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Pesquisa : D08.811.277.040.025.193.500 [Categoria DeCS]
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  1 / 5240 MEDLINE  
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[PMID]:27770501
[Au] Autor:Neumann S; Chassefeyre R; Campbell GE; Encalada SE
[Ad] Endereço:Department of Molecular and Experimental Medicine, Department of Molecular and Cellular Neuroscience, Dorris Neuroscience Center, The Scripps Research Institute, La Jolla, California.
[Ti] Título:KymoAnalyzer: a software tool for the quantitative analysis of intracellular transport in neurons.
[So] Source:Traffic;18(1):71-88, 2017 01.
[Is] ISSN:1600-0854
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In axons, proper localization of proteins, vesicles, organelles, and other cargoes is accomplished by the highly regulated coordination of kinesins and dyneins, molecular motors that bind to cargoes and translocate them along microtubule (MT) tracks. Impairment of axonal transport is implicated in the pathogenesis of multiple neurodegenerative disorders including Alzheimer's and Huntington's diseases. To understand how MT-based cargo motility is regulated and to delineate its role in neurodegeneration, it is critical to analyze the detailed dynamics of moving cargoes inside axons. Here, we present KymoAnalyzer, a software tool that facilitates the robust analysis of axonal transport from time-lapse live-imaging sequences. KymoAnalyzer is an open-source software that automatically classifies particle trajectories and systematically calculates velocities, run lengths, pauses, and a wealth of other parameters that are characteristic of motor-based transport. We anticipate that laboratories will easily use this package to unveil previously uncovered intracellular transport details of individually-moving cargoes inside neurons.
[Mh] Termos MeSH primário: Neurônios/metabolismo
Neurônios/fisiologia
[Mh] Termos MeSH secundário: Animais
Transporte Axonal/fisiologia
Axônios/metabolismo
Axônios/fisiologia
Dineínas/metabolismo
Cinesina/metabolismo
Microtúbulos/metabolismo
Microtúbulos/fisiologia
Doenças Neurodegenerativas/metabolismo
Doenças Neurodegenerativas/fisiopatologia
Organelas/metabolismo
Organelas/fisiologia
Software
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.6.4.2 (Dyneins); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE
[do] DOI:10.1111/tra.12456


  2 / 5240 MEDLINE  
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[PMID]:29349444
[Au] Autor:Hayashi K; Hasegawa S; Sagawa T; Tasaki S; Niwa S
[Ad] Endereço:Department of Applied Physics, Graduate School of Engineering, Tohoku University, Sendai, Japan. kumiko@camp.apph.tohoku.ac.jp.
[Ti] Título:Non-invasive force measurement reveals the number of active kinesins on a synaptic vesicle precursor in axonal transport regulated by ARL-8.
[So] Source:Phys Chem Chem Phys;20(5):3403-3410, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Kinesin superfamily protein UNC-104, a member of the kinesin-3 family, transports synaptic vesicle precursors (SVPs). In this study, the number of active UNC-104 molecules hauling a single SVP in axons in the worm Caenorhabditis elegans was counted by applying a newly developed non-invasive force measurement technique. The distribution of the force acting on a SVP transported by UNC-104 was spread out over several clusters, implying the presence of several force-producing units (FPUs). We then compared the number of FPUs in the wild-type worms with that in arl-8 gene-deletion mutant worms. ARL-8 is a SVP-bound arf-like small guanosine triphosphatase, and is known to promote unlocking of the autoinhibition of the motor, which is critical for avoiding unnecessary consumption of adenosine triphosphate when the motor does not bind to a SVP. There were fewer FPUs in the arl-8 mutant worms. This finding indicates that a lack of ARL-8 decreased the number of active UNC-104 motors, which then led to a decrease in the number of motors responsible for SVP transport.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Cinesina/metabolismo
Vesículas Sinápticas/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Axonal
Axônios/metabolismo
Caenorhabditis elegans
Proteínas de Caenorhabditis elegans/química
Proteínas de Caenorhabditis elegans/genética
GTP Fosfo-Hidrolases/química
GTP Fosfo-Hidrolases/genética
Cinesina/química
Microscopia de Fluorescência
Mutagênese
Vesículas Sinápticas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); EC 3.6.1.- (Arl8 protein, C elegans); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp05890j


  3 / 5240 MEDLINE  
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[PMID]:28459979
[Au] Autor:Whitman MC; Engle EC
[Ad] Endereço:F.M. Kirby Neurobiology Center, Boston Children's Hospital, Boston, MA 02115, USA.
[Ti] Título:Ocular congenital cranial dysinnervation disorders (CCDDs): insights into axon growth and guidance.
[So] Source:Hum Mol Genet;26(R1):R37-R44, 2017 08 01.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Unraveling the genetics of the paralytic strabismus syndromes known as congenital cranial dysinnervation disorders (CCDDs) is both informing physicians and their patients and broadening our understanding of development of the ocular motor system. Genetic mutations underlying ocular CCDDs alter either motor neuron specification or motor nerve development, and highlight the importance of modulations of cell signaling, cytoskeletal transport, and microtubule dynamics for axon growth and guidance. Here we review recent advances in our understanding of two CCDDs, congenital fibrosis of the extraocular muscles (CFEOM) and Duane retraction syndrome (DRS), and discuss what they have taught us about mechanisms of axon guidance and selective vulnerability. CFEOM presents with congenital ptosis and restricted eye movements, and can be caused by heterozygous missense mutations in the kinesin motor protein KIF21A or in the ß-tubulin isotypes TUBB3 or TUBB2B. CFEOM-causing mutations in these genes alter protein function and result in axon growth and guidance defects. DRS presents with inability to abduct one or both eyes. It can be caused by decreased function of several transcription factors critical for abducens motor neuron identity, including MAFB, or by heterozygous missense mutations in CHN1, which encodes α2-chimaerin, a Rac-GAP GTPase that affects cytoskeletal dynamics. Examination of the orbital innervation in mice lacking Mafb has established that the stereotypical misinnervation of the lateral rectus by fibers of the oculomotor nerve in DRS is secondary to absence of the abducens nerve. Studies of a CHN1 mouse model have begun to elucidate mechanisms of selective vulnerability in the nervous system.
[Mh] Termos MeSH primário: Axônios/fisiologia
Síndrome da Retração Ocular/genética
Fibrose/genética
Oftalmoplegia/genética
[Mh] Termos MeSH secundário: Animais
Axônios/metabolismo
Anormalidades Congênitas
Síndrome da Retração Ocular/metabolismo
Síndrome da Retração Ocular/patologia
Oftalmopatias Hereditárias/genética
Fibrose/metabolismo
Fibrose/patologia
Seres Humanos
Cinesina/genética
Cinesina/metabolismo
Camundongos
Mutação
Mutação de Sentido Incorreto
Transtornos da Motilidade Ocular/genética
Músculos Oculomotores/anormalidades
Músculos Oculomotores/patologia
Oftalmoplegia/metabolismo
Oftalmoplegia/patologia
Crânio/fisiopatologia
Tubulina (Proteína)/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (KIF21A protein, human); 0 (TUBB3 protein, human); 0 (Tubulin); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx168


  4 / 5240 MEDLINE  
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[PMID]:28455557
[Au] Autor:Goldstein A; Siegler N; Goldman D; Judah H; Valk E; Kõivomägi M; Loog M; Gheber L
[Ad] Endereço:Department of Chemistry and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, PO Box 653, 84105, Beer-Sheva, Israel.
[Ti] Título:Three Cdk1 sites in the kinesin-5 Cin8 catalytic domain coordinate motor localization and activity during anaphase.
[So] Source:Cell Mol Life Sci;74(18):3395-3412, 2017 09.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The bipolar kinesin-5 motors perform essential functions in mitotic spindle dynamics. We previously demonstrated that phosphorylation of at least one of the Cdk1 sites in the catalytic domain of the Saccharomyces cerevisiae kinesin-5 Cin8 (S277, T285, S493) regulates its localization to the anaphase spindle. The contribution of these three sites to phospho-regulation of Cin8, as well as the timing of such contributions, remains unknown. Here, we examined the function and spindle localization of phospho-deficient (serine/threonine to alanine) and phospho-mimic (serine/threonine to aspartic acid) Cin8 mutants. In vitro, the three Cdk1 sites undergo phosphorylation by Clb2-Cdk1. In cells, phosphorylation of Cin8 affects two aspects of its localization to the anaphase spindle, translocation from the spindle-pole bodies (SPBs) region to spindle microtubules (MTs) and the midzone, and detachment from the mitotic spindle. We found that phosphorylation of S277 is essential for the translocation of Cin8 from SPBs to spindle MTs and the subsequent detachment from the spindle. Phosphorylation of T285 mainly affects the detachment of Cin8 from spindle MTs during anaphase, while phosphorylation at S493 affects both the translocation of Cin8 from SPBs to the spindle and detachment from the spindle. Only S493 phosphorylation affected the anaphase spindle elongation rate. We conclude that each phosphorylation site plays a unique role in regulating Cin8 functions and postulate a model in which the timing and extent of phosphorylation of the three sites orchestrates the anaphase function of Cin8.
[Mh] Termos MeSH primário: Proteína Quinase CDC2/metabolismo
Cinesina/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Anáfase/fisiologia
Domínio Catalítico
Ciclina B/metabolismo
Cinesina/química
Cinesina/genética
Microtúbulos/metabolismo
Mutagênese Sítio-Dirigida
Fosforilação
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Fuso Acromático/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CLB2 protein, S cerevisiae); 0 (Cyclin B); 0 (Saccharomyces cerevisiae Proteins); EC 2.7.11.22 (CDC2 Protein Kinase); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180131
[Lr] Data última revisão:
180131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-017-2523-z


  5 / 5240 MEDLINE  
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[PMID]:29261664
[Au] Autor:Zamponi E; Buratti F; Cataldi G; Caicedo HH; Song Y; Jungbauer LM; LaDu MJ; Bisbal M; Lorenzo A; Ma J; Helguera PR; Morfini GA; Brady ST; Pigino GF
[Ad] Endereço:Laboratorio de Neuropatología Experimental, Instituto de Investigación Médica Mercedes y Martín Ferreyra, INIMEC-CONICET-Universidad Nacional de Córdoba, Córdoba, Argentina.
[Ti] Título:Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2.
[So] Source:PLoS One;12(12):e0188340, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prion diseases include a number of progressive neuropathies involving conformational changes in cellular prion protein (PrPc) that may be fatal sporadic, familial or infectious. Pathological evidence indicated that neurons affected in prion diseases follow a dying-back pattern of degeneration. However, specific cellular processes affected by PrPc that explain such a pattern have not yet been identified. Results from cell biological and pharmacological experiments in isolated squid axoplasm and primary cultured neurons reveal inhibition of fast axonal transport (FAT) as a novel toxic effect elicited by PrPc. Pharmacological, biochemical and cell biological experiments further indicate this toxic effect involves casein kinase 2 (CK2) activation, providing a molecular basis for the toxic effect of PrPc on FAT. CK2 was found to phosphorylate and inhibit light chain subunits of the major motor protein conventional kinesin. Collectively, these findings suggest CK2 as a novel therapeutic target to prevent the gradual loss of neuronal connectivity that characterizes prion diseases.
[Mh] Termos MeSH primário: Transporte Axonal/fisiologia
Axônios/metabolismo
Caseína Quinase II/metabolismo
Proteínas Priônicas/fisiologia
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Hipocampo/citologia
Hipocampo/metabolismo
Cinesina/metabolismo
Camundongos
Mitocôndrias/metabolismo
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prion Proteins); EC 2.7.11.1 (Casein Kinase II); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188340


  6 / 5240 MEDLINE  
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[PMID]:29211997
[Au] Autor:Ruhnow F; Kloß L; Diez S
[Ad] Endereço:B CUBE - Center for Molecular Bioengineering, Technische Universität Dresden, Dresden, Germany.
[Ti] Título:Challenges in Estimating the Motility Parameters of Single Processive Motor Proteins.
[So] Source:Biophys J;113(11):2433-2443, 2017 Dec 05.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytoskeletal motor proteins are essential to the function of a wide range of intracellular mechano-systems. The biophysical characterization of their movement along their filamentous tracks is therefore of large importance. Toward this end, single-molecule, in vitro stepping-motility assays are commonly used to determine motor velocity and run length. However, comparing results from such experiments has proved difficult due to influences from variations in the experimental conditions and the data analysis methods. Here, we investigate the movement of fluorescently labeled, processive, dimeric motor proteins and propose a unified algorithm to correct the measurements for finite filament length as well as photobleaching. Particular emphasis is put on estimating the statistical errors associated with the proposed evaluation method, as knowledge of these values is crucial when comparing measurements from different experiments. Testing our approach with simulated and experimental data from GFP-labeled kinesin-1 motors stepping along immobilized microtubules, we show 1) that velocity distributions should be fitted by a t location-scale probability density function rather than by a normal distribution; 2) that the impossibility to measure events shorter than the image acquisition time needs to be taken into account; 3) that the interaction time and run length of the motors can be estimated independent of the filament length distribution; and 4) that the dimeric nature of the motors needs to be considered when correcting for photobleaching. Moreover, our analysis reveals that controlling the temperature during the experiments with a precision below 1 K is of importance. We believe our method will not only improve the evaluation of experimental data, but also allow for better statistical comparisons between different populations of motor proteins (e.g., with distinct mutations or linked to different cargos) and filaments (e.g., in distinct nucleotide states or with different posttranslational modifications). Therefore, we include a detailed workflow for image processing and analysis (including MATLAB code), serving as a tutorial for the estimation of motility parameters in stepping-motility assays.
[Mh] Termos MeSH primário: Cinesina/metabolismo
Movimento
[Mh] Termos MeSH secundário: Animais
Cinesina/química
Cinética
Modelos Moleculares
Fotodegradação
Conformação Proteica
Ratos
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


  7 / 5240 MEDLINE  
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[PMID]:29244835
[Au] Autor:Jun DY; Lee JY; Park HS; Lee YH; Kim YH
[Ad] Endereço:Laboratory of Immunobiology, School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University, Daegu, Korea.
[Ti] Título:Tumor suppressor protein p53-mediated repression of human mitotic centromere-associated kinesin gene expression is exerted via down-regulation of Sp1 level.
[So] Source:PLoS One;12(12):e0189698, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The repressive role of p53 on the human mitotic centromere-associated kinesin (MCAK) core promoter from ‒266 to +54, relative to the transcription start site, has been determined. The MCAK mRNA and protein levels were 2.1- and 3.0-fold higher, respectively, in HCT116 (p53‒/‒) than in HCT116 (p53+/+) cells. Enforced down-regulation of p53 levels either in HCT116 (p53+/+) cells by p53 RNAi treatment or in MCF-7 cells using shRNA for p53 (shp53) resulted in a remarkable increase in the MCAK protein level. Site-directed mutagenesis and ChIP analyses showed that p53-mediated repression of the MCAK core promoter activity was not directly exerted by p53-binding to putative p53-response elements (p53-RE1 at -173/-166 and p53-RE2 at -245/-238), but indirectly by attenuating Sp1 binding to GC-motifs (GC1 at -93/-84 and GC2 at -119/-110). Treatment of HEK-293 cells bearing the MCAK core promoter-reporter (pGL2-320-Luc) with mithramycin A, which down-regulates Sp1 gene expression, reduced the promoter activity as well as endogenous MCAK levels. Exposure of HCT116 (p53+/+) cells to nutlin-3a, a validated activator of p53, caused a simultaneous reduction in Sp1 and MCAK protein levels, but not in HCT116 (p53-/-) cells. In contrast to wild-type (wt)-p53, tumor-derived p53 mutants (p53V143A, p53R248W, and p53R273H) failed to repress the Sp1-dependent activation of the MCAK promoter and to down-regulate endogenous levels of Sp1 and MCAK proteins. Collectively, these findings demonstrate that p53 can repress MCAK promoter activity indirectly via down-regulation of Sp1 expression level, and suggest that MCAK elevation in human tumor cells might be due to p53 mutation.
[Mh] Termos MeSH primário: Cinesina/biossíntese
Fator de Transcrição Sp1/genética
Proteína Supressora de Tumor p53/genética
[Mh] Termos MeSH secundário: Centrômero/genética
Células HCT116
Seres Humanos
Cinesina/genética
Células MCF-7
Mitose/genética
Mutagênese Sítio-Dirigida
Regiões Promotoras Genéticas
Ligação Proteica
Fator de Transcrição Sp1/biossíntese
Proteína Supressora de Tumor p53/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (KIF2C protein, human); 0 (Sp1 Transcription Factor); 0 (TP53 protein, human); 0 (Tumor Suppressor Protein p53); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189698


  8 / 5240 MEDLINE  
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[PMID]:29053796
[Au] Autor:Nibbeling EAR; Duarri A; Verschuuren-Bemelmans CC; Fokkens MR; Karjalainen JM; Smeets CJLM; de Boer-Bergsma JJ; van der Vries G; Dooijes D; Bampi GB; van Diemen C; Brunt E; Ippel E; Kremer B; Vlak M; Adir N; Wijmenga C; van de Warrenburg BPC; Franke L; Sinke RJ; Verbeek DS
[Ad] Endereço:Department of Genetics, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands.
[Ti] Título:Exome sequencing and network analysis identifies shared mechanisms underlying spinocerebellar ataxia.
[So] Source:Brain;140(11):2860-2878, 2017 Nov 01.
[Is] ISSN:1460-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The autosomal dominant cerebellar ataxias, referred to as spinocerebellar ataxias in genetic nomenclature, are a rare group of progressive neurodegenerative disorders characterized by loss of balance and coordination. Despite the identification of numerous disease genes, a substantial number of cases still remain without a genetic diagnosis. Here, we report five novel spinocerebellar ataxia genes, FAT2, PLD3, KIF26B, EP300, and FAT1, identified through a combination of exome sequencing in genetically undiagnosed families and targeted resequencing of exome candidates in a cohort of singletons. We validated almost all genes genetically, assessed damaging effects of the gene variants in cell models and further consolidated a role for several of these genes in the aetiology of spinocerebellar ataxia through network analysis. Our work links spinocerebellar ataxia to alterations in synaptic transmission and transcription regulation, and identifies these as the main shared mechanisms underlying the genetically diverse spinocerebellar ataxia types.
[Mh] Termos MeSH primário: Redes Reguladoras de Genes/genética
Ataxias Espinocerebelares/genética
[Mh] Termos MeSH secundário: Animais
Células COS
Caderinas/genética
Cercopithecus aethiops
Proteína p300 Associada a E1A/genética
Exoma/genética
Feminino
Células HEK293
Seres Humanos
Cinesina/genética
Masculino
Linhagem
Fosfolipase D/genética
Plasmídeos
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Análise de Sequência de DNA
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadherins); 0 (FAT1 protein, human); 0 (FAT2 protein, human); EC 2.3.1.48 (E1A-Associated p300 Protein); EC 2.3.1.48 (EP300 protein, human); EC 3.1.4.4 (Phospholipase D); EC 3.1.4.4 (phospholipase D3, human); EC 3.6.1.- (KIF26B protein, human); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE
[do] DOI:10.1093/brain/awx251


  9 / 5240 MEDLINE  
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[PMID]:29033361
[Au] Autor:Wang Z; Zhang F; He J; Wu P; Tay LWR; Cai M; Nian W; Weng Y; Qin L; Chang JT; McIntire LB; Di Paolo G; Xu J; Peng J; Du G
[Ad] Endereço:Department of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, TX 77030, USA.
[Ti] Título:Binding of PLD2-Generated Phosphatidic Acid to KIF5B Promotes MT1-MMP Surface Trafficking and Lung Metastasis of Mouse Breast Cancer Cells.
[So] Source:Dev Cell;43(2):186-197.e7, 2017 Oct 23.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Little is known about the cellular events promoting metastasis. We show that knockout of phospholipase D (PLD2), which generates the signaling lipid phosphatidic acid (PA), inhibits lung metastases in the mammary tumor virus (MMTV)-Neu transgenic mouse breast cancer model. PLD2 promotes local invasion through the regulation of the plasma membrane targeting of MT1-MMP and its associated invadopodia. A liposome pull-down screen identifies KIF5B, the heavy chain of the motor protein kinesin-1, as a new PA-binding protein. In vitro assays reveal that PA specifically and directly binds to the C terminus of KIF5B. The binding between PLD2-generated PA and KIF5B is required for the vesicular association of KIF5B, surface localization of MT1-MMP, invadopodia, and invasion in cancer cells. Taken together, these results identify a role of PLD2-generated PA in the regulation of kinesin-1 motor functions and breast cancer metastasis and suggest PLD2 as a potential therapeutic target for metastatic breast cancer.
[Mh] Termos MeSH primário: Cinesina/metabolismo
Neoplasias Pulmonares/secundário
Neoplasias Mamárias Animais/patologia
Metaloproteinase 14 da Matriz/metabolismo
Ácidos Fosfatídicos/metabolismo
Fosfolipase D/fisiologia
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Movimento Celular/fisiologia
Feminino
Seres Humanos
Cinesina/genética
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/metabolismo
Células MCF-7
Neoplasias Mamárias Animais/genética
Neoplasias Mamárias Animais/metabolismo
Metaloproteinase 14 da Matriz/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Ligação Proteica
Transporte Proteico
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphatidic Acids); EC 3.1.4.- (phospholipase D2); EC 3.1.4.4 (Phospholipase D); EC 3.4.24.80 (Matrix Metalloproteinase 14); EC 3.6.1.- (Kif5b protein, mouse); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171017
[St] Status:MEDLINE


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[PMID]:28991265
[Au] Autor:Atherton J; Jiang K; Stangier MM; Luo Y; Hua S; Houben K; van Hooff JJE; Joseph AP; Scarabelli G; Grant BJ; Roberts AJ; Topf M; Steinmetz MO; Baldus M; Moores CA; Akhmanova A
[Ad] Endereço:Institute of Structural and Molecular Biology, Birkbeck, University of London, London, UK.
[Ti] Título:A structural model for microtubule minus-end recognition and protection by CAMSAP proteins.
[So] Source:Nat Struct Mol Biol;24(11):931-943, 2017 Nov.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CAMSAP and Patronin family members regulate microtubule minus-end stability and localization and thus organize noncentrosomal microtubule networks, which are essential for cell division, polarization and differentiation. Here, we found that the CAMSAP C-terminal CKK domain is widely present among eukaryotes and autonomously recognizes microtubule minus ends. Through a combination of structural approaches, we uncovered how mammalian CKK binds between two tubulin dimers at the interprotofilament interface on the outer microtubule surface. In vitro reconstitution assays combined with high-resolution fluorescence microscopy and cryo-electron tomography suggested that CKK preferentially associates with the transition zone between curved protofilaments and the regular microtubule lattice. We propose that minus-end-specific features of the interprotofilament interface at this site serve as the basis for CKK's minus-end preference. The steric clash between microtubule-bound CKK and kinesin motors explains how CKK protects microtubule minus ends against kinesin-13-induced depolymerization and thus controls the stability of free microtubule minus ends.
[Mh] Termos MeSH primário: Cinesina/antagonistas & inibidores
Proteínas Associadas aos Microtúbulos/química
Proteínas Associadas aos Microtúbulos/metabolismo
Microtúbulos/metabolismo
[Mh] Termos MeSH secundário: Microscopia Crioeletrônica
Tomografia com Microscopia Eletrônica
Eucariotos
Microscopia de Fluorescência
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Microtubule-Associated Proteins); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171010
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3483



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