Cytoskeleton (Hoboken, N.J.)最新文献_第2页

Introducing our Associate Editorial Board: An interview with Agathe Chaigne, Utrecht University, The Netherlands. 介绍我们的副编辑委员会：采访荷兰乌特勒支大学的 Agathe Chaigne。

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-28 DOI: 10.1002/cm.21929

Paul Trevorrow, Agathe Chaigne

引用次数: 0

Multifaceted role of the actin-binding protein WIP: Promotor and inhibitor of tumor progression and dissemination. 肌动蛋白结合蛋白 WIP 的多方面作用：肿瘤进展和扩散的促进因子和抑制因子

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-27 DOI: 10.1002/cm.21935

Jorge Alonso-Eiras, Ines M Anton

{"title":"Multifaceted role of the actin-binding protein WIP: Promotor and inhibitor of tumor progression and dissemination.","authors":"Jorge Alonso-Eiras, Ines M Anton","doi":"10.1002/cm.21935","DOIUrl":"https://doi.org/10.1002/cm.21935","url":null,"abstract":"Cancer cells depend on actin cytoskeleton reorganization to achieve hallmark malignant functions including abnormal activation, proliferation, migration and invasiveness. (Neural)-Wiskott-Aldrich Syndrome protein ((N-)WASP) binds actin and forms a complex with the WASP-interacting protein (WIP), which plays a critical role in regulating the actin cytoskeleton, through (N)-WASP-dependent and independent functions. Mutations in the WIP gene (WIPF1) lead to severe early onset immunodeficiency in humans and severe autoimmunity and shortened lifespan in mice. This review covers the available evidence about the physiological role of WIP in different tissues and its contribution to human disease, focusing on cancer. In solid tumors overexpression of WIP has mostly been associated with tumor initiation, progression and dissemination through matrix degradation by invadopodia, while a suppressive function has been shown for WIP in certain hematological cancers. Interestingly, a minority of studies suggest a protective role for WIP in specific tumor contexts. These data support the need for further research to fully understand the mechanisms underlying WIP's diverse functions in health and disease and raise important questions for future work.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142333681","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Tristetraprolin affects invasion-associated genes expression and cell motility in triple-negative breast cancer model. Tristetraprolin可影响三阴性乳腺癌模型中侵袭相关基因的表达和细胞运动。

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-25 DOI: 10.1002/cm.21934

Anastasiia Hubiernatorova, Josef Novak, Michaela Vaskovicova, David Sekac, Serhii Kropyvko, Zdenek Hodny

{"title":"Tristetraprolin affects invasion-associated genes expression and cell motility in triple-negative breast cancer model.","authors":"Anastasiia Hubiernatorova, Josef Novak, Michaela Vaskovicova, David Sekac, Serhii Kropyvko, Zdenek Hodny","doi":"10.1002/cm.21934","DOIUrl":"https://doi.org/10.1002/cm.21934","url":null,"abstract":"Tristetraprolin (TTP) is an RNA-binding protein that negatively regulates its target mRNAs and has been shown to inhibit tumor progression and invasion. Tumor invasion requires precise regulation of cytoskeletal components, and dysregulation of cytoskeleton-associated genes can significantly alter cell motility and invasive capability. Several genes, including SH3PXD2A, SH3PXD2B, CTTN, WIPF1, and WASL, are crucial components of the cytoskeleton reorganization machinery and are essential for adequate cell motility. These genes are also involved in invasion processes, with SH3PXD2A, SH3PXD2B, WIPF1, and CTTN being key components of invadopodia-specialized structures that facilitate invasion. However, the regulation of these genes is not well understood. This study demonstrates that ectopic expression of TTP in MDA-MB-231 cells leads to decreased mRNA levels of CTTN and SH3PXD2A, as well as defects in cell motility and actin filament organization. Additionally, doxorubicin significantly increases TTP expression and reduces the mRNA levels of cytoskeleton-associated genes, enhancing our understanding of how doxorubicin may affect the transcriptional profile of cells. However, doxorubicin affects target mRNAs differently than TTP ectopic expression, suggesting it may not be the primary mechanism of doxorubicin in breast cancer (BC) treatment. High TTP expression is considered as a positive prognostic marker in multiple cancers, including BC. Given that doxorubicin is a commonly used drug for treating triple-negative BC, using TTP as a prognostic marker in this cohort of patients might be limited since it might be challenging to understand if high TTP expression occurred due to the favorable physiological state of the patient or as a consequence of treatment.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142333684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Distinct molecular features of FLNC mutations, associated with different clinical phenotypes. FLNC 基因突变的不同分子特征与不同的临床表型有关。

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-24 DOI: 10.1002/cm.21922

Klimenko E S, Zaytseva A K, Sorokina M Yu, Perepelina K I, Rodina N L, Nikitina E G, Sukhareva K S, Khudiakov A A, Vershinina T L, Muravyev A S, Mikhaylov E N, Pervunina T M, Vasichkina E S, Kostareva A A

{"title":"Distinct molecular features of FLNC mutations, associated with different clinical phenotypes.","authors":"Klimenko E S, Zaytseva A K, Sorokina M Yu, Perepelina K I, Rodina N L, Nikitina E G, Sukhareva K S, Khudiakov A A, Vershinina T L, Muravyev A S, Mikhaylov E N, Pervunina T M, Vasichkina E S, Kostareva A A","doi":"10.1002/cm.21922","DOIUrl":"https://doi.org/10.1002/cm.21922","url":null,"abstract":"Filamin С is a key an actin-binding protein of muscle cells playing a critical role in maintaining structural integrity and sarcomere organization. FLNC mutations contribute to various types of cardiomyopathies and myopathies through potentially different molecular mechanisms. Here, we described the impact of two clinically distinct FLNC variants (R1267Q associated with arrhythmogenic cardiomyopathy and V2264M associated with restrictive cardiomyopathy) on calcium homeostasis, electrophysiology, and gene expression profile of iPSC-derived patient-specific cardiomyocytes. We demonstrated that R1267Q FLNC variant leads to greater disturbances in calcium dynamics, Nav1.5 kinetics and action potentials compared to V2264M variant. These functional characteristics were accompanied by transcriptome changes in genes linked to action potential and sodium transport as well as structural cardiomyocyte genes. We suggest distinct molecular effects of two FLNC variants linked to different types of cardiomyopathies in terms of myofilament structure, electrophysiology, ion channel function and intracellular calcium homeostasis providing the molecular the bases for their different clinical phenotypes.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142309253","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

F-actin in the cuticular plate and junctions of auditory hair cells is regulated by ADF and cofilin to allow for normal stereocilia bundle patterning and maintenance. 听觉毛细胞角质板和连接处的 F-肌动蛋白受 ADF 和 cofilin 的调控，以实现正常的立体纤毛束模式化和维持。

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-21 DOI: 10.1002/cm.21933

Jamis McGrath, Katelin Hawbaker, Benjamin J Perrin

引用次数: 0

Introducing our Associate Editorial Board-Jayne Aiken, University of Pennsylvania, USA. 介绍我们的副编委--美国宾夕法尼亚大学的杰恩-艾肯（Jayne Aiken）。

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-09 DOI: 10.1002/cm.21915

Paul Trevorrow, Jayne Aiken

引用次数: 0

Exploring the potential role of palladin in modulating human CAF/ECM functional units. 探索 palladin 在调节人类 CAF/ECM 功能单元中的潜在作用。

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-06 DOI: 10.1002/cm.21926

Aleksandr Dolskii, Sérgio A Alcantara Dos Santos, Mark Andrake, Janusz Franco-Barraza, Roland L Dunbrack, Edna Cukierman

{"title":"Exploring the potential role of palladin in modulating human CAF/ECM functional units.","authors":"Aleksandr Dolskii, Sérgio A Alcantara Dos Santos, Mark Andrake, Janusz Franco-Barraza, Roland L Dunbrack, Edna Cukierman","doi":"10.1002/cm.21926","DOIUrl":"https://doi.org/10.1002/cm.21926","url":null,"abstract":"Fibroblasts, crucial for maintaining tissue homeostasis, significantly shape the tumor microenvironment (TME). In pancreatic cancer, a highly aggressive malignancy, cancer-associated fibroblast (CAF)/extracellular matrix (ECM) units dominate the TME, influencing tumor initiation, progression, and treatment responses. Palladin, an actin-associated protein, is vital for fibroblast structural integrity and activation, playing a key role in CAF/ECM functionality. Palladin interacts with cytoskeletal proteins such as alpha-actinin (α-Act) and can therefore regulate other proteins like syndecans, modulating cytoskeletal features, cell adhesion, integrin recycling, and signaling. In this review, we propose that targeting the palladin/α-Act/syndecan interaction network could modulate CAF/ECM units, potentially shifting the TME from a tumor-promoting to a tumor-suppressive state. In silico data and reported studies to suggest that stabilizing palladin-α-Act interactions, via excess palladin, influences syndecan functions; potentially modulating integrin endocytosis via syndecan engagement with protein kinase C alpha as opposed to syndecan binding to α-Act. This mechanism can then affect the distribution of active α5β1-integrin between the plasma membrane and known intracellular vesicular compartments, thereby influencing the tumor-suppressive versus tumor-promoting functions of CAF/ECM units. Understanding these interactions offers likely future therapeutic avenues for stroma normalization in pancreatic and other cancers, aiming to inhibit tumor progression and improve future treatment outcomes.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142141907","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Characterization of open chromatin sensitive to actin polymerization and identification of core-binding factor subunit beta as mechanosensitive nucleocytoplasmic shuttling protein. 对肌动蛋白聚合敏感的开放染色质的特征以及作为机械敏感核细胞质穿梭蛋白的核心结合因子亚基 beta 的鉴定

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-06 DOI: 10.1002/cm.21925

Yaxin Li, Kangjing Li, Fumihiko Nakamura

{"title":"Characterization of open chromatin sensitive to actin polymerization and identification of core-binding factor subunit beta as mechanosensitive nucleocytoplasmic shuttling protein.","authors":"Yaxin Li, Kangjing Li, Fumihiko Nakamura","doi":"10.1002/cm.21925","DOIUrl":"https://doi.org/10.1002/cm.21925","url":null,"abstract":"Mechanotransduction leads to a variety of biological responses including gene expression, changes in cell shape, migration, tissue development, and immune responses. Dysregulation of mechanotransduction is implicated in the progression of various diseases such as cardiovascular diseases and cancer. The actin cytoskeleton plays a crucial role in transmitting mechanical stimuli. Actin filaments, essential for cell motility and shape changes, respond to mechanical cues by remodeling, influencing gene expression via the linker of nucleoskeleton and cytoskeleton complex and mechanosensitive transcription factors. This study employs the dithiobis(succinimidyl propionate) (DSP)-micrococcal nuclease (MNase) proteogenomics method to explore the relationship between cellular mechanosensing, chromatin architecture, and the identification of proteins involved in mechanosensitive nucleocytoplasmic shuttling, revealing how actin polymerization affects chromatin and gene expression. We found that depolymerization of actin filaments by latrunculin B (Lat B) for 30 min is sufficient to alter open chromatin and identified core-binding factor subunit beta as mechanosensitive nucleocytoplasmic shuttling protein.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142141906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Disruption of salt bridge interactions in the inter-domain cleft of the tubulin-like protein FtsZ of Escherichia coli makes cells sensitive to the cell division inhibitor PC190723. 大肠杆菌的类管蛋白 FtsZ 的结构域间隙中的盐桥相互作用被破坏，使细胞对细胞分裂抑制剂 PC190723 敏感。

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-04 DOI: 10.1002/cm.21924

Sakshi Mahesh Poddar, Joyeeta Chakraborty, Pananghat Gayathri, Ramanujam Srinivasan

{"title":"Disruption of salt bridge interactions in the inter-domain cleft of the tubulin-like protein FtsZ of Escherichia coli makes cells sensitive to the cell division inhibitor PC190723.","authors":"Sakshi Mahesh Poddar, Joyeeta Chakraborty, Pananghat Gayathri, Ramanujam Srinivasan","doi":"10.1002/cm.21924","DOIUrl":"https://doi.org/10.1002/cm.21924","url":null,"abstract":"FtsZ forms a ring-like assembly at the site of division in bacteria. It is the first protein involved in the formation of the divisome complex to split the cell into two halves, indicating its importance in bacterial cell division. FtsZ is an attractive target for developing new anti-microbial drugs to overcome the challenges of antibiotic resistance. The most potent inhibitor against FtsZ is PC190723, which is effective against all strains and species of Staphylococcus, including the methicillin- and multi-drug-resistant Staphylococcus aureus and strains of Bacillus. However, FtsZs from bacteria such as E. coli, Streptococcus, and Enterococcus were shown to be resistant to this inhibitor. In this study, we provide further evidence that the three pairwise bridging interactions, between residues S227 and G191, R307 and E198 and D299 and R202, between S7, S9, S10 β-strands and the H7 helix occlude the inhibitor from binding to E. coli FtsZ. We generated single, double and triple mutations to disrupt those bridges and tested the effectiveness of PC190723 directly on Z-ring assembly in vivo. Our results show that the disruption of S227-G191 and R307-E198 bridges render EcFtsZ highly sensitive to PC190723 for Z-ring assembly. Ectopic expression of the double mutants, FtsZ S227I R307V results in hypersensitivity of the susceptible E. coli imp4213 strain to PC190723. Our studies could further predict the effectiveness of PC190723 or its derivatives towards FtsZs of other bacterial genera.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142127551","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Collective effect of Vigna sp. (mung) tubulin GTP hydrolysis rate divergence on microtubule filament assembly. Vigna sp. (mung)管蛋白 GTP 水解速率差异对微管丝组装的集体影响。

Cytoskeleton (Hoboken, N.J.) Pub Date : 2024-09-02 DOI: 10.1002/cm.21923

Jashaswi Basu, Chaitanya A Athale

{"title":"Collective effect of Vigna sp. (mung) tubulin GTP hydrolysis rate divergence on microtubule filament assembly.","authors":"Jashaswi Basu, Chaitanya A Athale","doi":"10.1002/cm.21923","DOIUrl":"https://doi.org/10.1002/cm.21923","url":null,"abstract":"Microtubules (MTs) are dynamic cytoskeletal filaments with highly conserved sequences across evolution, polymerizing by the GTP-dependent assembly of tubulin subunits. Despite the sequence conservation, MT polymerization kinetics diverge quantitatively between vertebrate brain, the model plant Arabidopsis and the protozoan Plasmodium. Previously, tubulin purified from seedlings of the plant Vigna sp. (mung) by temperature cycling was found to have a very low critical concentration. However, the lengths of MTs were sub-micron, much shorter than brain tubulin filaments. This was explained in simulations to be the result of the collective effect of high nucleation and GTP hydrolysis rates. Here, we test the effect of GTPase rates of affinity-purified Vigna sp. tubulin on microtubule polymerization and elongation. Affinity-purified mung tubulin is active and has a critical concentration of .37 μM. The GTP-dependent polymerization kinetics are transient, consistent with previous results. Polymerization is stabilized in the presence of either GTP analog GMPPNP (non-hydrolyzable) or GMPCPP (slow-hydrolyzable). Using interference reflection microscopy (IRM) we find polymerization with the non-hydrolysable analog significantly increases filament numbers, while lengths are unaffected for both GTP analogs. However, prolonged incubation with slow-hydrolyzable GMPCPP results in long filaments, pointing to GTP hydrolysis as a key factor determining MT length. We find the average GTPase turnover number of mung tubulin is 22.8 min-1, compared to 2.04 min-1 for goat brain tubulin. Thus modulating GTPase rates affects both nucleation and elongation. This quantitative divergence in kinetics despite high sequence conservation in the GTPase domains of α- and β-tubulin could help better understand the roles of selective pressure and function in the diverse organisms.","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-09-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142115588","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0