarding the relationship between MIDN and diseases, copy number loss of MIDN is associated with Parkinson's disease, suggesting that MIDN is a genetic risk factor for this disease. In addition, MIDN is relevant to many types of malignant cancer, including B-cell lymphoma and liver cancer. Thus, MIDN is an essential molecule for the maintenance of homeostasis, and its functional disorder triggers multiple diseases depending on the affected tissues/organs. MIDN therefore shows promise as a potential therapeutic target and prognostic biomarker.","PeriodicalId":18658,"journal":{"name":"Molecular and Cellular Biology","volume":" ","pages":"471-480"},"PeriodicalIF":2.7,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144690902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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

Protein Phosphatase 1 Regulatory Subunit PNUTS Prevents CENP-A Mislocalization and Chromosomal Instability. 蛋白磷酸酶1调控亚基PNUTS防止CENP-A错位和染色体不稳定性。

IF 3.2 2区生物学

Molecular and Cellular Biology Pub Date : 2025-01-01 Epub Date: 2025-04-24 DOI: 10.1080/10985549.2025.2487010

Vinutha Balachandra, Makenzie Thomas, Roshan L Shrestha, Subhash Chandra Sethi, Raj Chari, Shinjen Lin, Ken Chih-Chien Cheng, Tatiana S Karpova, Natasha J Caplen, Munira A Basrai

{"title":"Protein Phosphatase 1 Regulatory Subunit PNUTS Prevents CENP-A Mislocalization and Chromosomal Instability.","authors":"Vinutha Balachandra, Makenzie Thomas, Roshan L Shrestha, Subhash Chandra Sethi, Raj Chari, Shinjen Lin, Ken Chih-Chien Cheng, Tatiana S Karpova, Natasha J Caplen, Munira A Basrai","doi":"10.1080/10985549.2025.2487010","DOIUrl":"10.1080/10985549.2025.2487010","url":null,"abstract":"Chromosomal instability (CIN), a major hallmark of cancer, can be driven by defects in the integrity of centromere or kinetochore structure. Coordinated control of phosphorylation and dephosphorylation activities during cell division is critical to ensure chromosomal stability. Overexpression of the centromeric histone H3 variant CENP-A is observed in many cancers, and its mislocalization to noncentromeric regions promotes CIN. We identified protein phosphatase 1 (PP1) nuclear targeting subunit (PNUTS) as a top candidate in a genome-wide siRNA screen for gene depletions that lead to increased nuclear CENP-A levels. Here, we define a role for PNUTS in preventing CENP-A mislocalization and CIN. Depletion of PNUTS resulted in high nuclear CENP-A levels throughout the cell cycle in a PP1-dependent manner. Consistent with these results, mislocalization of CENP-A and its interacting partner CENP-C were observed on mitotic chromosomes from PNUTS-depleted cells. Defects in kinetochore integrity and CIN phenotypes were also observed in PNUTS-depleted cells. Mechanistically, we show that depletion of the histone H3.3 chaperone DAXX suppresses the mislocalization of CENP-A and micronuclei incidence in PNUTS-depleted cells. In summary, our studies highlight the importance of phospho-regulation mediated by PNUTS in preventing CENP-A mislocalization and CIN.","PeriodicalId":18658,"journal":{"name":"Molecular and Cellular Biology","volume":" ","pages":"185-197"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143972177","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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

An Intrinsically Disordered Region of the FACT Subunit, Spt16, Promotes Chromatin Disassembly in Stimulating the Pre-Initiation Complex Formation at the Promoter for Transcription Initiation In Vivo. 在体内，FACT亚基Spt16的内在紊乱区域促进染色质分解，刺激转录起始启动子处的起始前复合物形成。

IF 3.2 2区生物学

Molecular and Cellular Biology Pub Date : 2025-01-01 Epub Date: 2025-05-23 DOI: 10.1080/10985549.2025.2501630

Priyanka Barman, Sukesh R Bhaumik

{"title":"An Intrinsically Disordered Region of the FACT Subunit, Spt16, Promotes Chromatin Disassembly in Stimulating the Pre-Initiation Complex Formation at the Promoter for Transcription Initiation In Vivo.","authors":"Priyanka Barman, Sukesh R Bhaumik","doi":"10.1080/10985549.2025.2501630","DOIUrl":"10.1080/10985549.2025.2501630","url":null,"abstract":"Previous structural and biochemical studies revealed that a negatively charged intrinsically disordered region (IDR) at the C-terminal of the Spt16 subunit of an evolutionarily conserved heterodimeric histone chaperone, FACT (Facilitates chromatin transcription), interacts with histone H2A-H2B dimer, and hence interferes the interaction of DNA with histone H2A-H2B dimer. However, the functional relevance of the binding of Spt16's IDR to histone H2A-H2B dimer with impact on chromatin dynamics and transcription has not been clearly elucidated in living cells. Here, we show that Spt16's IDR facilitates the eviction of histone H2A-H2B dimer (and hence chromatin disassembly) from the inducible GAL promoters upon transcription induction. Such facilitation of chromatin disassembly by Spt16's IDR stimulates the pre-initiation complex (PIC) formation at the promoter, and hence transcription initiation. Further, we find that Spt16's IDR regulates chromatin reassembly at the coding sequence in the wake of elongating RNA polymerase II. Collectively, our results reveal that Spt16's IDR facilitates promoter chromatin disassembly for stimulation of the PIC formation for transcription initiation with additional function in chromatin reassembly at the coding sequence in the wake of elongating RNA polymerase II, thus illuminating novel IDR regulation of chromatin dynamics and transcription in vivo.","PeriodicalId":18658,"journal":{"name":"Molecular and Cellular Biology","volume":" ","pages":"263-282"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144128156","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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

Net1 Controls Src Activation to Regulate Breast Cancer Cell Motility and Invasion. Net1控制Src激活调节乳腺癌细胞运动和侵袭

IF 2.7 2区生物学

Molecular and Cellular Biology Pub Date : 2025-01-01 Epub Date: 2025-08-05 DOI: 10.1080/10985549.2025.2536115

Yan Zuo, Heather S Carr, Wen Li, Songlin Zhang, Jeffrey A Frost

{"title":"Net1 Controls Src Activation to Regulate Breast Cancer Cell Motility and Invasion.","authors":"Yan Zuo, Heather S Carr, Wen Li, Songlin Zhang, Jeffrey A Frost","doi":"10.1080/10985549.2025.2536115","DOIUrl":"10.1080/10985549.2025.2536115","url":null,"abstract":"The cytoplasmic tyrosine kinase Src supports many phenotypes in cancer cells, including proliferation, migration and invasion, survival, and metastasis. We have previously shown that Src promotes cytoplasmic localization of the RhoGEF Net1, where it stimulates RhoA activation, breast cancer cell motility, and extracellular matrix invasion. In the present work, we show that the Net1 expression in human breast tumors correlates with Src phosphorylation on its activating site Y419. We also show in human breast cancer cell lines that endogenous Net1 and Src interact, and that Net1 expression is required for full Src activation. Net1 must localize to the cytosol to promote Src activation, but surprisingly, the catalytic activity of Net1 toward Rho GTPases is not necessary for Src activation. Instead, Net1 requires interaction with the scaffolding protein Dlg1. Dlg1 knockdown prevents Src activation by Net1 and precludes interaction between Net1 and Src. Moreover, Net1 knockdown cooperates with small molecule inhibition of Src to inhibit breast cancer cell motility and extracellular matrix invasion. These data show a previously unrecognized relationship between Net1 and Src in human breast tumors and breast cancer cell lines, and suggest that therapeutic targeting of Net1 may be of benefit in breast cancers with elevated Src activity.","PeriodicalId":18658,"journal":{"name":"Molecular and Cellular Biology","volume":" ","pages":"419-437"},"PeriodicalIF":2.7,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144789555","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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

Midnolin, a Genetic Risk Factor for Parkinson’s Disease, Promotes Neurite Outgrowth Accompanied by Early Growth Response 1 Activation in PC12 Cells 帕金森病的遗传风险因子 Midnolin 能促进 PC12 细胞中神经元的生长，同时激活早期生长应答 1

IF 5.3 2区生物学

Molecular and Cellular Biology Pub Date : 2024-09-12 DOI: 10.1080/10985549.2024.2399358

Ayano Chiba Chisato Kato Tadashi Nakagawa Tsukasa Osaki Kohei Nakamura Ikuo Norota Mikako Nagashima Toru Hosoi Kuniaki Ishii Yutaro Obara a Department of Pharmacology, Yamagata University School of Medicine, Yamagata, Japanb Department of Clinical Pharmacology, Faculty of Pharmaceutical Sciences, Sanyo-Onoda City University, Sanyo Onoda, Japanc Department of Biochemistry and Molecular Biology, Yamagata University School of Medicine, Yamagata, Japan

引用次数: 0

Statement of Retraction: FLIP Protects against Hypoxia/Reoxygenation-Induced Endothelial Cell Apoptosis by Inhibiting Bax Activation. 撤回声明：FLIP通过抑制Bax活化防止缺氧/再氧诱导的内皮细胞凋亡

IF 3.2 2区生物学

Molecular and Cellular Biology Pub Date : 2024-09-03 DOI: 10.1080/10985549.2024.2396764

引用次数: 0

Selective Hypoxia-Sensitive Oxomer Formation by FIH Prevents Binding of the NF-κB Inhibitor IκBβ to NF-κB Subunits FIH选择性缺氧敏感氧化物形成可阻止NF-κB抑制剂IκBβ与NF-κB亚基结合

IF 5.3 2区生物学

Molecular and Cellular Biology Pub Date : 2024-04-22 DOI: 10.1080/10985549.2024.2338727

Yulia L. VolkovaAgnieszka E. JuchtNina OechslerRoopesh KrishnankuttyAlex von KriegsheimRoland H. WengerCarsten C. Scholza Institute of Physiology, University of Zurich, Zurich, Switzerlandb Institute of Physiology, University Medicine Greifswald, Greifswald, Germanyc Institute of Genetics and Cancer, University of Edinburgh, UK

引用次数: 0

Endogenous EWSR1 Exists in Two Visual Modalities That Reflect Its Associations with Nucleic Acids and Concentration at Sites of Active Transcription 内源性 EWSR1 存在于两种视觉模式，反映了它与核酸的关联以及在活性转录位点的浓度

IF 5.3 2区生物学

Molecular and Cellular Biology Pub Date : 2024-03-20 DOI: 10.1080/10985549.2024.2315425

Soumya Sundara RajanVernon J. EbegboniPatricio PichlingKatelyn R. LudwigTamara L. JonesRaj ChariAndy TranMichael J. KruhlakJadranka LoncarekNatasha J. Caplena Functional Genetics Section, Genetics Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USAb Genome Modification Core, Laboratory Animal Sciences Program, Frederick National Lab for Cancer Research, Frederick, Maryland, USAc CCR Confocal Microscopy Core Facility, Laboratory of Cancer Biology and Genetics, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USAd Centrosome Biology Section, Cancer Innovation Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA

引用次数: 0

Uncovering the Role of the Yeast Lysine Acetyltransferase NuA4 in the Regulation of Nuclear Shape and Lipid Metabolism. 揭示酵母赖氨酸乙酰转移酶 NuA4 在核形状和脂质代谢调控中的作用

IF 3.2 2区生物学

Molecular and Cellular Biology Pub Date : 2024-01-01 Epub Date: 2024-07-04 DOI: 10.1080/10985549.2024.2366206

Sarah Jane Laframboise, Lauren F Deneault, Alix Denoncourt, Michael Downey, Kristin Baetz

{"title":"Uncovering the Role of the Yeast Lysine Acetyltransferase NuA4 in the Regulation of Nuclear Shape and Lipid Metabolism.","authors":"Sarah Jane Laframboise, Lauren F Deneault, Alix Denoncourt, Michael Downey, Kristin Baetz","doi":"10.1080/10985549.2024.2366206","DOIUrl":"10.1080/10985549.2024.2366206","url":null,"abstract":"Here, we report a novel role for the yeast lysine acetyltransferase NuA4 in regulating phospholipid availability for organelle morphology. Disruption of the NuA4 complex results in 70% of cells displaying nuclear deformations and nearly 50% of cells exhibiting vacuolar fragmentation. Cells deficient in NuA4 also show severe defects in the formation of nuclear-vacuole junctions (NJV), as well as a decrease in piecemeal microautophagy of the nucleus (PMN). To determine the cause of these defects we focused on Pah1, an enzyme that converts phosphatidic acid into diacylglycerol, favoring accumulation of lipid droplets over phospholipids that are used for membrane expansion. NuA4 subunit Eaf1 was required for Pah1 localization to the inner nuclear membrane and artificially tethering of Pah1 to the nuclear membrane rescued nuclear deformation and vacuole fragmentation defects, but not defects related to the formation of NVJs. Mutation of a NuA4-dependent acetylation site on Pah1 also resulted in aberrant Pah1 localization and defects in nuclear morphology and NVJ. Our work suggests a critical role for NuA4 in organelle morphology that is partially mediated through the regulation of Pah1 subcellular localization.","PeriodicalId":18658,"journal":{"name":"Molecular and Cellular Biology","volume":" ","pages":"273-288"},"PeriodicalIF":3.2,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11253884/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141498377","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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