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  1 / 7537 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 / 7537 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 / 7537 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


  4 / 7537 MEDLINE  
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[PMID]:28950095
[Au] Autor:Barford K; Keeler A; Deppmann C; Winckler B
[Ad] Endereço:Department of Cell Biology, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908-0732, USA.
[Ti] Título:TrkA Bumps into Its Future Self.
[So] Source:Dev Cell;42(6):557-558, 2017 09 25.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In neurons, correct targeting of receptors to the axon is critical for cell survival and circuit formation. In this issue of Developmental Cell, Yamashita et al. (2017) report that the ER-resident phosphatase PTP1B is required to prime TrkA for axonal transport.
[Mh] Termos MeSH primário: Transporte Axonal
Receptor trkA
[Mh] Termos MeSH secundário: Axônios
Sobrevivência Celular
Seres Humanos
Neurônios
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
EC 2.7.10.1 (Receptor, trkA)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE


  5 / 7537 MEDLINE  
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[PMID]:28784610
[Au] Autor:Gowrishankar S; Wu Y; Ferguson SM
[Ad] Endereço:Department of Cell Biology, Yale University School of Medicine, New Haven, CT.
[Ti] Título:Impaired JIP3-dependent axonal lysosome transport promotes amyloid plaque pathology.
[So] Source:J Cell Biol;216(10):3291-3305, 2017 Oct 02.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysosomes robustly accumulate within axonal swellings at Alzheimer's disease (AD) amyloid plaques. However, the underlying mechanisms and disease relevance of such lysosome accumulations are not well understood. Motivated by these problems, we identified JNK-interacting protein 3 (JIP3) as an important regulator of axonal lysosome transport and maturation. JIP3 knockout mouse neuron primary cultures accumulate lysosomes within focal axonal swellings that resemble the dystrophic axons at amyloid plaques. These swellings contain high levels of amyloid precursor protein processing enzymes (BACE1 and presenilin 2) and are accompanied by elevated Aß peptide levels. The in vivo importance of the JIP3-dependent regulation of axonal lysosomes was revealed by the worsening of the amyloid plaque pathology arising from JIP3 haploinsufficiency in a mouse model of AD. These results establish the critical role of JIP3-dependent axonal lysosome transport in regulating amyloidogenic amyloid precursor protein processing and support a model wherein Aß production is amplified by plaque-induced axonal lysosome transport defects.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Doença de Alzheimer/metabolismo
Peptídeos beta-Amiloides/metabolismo
Transporte Axonal
Axônios/metabolismo
Lisossomos/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Placa Amiloide/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Doença de Alzheimer/genética
Doença de Alzheimer/patologia
Secretases da Proteína Precursora do Amiloide/genética
Secretases da Proteína Precursora do Amiloide/metabolismo
Peptídeos beta-Amiloides/genética
Animais
Ácido Aspártico Endopeptidases/genética
Ácido Aspártico Endopeptidases/metabolismo
Axônios/patologia
Modelos Animais de Doenças
Lisossomos/genética
Lisossomos/patologia
Camundongos
Camundongos Knockout
Proteínas do Tecido Nervoso/genética
Placa Amiloide/genética
Placa Amiloide/patologia
Presenilina-2/genética
Presenilina-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Amyloid beta-Peptides); 0 (Mapk8ip3 protein, mouse); 0 (Nerve Tissue Proteins); 0 (Presenilin-2); 0 (Psen2 protein, mouse); EC 3.4.- (Amyloid Precursor Protein Secretases); EC 3.4.23.- (Aspartic Acid Endopeptidases); EC 3.4.23.46 (Bace1 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201612148


  6 / 7537 MEDLINE  
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[PMID]:28559423
[Au] Autor:Ganguly A; Han X; Das U; Wang L; Loi J; Sun J; Gitler D; Caillol G; Leterrier C; Yates JR; Roy S
[Ad] Endereço:Department of Pathology, University of California, San Diego, La Jolla, CA.
[Ti] Título:Hsc70 chaperone activity is required for the cytosolic slow axonal transport of synapsin.
[So] Source:J Cell Biol;216(7):2059-2074, 2017 Jul 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Soluble cytosolic proteins vital to axonal and presynaptic function are synthesized in the neuronal soma and conveyed via slow axonal transport. Our previous studies suggest that the overall slow transport of synapsin is mediated by dynamic assembly/disassembly of cargo complexes followed by short-range vectorial transit (the "dynamic recruitment" model). However, neither the composition of these complexes nor the mechanistic basis for the dynamic behavior is understood. In this study, we first examined putative cargo complexes associated with synapsin using coimmunoprecipitation and multidimensional protein identification technology mass spectrometry (MS). MS data indicate that synapsin is part of a multiprotein complex enriched in chaperones/cochaperones including Hsc70. Axonal synapsin-Hsc70 coclusters are also visualized by two-color superresolution microscopy. Inhibition of Hsc70 ATPase activity blocked the slow transport of synapsin, disrupted axonal synapsin organization, and attenuated Hsc70-synapsin associations, advocating a model where Hsc70 activity dynamically clusters cytosolic proteins into cargo complexes, allowing transport. Collectively, our study offers insight into the molecular organization of cytosolic transport complexes and identifies a novel regulator of slow transport.
[Mh] Termos MeSH primário: Transporte Axonal
Proteínas de Choque Térmico HSC70/metabolismo
Hipocampo/metabolismo
Neurônios/metabolismo
Sinapsinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Feminino
Células HEK293
Proteínas de Choque Térmico HSC70/genética
Hipocampo/citologia
Seres Humanos
Imunoprecipitação
Cinética
Masculino
Espectrometria de Massas
Camundongos Knockout
Microscopia/métodos
Modelos Biológicos
Complexos Multiproteicos
Mapas de Interação de Proteínas
Proteômica/métodos
Ratos
Sinapsinas/deficiência
Sinapsinas/genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HSC70 Heat-Shock Proteins); 0 (HSPA8 protein, human); 0 (Hspa8 protein, mouse); 0 (Hspa8 protein, rat); 0 (Multiprotein Complexes); 0 (Synapsins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170601
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201604028


  7 / 7537 MEDLINE  
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[PMID]:28542430
[Au] Autor:Liao PC; Tandarich LC; Hollenbeck PJ
[Ad] Endereço:Department of Biological Sciences, Purdue University, West Lafayette, Indiana, United States of America.
[Ti] Título:ROS regulation of axonal mitochondrial transport is mediated by Ca2+ and JNK in Drosophila.
[So] Source:PLoS One;12(5):e0178105, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondria perform critical functions including aerobic ATP production and calcium (Ca2+) homeostasis, but are also a major source of reactive oxygen species (ROS) production. To maintain cellular function and survival in neurons, mitochondria are transported along axons, and accumulate in regions with high demand for their functions. Oxidative stress and abnormal mitochondrial axonal transport are associated with neurodegenerative disorders. However, we know little about the connection between these two. Using the Drosophila third instar larval nervous system as the in vivo model, we found that ROS inhibited mitochondrial axonal transport more specifically, primarily due to reduced flux and velocity, but did not affect transport of other organelles. To understand the mechanisms underlying these effects, we examined Ca2+ levels and the JNK (c-Jun N-terminal Kinase) pathway, which have been shown to regulate mitochondrial transport and general fast axonal transport, respectively. We found that elevated ROS increased Ca2+ levels, and that experimental reduction of Ca2+ to physiological levels rescued ROS-induced defects in mitochondrial transport in primary neuron cell cultures. In addition, in vivo activation of the JNK pathway reduced mitochondrial flux and velocities, while JNK knockdown partially rescued ROS-induced defects in the anterograde direction. We conclude that ROS have the capacity to regulate mitochondrial traffic, and that Ca2+ and JNK signaling play roles in mediating these effects. In addition to transport defects, ROS produces imbalances in mitochondrial fission-fusion and metabolic state, indicating that mitochondrial transport, fission-fusion steady state, and metabolic state are closely interrelated in the response to ROS.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila/metabolismo
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Mitocôndrias/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Axonal/efeitos dos fármacos
Axônios/metabolismo
Proteínas de Drosophila/antagonistas & inibidores
Proteínas de Drosophila/genética
Peróxido de Hidrogênio/toxicidade
Proteínas Quinases JNK Ativadas por Mitógeno/antagonistas & inibidores
Proteínas Quinases JNK Ativadas por Mitógeno/genética
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Mitocôndrias/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Paraquat/farmacologia
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Superóxido Dismutase/genética
Superóxido Dismutase/metabolismo
Tapsigargina/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); 67526-95-8 (Thapsigargin); BBX060AN9V (Hydrogen Peroxide); EC 1.15.1.1 (Superoxide Dismutase); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); PLG39H7695 (Paraquat); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178105


  8 / 7537 MEDLINE  
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[PMID]:28432142
[Au] Autor:Vullhorst D; Ahmad T; Karavanova I; Keating C; Buonanno A
[Ad] Endereço:Section on Molecular Neurobiology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, Maryland 20892.
[Ti] Título:Structural Similarities between Neuregulin 1-3 Isoforms Determine Their Subcellular Distribution and Signaling Mode in Central Neurons.
[So] Source:J Neurosci;37(21):5232-5249, 2017 May 24.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Neuregulin (NRG) family of ErbB ligands is comprised of numerous variants originating from the use of different genes, alternative promoters, and splice variants. NRGs have generally been thought to be transported to axons and presynaptic terminals where they signal via ErbB3/4 receptors in paracrine or juxtacrine mode. However, we recently demonstrated that unprocessed pro-NRG2 accumulates on cell bodies and proximal dendrites, and that NMDAR activity is required for shedding of its ectodomain by metalloproteinases. Here we systematically investigated the subcellular distribution and processing of major NRG isoforms in rat hippocampal neurons. We show that NRG1 isotypes I and II, which like NRG2 are single-pass transmembrane proteins with an Ig-like domain, share the same subcellular distribution and ectodomain shedding properties. We furthermore show that NRG3, like CRD-NRG1, is a dual-pass transmembrane protein that harbors a second transmembrane domain near its amino terminus. Both NRG3 and CRD-NRG1 cluster on axons through juxtacrine interactions with ErbB4 present on GABAergic interneurons. Interestingly, although single-pass NRGs accumulate as unprocessed proforms, axonal puncta of CRD-NRG1 and NRG3 are comprised of processed protein. Mutations of CRD-NRG1 and NRG3 that render them resistant to BACE cleavage, as well as BACE inhibition, result in the loss of axonal puncta and in the accumulation of unprocessed proforms in neuronal soma. Together, these results define two groups of NRGs with distinct membrane topologies and fundamentally different targeting and processing properties in central neurons. The implications of this functional diversity for the regulation of neuronal processes by the NRG/ErbB pathway are discussed. Numerous Neuregulins (NRGs) are generated through the use of different genes, promoters, and alternative splicing, but the functional significance of this evolutionary conserved diversity remains poorly understood. Here we show that NRGs can be categorized by their membrane topologies. Single-pass NRGs, such as NRG1 Types I/II and NRG2, accumulate as unprocessed proforms on cell bodies, and their ectodomains are shed by metalloproteinases in response to NMDA receptor activation. By contrast, dual-pass CRD-NRG1 and NRG3 are constitutively processed by BACE and accumulate on axons where they interact with ErbB4 in juxtacrine mode. These findings reveal a previously unknown functional relationship between membrane topology, protein processing, and subcellular distribution, and suggest that single- and dual-pass NRGs regulate neuronal functions in fundamentally different ways.
[Mh] Termos MeSH primário: Neuregulina-1/metabolismo
Neurônios/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Ácido Aspártico Endopeptidases/metabolismo
Transporte Axonal
Células Cultivadas
Córtex Cerebral/citologia
Feminino
Células HEK293
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Neuregulina-1/genética
Neurônios/classificação
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Transporte Proteico
Proteólise
Ratos
Ratos Sprague-Dawley
Receptor ErbB-4/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neuregulin-1); 0 (Protein Isoforms); EC 2.7.10.1 (Receptor, ErbB-4); EC 3.4.23.- (Aspartic Acid Endopeptidases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170423
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.2630-16.2017


  9 / 7537 MEDLINE  
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[PMID]:28426968
[Au] Autor:Gumy LF; Katrukha EA; Grigoriev I; Jaarsma D; Kapitein LC; Akhmanova A; Hoogenraad CC
[Ad] Endereço:Cell Biology, Department of Biology, Faculty of Science, Utrecht University, 3584 CH Utrecht, the Netherlands.
[Ti] Título:MAP2 Defines a Pre-axonal Filtering Zone to Regulate KIF1- versus KIF5-Dependent Cargo Transport in Sensory Neurons.
[So] Source:Neuron;94(2):347-362.e7, 2017 Apr 19.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polarized cargo transport is essential for neuronal function. However, the minimal basic components required for selective cargo sorting and distribution in neurons remain elusive. We found that in sensory neurons the axon initial segment is largely absent and that microtubule-associated protein 2 (MAP2) defines the cargo-filtering zone in the proximal axon. Here, MAP2 directs axonal cargo entry by coordinating the activities of molecular motors. We show that distinct kinesins differentially regulate cargo velocity: kinesin-3 drives fast axonal cargo trafficking, while kinesin-1 slows down axonal cargo transport. MAP2 inhibits "slow" kinesin-1 motor activity and allows kinesin-3 to drive robust cargo transport from the soma into the axon. In the distal axon, the inhibitory action of MAP2 decreases, leading to regained kinesin-1 activity and vesicle distribution. We propose that selective axonal cargo trafficking requires the MAP2-defined pre-axonal filtering zone and the ability of cargos to switch between distinct kinesin motor activities.
[Mh] Termos MeSH primário: Transporte Axonal/fisiologia
Axônios/metabolismo
Cinesina/metabolismo
Proteínas Associadas aos Microtúbulos/metabolismo
Células Receptoras Sensoriais/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Células Cultivadas
Dendritos/metabolismo
Microtúbulos/metabolismo
Modelos Biológicos
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Microtubule-Associated Proteins); 0 (Mtap2 protein, rat); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE


  10 / 7537 MEDLINE  
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[PMID]:28426954
[Au] Autor:Ribeiro LF; de Wit J
[Ad] Endereço:VIB Center for Brain & Disease Research, Herestraat 49, 3000 Leuven, Belgium; Department of Neurosciences, KU Leuven, Herestraat 49, 3000 Leuven, Belgium.
[Ti] Título:Neuronal Polarity: MAP2 Shifts Secretory Vesicles into High Gear for Long-Haul Transport down the Axon.
[So] Source:Neuron;94(2):223-225, 2017 Apr 19.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accurate control of polarized cargo trafficking is essential for neuronal function. In this issue of Neuron, Gumy et al. (2017) show that MAP2 defines a pre-axonal filtering zone and controls axonal cargo transport by influencing the activities of distinct kinesin motors.
[Mh] Termos MeSH primário: Transporte Axonal/fisiologia
Axônios/metabolismo
Polaridade Celular/fisiologia
Microtúbulos/metabolismo
Neurônios/metabolismo
Vesículas Secretórias/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE



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