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[PMID]:28295256
[Au] Autor:Komatsu S; Kitazawa T; Ikebe M
[Ad] Endereço:Department of Cellular and Molecular Biology, The University of Texas Health Science Center at Tyler, Tyler, Texas.
[Ti] Título:Visualization of stimulus-specific heterogeneous activation of individual vascular smooth muscle cells in aortic tissues.
[So] Source:J Cell Physiol;233(1):434-446, 2018 Jan.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Intercellular communication among autonomic nerves, endothelial cells (ECs), and vascular smooth muscle cells (VSMCs) plays a central role in an uninterrupted regulation of blood flow through vascular contractile machinery. Impairment of this communication is linked to development of vascular diseases such as hypertension, cerebral/coronary vasospasms, aortic aneurism, and erectile dysfunction. Although the basic concept of the communication as a whole has been studied, the spatiotemporal correlation of ECs/VSMCs in tissues at the cellular level is unknown. Here, we show a unique VSMC response to ECs during contraction and relaxation of isolated aorta tissues through visualization of spatiotemporal activation patterns of smooth muscle myosin II. ECs in the intimal layer dictate the stimulus-specific heterogeneous activation pattern of myosin II in VSMCs within distinct medial layers. Myosin light chain (MLC) phosphorylation (active form of myosin II) gradually increases towards outer layers (approximately threefold higher MLC phosphorylation at the outermost layer than that of the innermost layer), presumably by release of an intercellular messenger, nitric oxide (NO). Our study also demonstrates that the MLC phosphorylation at the outermost layer in spontaneously hypertensive rats (SHR) during NO-induced relaxation is quite high and approximately 10-fold higher than that of its counterpart, the Wister-Kyoto rats (WKY), suggesting that the distinct pattern of myosin II activation within tissues is important for vascular protection against elevated blood pressure.
[Mh] Termos MeSH primário: Células Endoteliais/fisiologia
Imunofluorescência
Microscopia de Fluorescência
Músculo Liso Vascular/fisiologia
Miócitos de Músculo Liso/fisiologia
Vasoconstrição
[Mh] Termos MeSH secundário: Animais
Aorta Torácica/metabolismo
Aorta Torácica/fisiologia
Biomarcadores
Comunicação Celular
Modelos Animais de Doenças
Células Endoteliais/metabolismo
Hipertensão/metabolismo
Hipertensão/fisiopatologia
Técnicas In Vitro
Músculo Liso Vascular/metabolismo
Miócitos de Músculo Liso/metabolismo
Cadeias Leves de Miosina/metabolismo
Miosina Tipo II/metabolismo
Óxido Nítrico/metabolismo
Fosforilação
Ratos Endogâmicos SHR
Ratos Endogâmicos WKY
Fatores de Tempo
Vasodilatação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Myosin Light Chains); 31C4KY9ESH (Nitric Oxide); EC 3.6.1.- (Myosin Type II)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171224
[Lr] Data última revisão:
171224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25903


  2 / 1290 MEDLINE  
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[PMID]:27773487
[Au] Autor:Coravos JS; Martin AC
[Ad] Endereço:Department of Biology, Massachusetts Institute of Technology, 31 Ames Street, Cambridge, MA 02142, USA.
[Ti] Título:Apical Sarcomere-like Actomyosin Contracts Nonmuscle Drosophila Epithelial Cells.
[So] Source:Dev Cell;39(3):346-358, 2016 11 07.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Actomyosin networks generate contractile force that changes cell and tissue shape. In muscle cells, actin filaments and myosin II appear in a polarized structure called a sarcomere, in which myosin II is localized in the center. Nonmuscle cortical actomyosin networks are thought to contract when nonmuscle myosin II (myosin) is activated throughout a mixed-polarity actin network. Here, we identified a mutant version of the myosin-activating kinase, ROCK, that localizes diffusely, rather than centrally, in epithelial cell apices. Surprisingly, this mutant inhibits constriction, suggesting that centrally localized apical ROCK/myosin activity promotes contraction. We determined actin cytoskeletal polarity by developing a barbed end incorporation assay for Drosophila embryos, which revealed barbed end enrichment at junctions. Our results demonstrate that epithelial cells contract with a spatially organized apical actomyosin cortex, involving a polarized actin cytoskeleton and centrally positioned myosin, with cell-scale order that resembles a muscle sarcomere.
[Mh] Termos MeSH primário: Actomiosina/metabolismo
Polaridade Celular
Células Epiteliais/citologia
Contração Muscular
Músculos/citologia
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Actinas/metabolismo
Animais
Forma Celular
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/embriologia
Células Epiteliais/metabolismo
Modelos Biológicos
Morfogênese
Miosina Tipo II/metabolismo
Sarcômeros/metabolismo
Quinases Associadas a rho/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Drosophila Proteins); 9013-26-7 (Actomyosin); EC 2.7.11.1 (rho-Associated Kinases); EC 3.6.1.- (Myosin Type II)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171207
[Lr] Data última revisão:
171207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  3 / 1290 MEDLINE  
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[PMID]:28898058
[Au] Autor:Liu R; Hossain MM; Chen X; Jin JP
[Ad] Endereço:Department of Physiology, Wayne State University School of Medicine , Detroit, Michigan 48201, United States.
[Ti] Título:Mechanoregulation of SM22α/Transgelin.
[So] Source:Biochemistry;56(41):5526-5538, 2017 Oct 17.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SM22α, also named transgelin, is an actin filament-associated protein in smooth muscle and fibroblasts. Three decades after its discovery, the biological function of SM22α remains under investigation. Here we report a novel finding that the expression and degradation of SM22α/transgelin are regulated by mechanical tension. Following a mass spectrometry identification of SM22α degradation in isolated and tension-unloaded mouse aorta, we developed specific monoclonal antibodies to study the regulation of SM22α in human fetal lung myofibroblast line MRC-5 and primary cultures of neonatal mouse skin fibroblasts. The level of SM22α is positively related to the mechanical tension in the cytoskeleton produced by the myosin II motor in response to the stiffness of the culture matrix. Quantitative reverse transcription polymerase chain reaction demonstrated that the expression of SM22α is regulated at the transcriptional level. This mechanical regulation resembles that of calponin 2, another actin filament-associated protein. Immunofluorescent staining co-localized SM22α with F-actin, myosin, and calponin 2 in mouse skin fibroblasts. The close phylogenetic relationship between SM22α and the calponin family supports that SM22α is a calponin-like regulatory protein. The level of SM22α is decreased in skin fibroblasts isolated from calponin 2 knockout mice, suggesting interrelated regulation and function of the two proteins. On the other hand, SM22α expression was maximized at a matrix stiffness higher than that for calponin 2 in the same cell type, indicating differentiated regulation and tension responsiveness. The novel mechanoregulation of SM22α/transgelin lays the groundwork for understanding its cellular functions.
[Mh] Termos MeSH primário: Citoesqueleto/metabolismo
Matriz Extracelular/metabolismo
Regulação da Expressão Gênica
Queratinócitos/metabolismo
Proteínas dos Microfilamentos/metabolismo
Proteínas Musculares/metabolismo
Miofibroblastos/metabolismo
[Mh] Termos MeSH secundário: Animais
Biomarcadores/metabolismo
Calpaína/metabolismo
Linhagem Celular
Células Cultivadas
Citoesqueleto/química
Citoesqueleto/efeitos dos fármacos
Inibidores Enzimáticos/farmacologia
Matriz Extracelular/química
Matriz Extracelular/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Compostos Heterocíclicos de 4 ou mais Anéis/farmacologia
Seres Humanos
Queratinócitos/citologia
Queratinócitos/efeitos dos fármacos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Camundongos Transgênicos
Proteínas dos Microfilamentos/genética
Proteínas Musculares/genética
Miofibroblastos/citologia
Miofibroblastos/efeitos dos fármacos
Miosina Tipo II/antagonistas & inibidores
Miosina Tipo II/metabolismo
Especificidade de Órgãos
Maleabilidade
Transporte Proteico/efeitos dos fármacos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Enzyme Inhibitors); 0 (Heterocyclic Compounds, 4 or More Rings); 0 (Microfilament Proteins); 0 (Muscle Proteins); 0 (calponin protein, mouse); 0 (transgelin); 20WC4J7CQ6 (blebbistatin); EC 3.4.22.- (Calpain); EC 3.4.22.- (m-calpain); EC 3.6.1.- (Myosin Type II)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00794


  4 / 1290 MEDLINE  
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[PMID]:28887414
[Au] Autor:Halaoui R; Rejon C; Chatterjee SJ; Szymborski J; Meterissian S; Muller WJ; Omeroglu A; McCaffrey L
[Ad] Endereço:Rosalind and Morris Goodman Cancer Research Centre, McGill University, Montreal, Quebec H3A 1A3, Canada.
[Ti] Título:Progressive polarity loss and luminal collapse disrupt tissue organization in carcinoma.
[So] Source:Genes Dev;31(15):1573-1587, 2017 Aug 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epithelial cancers (carcinoma) account for 80%-90% of all cancers. The development of carcinoma is associated with disrupted epithelial organization and solid ductal structures. The mechanisms underlying the morphological development of carcinoma are poorly understood, but it is thought that loss of cell polarity is an early event. Here we report the characterization of the development of human breast lesions leading to carcinoma. We identified a unique mechanism that generates solid ducts in carcinoma through progressive loss of polarity and collapse of the luminal architecture. This program initiates with asymmetric divisions of polarized cells that generate a stratified epithelium containing both polarized and depolarized cells. Stratified regions form cords that penetrate into the lumen, subdividing it into polarized secondary lumina. The secondary lumina then collapse with a concomitant decrease in RhoA and myosin II activity at the apical membrane and ultimately lose apical-basal polarity. By restoring RhoA activity in mice, ducts maintained lumen and cell polarity. Notably, disrupted tissue architecture through luminal collapse was reversible, and ducts with a lumen were re-established after oncogene suppression in vivo. This reveals a novel and common mechanism that contributes to carcinoma development by progressively disrupting cell and tissue organization.
[Mh] Termos MeSH primário: Neoplasias da Mama/patologia
Carcinogênese
Carcinoma/patologia
Polaridade Celular/fisiologia
[Mh] Termos MeSH secundário: Animais
Membrana Celular
Células Cultivadas
Feminino
Imunofluorescência
Seres Humanos
Camundongos
Microscopia Confocal
Miosina Tipo II/metabolismo
Cultura Primária de Células
Proteína rhoA de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.- (Myosin Type II); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170910
[St] Status:MEDLINE
[do] DOI:10.1101/gad.300566.117


  5 / 1290 MEDLINE  
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[PMID]:28870992
[Au] Autor:Driver EC; Northrop A; Kelley MW
[Ad] Endereço:Laboratory of Cochlear Development, National Institute on Deafness and Other Communication Disorders, NIH, Bethesda, MD 20892, USA drivere@nidcd.nih.gov.
[Ti] Título:Cell migration, intercalation and growth regulate mammalian cochlear extension.
[So] Source:Development;144(20):3766-3776, 2017 10 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Developmental remodeling of the sensory epithelium of the cochlea is required for the formation of an elongated, tonotopically organized auditory organ, but the cellular processes that mediate these events are largely unknown. We used both morphological assessments of cellular rearrangements and time-lapse imaging to visualize cochlear remodeling in mouse. Analysis of cell redistribution showed that the cochlea extends through a combination of radial intercalation and cell growth. Live imaging demonstrated that concomitant cellular intercalation results in a brief period of epithelial convergence, although subsequent changes in cell size lead to medial-lateral spreading. Supporting cells, which retain contact with the basement membrane, exhibit biased protrusive activity and directed movement along the axis of extension. By contrast, hair cells lose contact with the basement membrane, but contribute to continued outgrowth through increased cell size. Regulation of cellular protrusions, movement and intercalation within the cochlea all require myosin II. These results establish, for the first time, many of the cellular processes that drive the distribution of sensory cells along the tonotopic axis of the cochlea.
[Mh] Termos MeSH primário: Movimento Celular
Cóclea/embriologia
Regulação da Expressão Gênica no Desenvolvimento
[Mh] Termos MeSH secundário: Animais
Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Padronização Corporal
Proliferação Celular
Tamanho Celular
Feminino
Genótipo
Células Ciliadas Auditivas/citologia
Homozigoto
Mamíferos
Camundongos
Miosina Tipo II/metabolismo
Órgão Espiral/embriologia
Fatores de Transcrição SOXB1/genética
Imagem com Lapso de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Atoh1 protein, mouse); 0 (Basic Helix-Loop-Helix Transcription Factors); 0 (SOXB1 Transcription Factors); 0 (Sox2 protein, mouse); EC 3.6.1.- (Myosin Type II)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE
[do] DOI:10.1242/dev.151761


  6 / 1290 MEDLINE  
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[PMID]:28829941
[Au] Autor:Discher DE; Dooling LJ
[Ad] Endereço:Biophysical Engineering Labs, University of Pennsylvania, Philadelphia, PA 19104, USA. Electronic address: discher@seas.upenn.edu.
[Ti] Título:Optimal Contractile Forces for a Mesenchymal Engine.
[So] Source:Dev Cell;42(4):313-315, 2017 08 21.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cell and molecular mechanisms that cause a smooth epithelium to become topographically patterned during development are poorly understood. In a recent issue of Science, Shyer et al. (2017) show that myosin II contractility drives the smooth dermal mesenchyme into a pattern of surface bumps that triggers epithelial gene expression.
[Mh] Termos MeSH primário: Epitélio
Mesoderma
[Mh] Termos MeSH secundário: Contração Muscular
Miosina Tipo II
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
EC 3.6.1.- (Myosin Type II)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE


  7 / 1290 MEDLINE  
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[PMID]:28825699
[Au] Autor:Zihni C; Vlassaks E; Terry S; Carlton J; Leung TKC; Olson M; Pichaud F; Balda MS; Matter K
[Ad] Endereço:Institute of Ophthalmology, University College London, Bath Street, London EC1V 9EL, UK.
[Ti] Título:An apical MRCK-driven morphogenetic pathway controls epithelial polarity.
[So] Source:Nat Cell Biol;19(9):1049-1060, 2017 Sep.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Polarized epithelia develop distinct cell surface domains, with the apical membrane acquiring characteristic morphological features such as microvilli. Cell polarization is driven by polarity determinants including the evolutionarily conserved partitioning-defective (PAR) proteins that are separated into distinct cortical domains. PAR protein segregation is thought to be a consequence of asymmetric actomyosin contractions. The mechanism of activation of apically polarized actomyosin contractility is unknown. Here we show that the Cdc42 effector MRCK activates myosin-II at the apical pole to segregate aPKC-Par6 from junctional Par3, defining the apical domain. Apically polarized MRCK-activated actomyosin contractility is reinforced by cooperation with aPKC-Par6 downregulating antagonistic RhoA-driven junctional actomyosin contractility, and drives polarization of cytosolic brush border determinants and apical morphogenesis. MRCK-activated polarized actomyosin contractility is required for apical differentiation and morphogenesis in vertebrate epithelia and Drosophila photoreceptors. Our results identify an apical origin of actomyosin-driven morphogenesis that couples cytoskeletal reorganization to PAR polarity signalling.
[Mh] Termos MeSH primário: Membrana Celular/enzimologia
Polaridade Celular
Células Epiteliais/enzimologia
Miotonina Proteína Quinase/metabolismo
[Mh] Termos MeSH secundário: Actomiosina/metabolismo
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Animais
Animais Geneticamente Modificados
Células CACO-2
Proteínas de Ciclo Celular/metabolismo
Diferenciação Celular
Cães
Proteínas de Drosophila/genética
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/enzimologia
Genótipo
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Seres Humanos
Células Madin Darby de Rim Canino
Proteínas de Membrana/metabolismo
Morfogênese
Miosina Tipo II/metabolismo
Miotonina Proteína Quinase/genética
Fenótipo
Células Fotorreceptoras de Invertebrados/enzimologia
Proteína Quinase C/metabolismo
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Interferência de RNA
Transdução de Sinais
Fatores de Tempo
Transfecção
Proteína cdc42 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Cell Cycle Proteins); 0 (Drosophila Proteins); 0 (Guanine Nucleotide Exchange Factors); 0 (Membrane Proteins); 0 (PARD3 protein, human); 0 (PARD6A protein, human); 9013-26-7 (Actomyosin); EC 2.7.11.1 (Gek protein, Drosophila); EC 2.7.11.1 (Myotonin-Protein Kinase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.13 (PKC-3 protein); EC 2.7.11.13 (Protein Kinase C); EC 3.6.1.- (Myosin Type II); EC 3.6.5.2 (cdc42 GTP-Binding Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170822
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3592


  8 / 1290 MEDLINE  
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[PMID]:28811312
[Au] Autor:Ochoa-Espinosa A; Harmansa S; Caussinus E; Affolter M
[Ad] Endereço:Biozentrum, University of Basel, Klingelbergstr. 50/70, 4056 Basel, Switzerland amanda.ochoa@unibas.ch markus.affolter@unibas.ch.
[Ti] Título:Myosin II is not required for tracheal branch elongation and cell intercalation.
[So] Source:Development;144(16):2961-2968, 2017 08 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The tracheal system consists of an interconnected network of monolayered epithelial tubes that ensures oxygen transport in the larval and adult body. During tracheal dorsal branch (DB) development, individual DBs elongate as a cluster of cells, led by tip cells at the front and trailing cells in the rear. Branch elongation is accompanied by extensive cell intercalation and cell lengthening of the trailing stalk cells. Although cell intercalation is governed by Myosin II (MyoII)-dependent forces during tissue elongation in the embryo that lead to germ-band extension, it remained unclear whether MyoII plays a similar active role during tracheal branch elongation and intercalation. Here, we have used a nanobody-based approach to selectively knock down MyoII in tracheal cells. Our data show that, despite the depletion of MyoII function, tip cell migration and stalk cell intercalation (SCI) proceed at a normal rate. This confirms a model in which DB elongation and SCI in the trachea occur as a consequence of tip cell migration, which produces the necessary forces for the branching process.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Miosina Tipo II/metabolismo
Traqueia/embriologia
Traqueia/metabolismo
[Mh] Termos MeSH secundário: Animais
Proliferação Celular/genética
Proliferação Celular/fisiologia
Drosophila
Proteínas de Drosophila/genética
Embrião não Mamífero/metabolismo
Feminino
Masculino
Morfogênese/genética
Morfogênese/fisiologia
Miosina Tipo II/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); EC 3.6.1.- (Myosin Type II)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1242/dev.148940


  9 / 1290 MEDLINE  
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[PMID]:28687667
[Au] Autor:Pontes B; Monzo P; Gole L; Le Roux AL; Kosmalska AJ; Tam ZY; Luo W; Kan S; Viasnoff V; Roca-Cusachs P; Tucker-Kellogg L; Gauthier NC
[Ad] Endereço:Mechanobiology Institute, National University of Singapore, Singapore.
[Ti] Título:Membrane tension controls adhesion positioning at the leading edge of cells.
[So] Source:J Cell Biol;216(9):2959-2977, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cell migration is dependent on adhesion dynamics and actin cytoskeleton remodeling at the leading edge. These events may be physically constrained by the plasma membrane. Here, we show that the mechanical signal produced by an increase in plasma membrane tension triggers the positioning of new rows of adhesions at the leading edge. During protrusion, as membrane tension increases, velocity slows, and the lamellipodium buckles upward in a myosin II-independent manner. The buckling occurs between the front of the lamellipodium, where nascent adhesions are positioned in rows, and the base of the lamellipodium, where a vinculin-dependent clutch couples actin to previously positioned adhesions. As membrane tension decreases, protrusion resumes and buckling disappears, until the next cycle. We propose that the mechanical signal of membrane tension exerts upstream control in mechanotransduction by periodically compressing and relaxing the lamellipodium, leading to the positioning of adhesions at the leading edge of cells.
[Mh] Termos MeSH primário: Adesão Celular
Membrana Celular/fisiologia
Movimento Celular
Citoesqueleto/fisiologia
Fibroblastos/fisiologia
Mecanotransdução Celular
Pseudópodes/fisiologia
[Mh] Termos MeSH secundário: Actinas/genética
Actinas/metabolismo
Animais
Moléculas de Adesão Celular/genética
Moléculas de Adesão Celular/metabolismo
Membrana Celular/metabolismo
Forma Celular
Células Cultivadas
Simulação por Computador
Citoesqueleto/metabolismo
Fibroblastos/metabolismo
Camundongos
Proteínas dos Microfilamentos/genética
Proteínas dos Microfilamentos/metabolismo
Microscopia de Fluorescência
Microscopia de Vídeo
Modelos Biológicos
Miosina Tipo II/metabolismo
Fosfoproteínas/genética
Fosfoproteínas/metabolismo
Pseudópodes/metabolismo
Estresse Mecânico
Fatores de Tempo
Transfecção
Vinculina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Actins); 0 (Cell Adhesion Molecules); 0 (Microfilament Proteins); 0 (Phosphoproteins); 0 (vasodilator-stimulated phosphoprotein); 125361-02-6 (Vinculin); EC 3.6.1.- (Myosin Type II)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170709
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201611117


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[PMID]:28648599
[Au] Autor:Komatsu H; Koseki Y; Kanno T; Aoki S; Kodama T
[Ad] Endereço:Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Kawazu 680-4, Iizuka 820-8502, Japan. Electronic address: komatsu@bio.kyutech.ac.jp.
[Ti] Título:2,3-Butandione 2-monoxime inhibits skeletal myosin II by accelerating ATP cleavage.
[So] Source:Biochem Biophys Res Commun;490(3):849-854, 2017 Aug 26.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:2,3-Butandione 2-monoxime (BDM) is a widely used myosin inhibitor with an unclear mode of action. In this report, we investigated the mechanism of BDM oxime group nucleophilic reactivity on the phosphoester bond of ATP. BDM increased the ATPase activity of skeletal myosin subfragment 1 (S1) under conditions in which ATP cleavage is the rate-limiting step (K , EDTA-ATPase activity of native S1 and Mg -ATPase activity of trinitrophenylated S1 and partially unfolded S1). Furthermore, the effect of BDM on the S1-bound adenosine 5'-(ß,γ-imido) triphosphate (AMPPNP) P NMR spectrum suggests that BDM changes the microenvironment around the phosphorus atoms of myosin-bound nucleotide. A computational search for the BDM-binding site in the adenosine 5'-[γ-thio] triphosphate (myosin-ATPγS) complex predicted that BDM is located adjacent to the nucleotide on myosin. Therefore, we propose that the BDM oxime group catalytically assists in ATP cleavage, thereby enhancing the ATPase activity of myosin in a manner analogous to pralidoxime-mediated reactivation of organophosphate-inactivated acetylcholinesterase. This is the first study suggesting that oxime provides catalytic assistance for ATP cleavage by an ATP-hydrolyzing enzyme.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Miosina Tipo II/antagonistas & inibidores
Miosina Tipo II/metabolismo
Oximas/química
Oximas/farmacologia
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/metabolismo
Animais
ATPase de Ca(2+) e Mg(2+)/metabolismo
Simulação de Acoplamento Molecular
Subfragmentos de Miosina/metabolismo
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Myosin Subfragments); 0 (Oximes); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (Ca(2+) Mg(2+)-ATPase); EC 3.6.1.- (EDTA-ATPase); EC 3.6.1.- (Myosin Type II)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE



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