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Pesquisa : D08.811.277.040.013.500.250 [Categoria DeCS]
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[PMID]:28783150
[Au] Autor:Zehr E; Szyk A; Piszczek G; Szczesna E; Zuo X; Roll-Mecak A
[Ad] Endereço:Cell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland, USA.
[Ti] Título:Katanin spiral and ring structures shed light on power stroke for microtubule severing.
[So] Source:Nat Struct Mol Biol;24(9):717-725, 2017 Sep.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/química
Adenosina Trifosfatases/ultraestrutura
Caenorhabditis elegans/enzimologia
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Microscopia Crioeletrônica
Cristalografia por Raios X
Katanina
Modelos Moleculares
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170808
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3448


  2 / 155 MEDLINE  
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[PMID]:28644898
[Au] Autor:Ren H; Dang X; Cai X; Yu P; Li Y; Zhang S; Liu M; Chen B; Lin D
[Ad] Endereço:Basic Forestry and Proteomics Research Center, Fujian Provincial Key Laboratory of Haixia Applied Plant Systems Biology, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou, China.
[Ti] Título:Spatio-temporal orientation of microtubules controls conical cell shape in Arabidopsis thaliana petals.
[So] Source:PLoS Genet;13(6):e1006851, 2017 Jun.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The physiological functions of epidermal cells are largely determined by their diverse morphologies. Most flowering plants have special conical-shaped petal epidermal cells that are thought to influence light capture and reflectance, and provide pollinator grips, but the molecular mechanisms controlling conical cell shape remain largely unknown. Here, we developed a live-confocal imaging approach to quantify geometric parameters of conical cells in Arabidopsis thaliana (A. thaliana). Through genetic screens, we identified katanin (KTN1) mutants showing a phenotype of decreased tip sharpening of conical cells. Furthermore, we demonstrated that SPIKE1 and Rho of Plants (ROP) GTPases were required for the final shape formation of conical cells, as KTN1 does. Live-cell imaging showed that wild-type cells exhibited random orientation of cortical microtubule arrays at early developmental stages but displayed a well-ordered circumferential orientation of microtubule arrays at later stages. By contrast, loss of KTN1 prevented random microtubule networks from shifting into well-ordered arrays. We further showed that the filamentous actin cap, which is a typical feature of several plant epidermal cell types including root hairs and leaf trichomes, was not observed in the growth apexes of conical cells during cell development. Moreover, our genetic and pharmacological data suggested that microtubules but not actin are required for conical cell shaping. Together, our results provide a novel imaging approach for studying petal conical cell morphogenesis and suggest that the spatio-temporal organization of microtubule arrays plays crucial roles in controlling conical cell shape.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Proteínas de Arabidopsis/genética
Forma Celular/genética
Flores/genética
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/genética
Arabidopsis/genética
Arabidopsis/crescimento & desenvolvimento
Epiderme/citologia
Epiderme/crescimento & desenvolvimento
Flores/crescimento & desenvolvimento
Flores/ultraestrutura
Proteínas de Ligação ao GTP/genética
Katanina
Microtúbulos/genética
Microtúbulos/ultraestrutura
Proteínas Mutantes/genética
Folhas de Planta/citologia
Folhas de Planta/genética
Tricomas/genética
Tricomas/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Mutant Proteins); 0 (SPIKE1 protein, Arabidopsis); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (GTP-Binding Proteins); EC 3.6.1.- (ROP1 protein, Arabidopsis); EC 3.6.4.3 (KTN1 protein, Arabidopsis); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006851


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[PMID]:28436967
[Au] Autor:Jiang K; Rezabkova L; Hua S; Liu Q; Capitani G; Altelaar AFM; Heck AJR; Kammerer RA; Steinmetz MO; Akhmanova A
[Ad] Endereço:Cell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
[Ti] Título:Microtubule minus-end regulation at spindle poles by an ASPM-katanin complex.
[So] Source:Nat Cell Biol;19(5):480-492, 2017 05.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:ASPM (known as Asp in fly and ASPM-1 in worm) is a microcephaly-associated protein family that regulates spindle architecture, but the underlying mechanism is poorly understood. Here, we show that ASPM forms a complex with another protein linked to microcephaly, the microtubule-severing ATPase katanin. ASPM and katanin localize to spindle poles in a mutually dependent manner and regulate spindle flux. X-ray crystallography revealed that the heterodimer formed by the N- and C-terminal domains of the katanin subunits p60 and p80, respectively, binds conserved motifs in ASPM. Reconstitution experiments demonstrated that ASPM autonomously tracks growing microtubule minus ends and inhibits their growth, while katanin decorates and bends both ends of dynamic microtubules and potentiates the minus-end blocking activity of ASPM. ASPM also binds along microtubules, recruits katanin and promotes katanin-mediated severing of dynamic microtubules. We propose that the ASPM-katanin complex controls microtubule disassembly at spindle poles and that misregulation of this process can lead to microcephaly.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Microcefalia/metabolismo
Microtúbulos/enzimologia
Proteínas do Tecido Nervoso/metabolismo
Polos do Fuso/enzimologia
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/química
Adenosina Trifosfatases/genética
Sistemas CRISPR-Cas
Células HEK293
Células HeLa
Seres Humanos
Katanina
Microcefalia/genética
Microcefalia/patologia
Microtúbulos/genética
Microtúbulos/patologia
Modelos Moleculares
Mutação
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Ligação Proteica
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Transdução de Sinais
Polos do Fuso/genética
Polos do Fuso/patologia
Relação Estrutura-Atividade
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (ASPM protein, human); 0 (Nerve Tissue Proteins); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (katanin p80, human); EC 3.6.4.3 (KATNA1 protein, human); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170425
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3511


  4 / 155 MEDLINE  
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[PMID]:28093975
[Au] Autor:Sarma K; Roychoudhury S; Bora SS; Dehury B; Parida P; Das S; Das R; Dohutia C; Nath S; Deb B; Modi MK
[Ad] Endereço:Department of Life Science and Bioinformatics, Assam University, Silchar 788011, Assam. India.
[Ti] Título:Molecular Modeling and Dynamics Simulation Analysis of KATNAL1 for Identification of Novel Inhibitor of Sperm Maturation.
[So] Source:Comb Chem High Throughput Screen;20(1):82-92, 2017.
[Is] ISSN:1875-5402
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hormone based birth control often causes various side effects. A recent study revealed that temporary infertility without changing hormone levels can be attained by inhibiting Katanin p60 ATPase-containing subunit A-like 1 protein (KATNAL1) which is critical for sperm maturation in the testes. OBJECTIVE: This study aimed at attaining the most energetically stable three dimensional (3D) structure of KATNAL1 protein using comparative modeling followed by screening of a ligand library of known natural spermicidal compounds for their binding affinity with KATNAL1. This in turn may inhibit the development of mature sperm in the seminiferous epithelium. METHOD: A series of computational techniques were used for building the 3D structure of KATNAL1 which was further optimized by molecular dynamics (MD) simulation. For revealing the ATP binding mode of KATNAL1, docking study was carried out using the optimized model obtained from the MD simulation. The docking study was also employed to test the binding efficiency of the ligand library. RESULTS: Molecular docking study confirmed the ATP binding of KATNAL1 with various hydrophobic and hydrogen bond interactions. Binding efficiency of the ligand library suggested that calotropin, a cardenolide of Calotropis procera showed the highest binding efficiency against the target protein without toxicity. MD simulation of the docked complex validated the results of the docking study. CONCLUSION: This study revealed the ATP binding mode of KATNAL1 and identified calotropin as a potential lead molecule against it showing high binding efficiency with good bioavailability and no mutagenicity. Further in vitro and in vivo bioassay of calotropin could facilitate the development of novel non-hormonal male-specific contraceptive in near future.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/antagonistas & inibidores
Adenosina Trifosfatases/metabolismo
Anticoncepcionais Masculinos/farmacologia
Descoberta de Drogas
Maturação do Esperma/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/química
Trifosfato de Adenosina/metabolismo
Sítios de Ligação
Cardenolídeos/farmacologia
Seres Humanos
Katanina
Ligantes
Masculino
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
Ligação Proteica
Relação Quantitativa Estrutura-Atividade
Bibliotecas de Moléculas Pequenas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cardenolides); 0 (Contraceptive Agents, Male); 0 (Ligands); 0 (Small Molecule Libraries); 0 (calotropin); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (KATNAL1 protein, human); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170118
[St] Status:MEDLINE
[do] DOI:10.2174/1386207320666170116120104


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[PMID]:27726198
[Au] Autor:Waclawek E; Joachimiak E; Hall MH; Fabczak H; Wloga D
[Ad] Endereço:Laboratory of Cytoskeleton and Cilia Biology, Department of Cell Biology, Nencki Institute of Experimental Biology of Polish Academy of Sciences, 3 Pasteur Str, Warsaw, 02-093, Poland.
[Ti] Título:Regulation of katanin activity in the ciliate Tetrahymena thermophila.
[So] Source:Mol Microbiol;103(1):134-150, 2017 01.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Katanin is a microtubule severing protein that functions as a heterodimer composed of an AAA domain catalytic subunit, p60, and a regulatory subunit, a WD40 repeat protein, p80. Katanin-dependent severing of microtubules is important for proper execution of key cellular activities including cell division, migration, and differentiation. Published data obtained in Caenorhabditis elegans, Xenopus and mammals indicate that katanin is regulated at multiple levels including transcription, posttranslational modifications (of both katanin and microtubules) and degradation. Little is known about how katanin is regulated in unicellular organisms. Here we show that in the ciliated protist Tetrahymena thermophila, as in Metazoa, the localization and activity of katanin requires specific domains of both p60 and p80, and that the localization of p60, but not p80, is sensitive to the levels of microtubule glutamylation. A prolonged overexpression of either a full length, or a fragment of p80 containing WD40 repeats, partly phenocopies a knockout of p60, indicating that in addition to its activating role, p80 could also contribute to the inhibition of p60. We also show that the level of p80 depends on the 26S proteasome activity.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Microtúbulos/metabolismo
Tetrahymena thermophila/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Sequência de Aminoácidos
Hidrólise
Transporte de Íons
Katanina
Domínios Proteicos
Tetrahymena thermophila/genética
Tubulina (Proteína)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Tubulin); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161012
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13547


  6 / 155 MEDLINE  
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[PMID]:27578779
[Au] Autor:Joly N; Martino L; Gigant E; Dumont J; Pintard L
[Ad] Endereço:Institut Jacques Monod, Cell Cycle and Development Team, Centre National de la Recherche Scientifique and University of Paris Diderot and Sorbonne Paris Cité UMR7592, Paris 75013, France nicolas.joly@ijm.fr lionel.pintard@ijm.fr.
[Ti] Título:Microtubule-severing activity of the AAA+ ATPase Katanin is essential for female meiotic spindle assembly.
[So] Source:Development;143(19):3604-3614, 2016 10 01.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In most animals, female meiotic spindles are assembled in the absence of centrosomes. How microtubules (MTs) are organized into acentrosomal meiotic spindles is poorly understood. In Caenorhabditis elegans, assembly of female meiotic spindles requires MEI-1 and MEI-2, which constitute the microtubule-severing AAA+ ATPase Katanin. However, the role of MEI-2 is not known and whether MT severing is required for meiotic spindle assembly is unclear. Here, we show that the essential role of MEI-2 is to confer MT binding to Katanin, which in turn stimulates the ATPase activity of MEI-1, leading to MT severing. To test directly the contribution of MT severing to meiotic spindle assembly, we engineered Katanin variants that retained MT binding and MT bundling activities but that were inactive for MT severing. In vivo analysis of these variants showed disorganized microtubules that lacked focused spindle poles reminiscent of the Katanin loss-of-function phenotype, demonstrating that the MT-severing activity is essential for meiotic spindle assembly in C. elegans Overall, our results reveal the essential role of MEI-2 and provide the first direct evidence supporting an essential role of MT severing in meiotic spindle assembly in C. elegans.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Microtúbulos/metabolismo
Fuso Acromático/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Animais
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Feminino
Katanina
Meiose/genética
Meiose/fisiologia
Microtúbulos/genética
Fuso Acromático/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (MEI-1 protein, C elegans); EC 3.6.1.- (MEI-2 protein, C elegans); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160901
[St] Status:MEDLINE


  7 / 155 MEDLINE  
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[PMID]:27536893
[Au] Autor:Kuo TC; Li LW; Pan SH; Fang JM; Liu JH; Cheng TJ; Wang CJ; Hung PF; Chen HY; Hong TM; Hsu YL; Wong CH; Yang PC
[Ad] Endereço:Ph.D. Program in Translational Medicine, National Taiwan University and Academia Sinica , Taipei, Taiwan.
[Ti] Título:Purine-Type Compounds Induce Microtubule Fragmentation and Lung Cancer Cell Death through Interaction with Katanin.
[So] Source:J Med Chem;59(18):8521-34, 2016 Sep 22.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microtubule targeting agents (MTAs) constitute a class of drugs for cancer treatment. Despite many MTAs have been proven to significantly improve the treatment outcomes of various malignancies, resistance has usually occurred. By selection from a two million entry chemical library based on the efficacy and safety, we identified purine-type compounds that were active against lung small cell lung cancer (NSCLC). The purine compound 5a (GRC0321) was an MTA with good effects against NSCLC. Lung cancer cells H1975 treated with 5a could induce microtubule fragmentation, leading to G2/M cell cycle arrest and intrinsic apoptosis. Compound 5a directly targeted katanin and regulated the severing activity of katanin, which cut the cellular microtubules into short pieces and activated c-Jun N-terminal kinases (JNK). The microtubule fragmenting effect of 5a is a unique mechanism in MTAs. It might overcome the resistance problems that most of the MTAs have faced.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Antineoplásicos/farmacologia
Carcinoma Pulmonar de Células não Pequenas/tratamento farmacológico
Neoplasias Pulmonares/tratamento farmacológico
Microtúbulos/efeitos dos fármacos
Purinas/farmacologia
[Mh] Termos MeSH secundário: Antineoplásicos/química
Carcinoma Pulmonar de Células não Pequenas/metabolismo
Carcinoma Pulmonar de Células não Pequenas/patologia
Ciclo Celular/efeitos dos fármacos
Morte Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Seres Humanos
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Katanina
Neoplasias Pulmonares/metabolismo
Neoplasias Pulmonares/patologia
Microtúbulos/metabolismo
Microtúbulos/patologia
Purinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Purines); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160819
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.6b00797


  8 / 155 MEDLINE  
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[PMID]:27527792
[Au] Autor:Beard SM; Smit RB; Chan BG; Mains PE
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Alberta Children's Hospital Research Institute, University of Calgary, T2N 4N1, Canada.
[Ti] Título:Regulation of the MEI-1/MEI-2 Microtubule-Severing Katanin Complex in Early Caenorhabditis elegans Development.
[So] Source:G3 (Bethesda);6(10):3257-3268, 2016 Oct 13.
[Is] ISSN:2160-1836
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:After fertilization, rapid changes of the Caenorhabditis elegans cytoskeleton occur in the transition from meiosis to mitosis, requiring precise regulation. The MEI-1/MEI-2 katanin microtubule-severing complex is essential for meiotic spindle formation but must be quickly inactivated to allow for proper formation of the mitotic spindle. MEI-1/MEI-2 inactivation is dependent on multiple redundant pathways. The primary pathway employs the MEL-26 substrate adaptor for the CUL-3/cullin-based E3 ubiquitin ligase, which targets MEI-1 for proteosomal degradation. Here, we used quantitative antibody staining to measure MEI-1 levels to determine how other genes implicated in MEI-1 regulation act relative to CUL-3/MEL-26 The anaphase-promoting complex/cyclosome, APC/C, the DYRK (Dual-specificity tyrosine-regulated kinase), MBK-2, and the CUL-2-based E3 ubiquitin ligase act together to degrade MEI-1, in parallel to MEL-26/CUL-3 CUL-2 is known to keep MEL-26 low during meiosis, so CUL-2 apparently changes its target from MEL-26 in meiosis to MEI-1 in mitosis. RFL-1, an activator of cullin E3 ubiquitin ligases, activates CUL-2 but not CUL-3 for MEI-1 elimination. HECD-1 (HECT/Homologous to the E6AP carboxyl terminus domain) E3 ligase acts as a MEI-1 activator in meiosis but functions as an inhibitor during mitosis, without affecting levels of MEI-1 or MEI-2 Our results highlight the multiple layers of MEI-1 regulation that are required during the switch from the meiotic to mitotic modes of cell division.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/genética
Caenorhabditis elegans/metabolismo
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/embriologia
Ciclo Celular/genética
Epistasia Genética
Regulação da Expressão Gênica no Desenvolvimento
Genótipo
Katanina
Meiose/genética
Microtúbulos
Mitose/genética
Complexos Multiproteicos/metabolismo
Ligação Proteica
Interferência de RNA
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Multiprotein Complexes); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (MEI-1 protein, C elegans); EC 3.6.1.- (MEI-2 protein, C elegans); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160817
[St] Status:MEDLINE
[do] DOI:10.1534/g3.116.031666


  9 / 155 MEDLINE  
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[PMID]:27482848
[Au] Autor:Louveaux M; Rochette S; Beauzamy L; Boudaoud A; Hamant O
[Ad] Endereço:Laboratoire Reproduction et Développement des Plantes, Université de Lyon, ENS de Lyon, UCB Lyon 1, CNRS, INRA, F-69342, Lyon, France.
[Ti] Título:The impact of mechanical compression on cortical microtubules in Arabidopsis: a quantitative pipeline.
[So] Source:Plant J;88(2):328-342, 2016 Oct.
[Is] ISSN:1365-313X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Exogenous mechanical perturbations on living tissues are commonly used to investigate whether cell effectors can respond to mechanical cues. However, in most of these experiments, the applied mechanical stress and/or the biological response are described only qualitatively. We developed a quantitative pipeline based on microindentation and image analysis to investigate the impact of a controlled and prolonged compression on microtubule behaviour in the Arabidopsis shoot apical meristem, using microtubule fluorescent marker lines. We found that a compressive stress, in the order of magnitude of turgor pressure, induced apparent microtubule bundling. Importantly, that response could be reversed several hours after the release of compression. Next, we tested the contribution of microtubule severing to compression-induced bundling: microtubule bundling seemed less pronounced in the katanin mutant, in which microtubule severing is dramatically reduced. Conversely, some microtubule bundles could still be observed 16 h after the release of compression in the spiral2 mutant, in which severing rate is instead increased. To quantify the impact of mechanical stress on anisotropy and orientation of microtubule arrays, we used the nematic tensor based FibrilTool ImageJ/Fiji plugin. To assess the degree of apparent bundling of the network, we developed several methods, some of which were borrowed from geostatistics. The final microtubule bundling response could notably be related to tissue growth velocity that was recorded by the indenter during compression. Because both input and output are quantified, this pipeline is an initial step towards correlating more precisely the cytoskeleton response to mechanical stress in living tissues.
[Mh] Termos MeSH primário: Arabidopsis/metabolismo
Microtúbulos/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Arabidopsis/genética
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Katanina
Meristema/genética
Meristema/metabolismo
Microtúbulos/genética
Mutação
Estresse Mecânico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160803
[St] Status:MEDLINE
[do] DOI:10.1111/tpj.13290


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[PMID]:26929214
[Au] Autor:Cheung K; Senese S; Kuang J; Bui N; Ongpipattanakul C; Gholkar A; Cohn W; Capri J; Whitelegge JP; Torres JZ
[Ad] Endereço:From the ‡Department of Chemistry and Biochemistry, University of California, Los Angeles, California, 90095;
[Ti] Título:Proteomic Analysis of the Mammalian Katanin Family of Microtubule-severing Enzymes Defines Katanin p80 subunit B-like 1 (KATNBL1) as a Regulator of Mammalian Katanin Microtubule-severing.
[So] Source:Mol Cell Proteomics;15(5):1658-69, 2016 05.
[Is] ISSN:1535-9484
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Katanin family of microtubule-severing enzymes is critical for remodeling microtubule-based structures that influence cell division, motility, morphogenesis and signaling. Katanin is composed of a catalytic p60 subunit (A subunit, KATNA1) and a regulatory p80 subunit (B subunit, KATNB1). The mammalian genome also encodes two additional A-like subunits (KATNAL1 and KATNAL2) and one additional B-like subunit (KATNBL1) that have remained poorly characterized. To better understand the factors and mechanisms controlling mammalian microtubule-severing, we have taken a mass proteomic approach to define the protein interaction module for each mammalian Katanin subunit and to generate the mammalian Katanin family interaction network (Katan-ome). Further, we have analyzed the function of the KATNBL1 subunit and determined that it associates with KATNA1 and KATNAL1, it localizes to the spindle poles only during mitosis and it regulates Katanin A subunit microtubule-severing activity in vitro Interestingly, during interphase, KATNBL1 is sequestered in the nucleus through an N-terminal nuclear localization signal. Finally KATNB1 was able to compete the interaction of KATNBL1 with KATNA1 and KATNAL1. These data indicate that KATNBL1 functions as a regulator of Katanin A subunit microtubule-severing activity during mitosis and that it likely coordinates with KATNB1 to perform this function.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Microtúbulos/metabolismo
Proteômica/métodos
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/química
Núcleo Celular/metabolismo
Células HeLa
Seres Humanos
Katanina
Espectrometria de Massas
Meiose
Mapas de Interação de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (KATNBL1 protein, human); EC 3.6.1.- (katanin p80, human); EC 3.6.4.3 (KATNA1 protein, human); EC 3.6.4.3 (KATNAL1 protein, human); EC 3.6.4.3 (Katanin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171127
[Lr] Data última revisão:
171127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160302
[St] Status:MEDLINE
[do] DOI:10.1074/mcp.M115.056465



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