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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 / 3564 MEDLINE  
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[PMID]:28743734
[Au] Autor:Li W; Yi P; Zhu Z; Zhang X; Li W; Ou G
[Ad] Endereço:Tsinghua-Peking Center for Life Sciences, School of Life Sciences and MOE Key Laboratory for Protein Science, Tsinghua University, Beijing, China.
[Ti] Título:Centriole translocation and degeneration during ciliogenesis in neurons.
[So] Source:EMBO J;36(17):2553-2566, 2017 09 01.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Neuronal cilia that are formed at the dendritic endings of sensory neurons are essential for sensory perception. However, it remains unclear how the centriole-derived basal body is positioned to form a template for cilium formation. Using fluorescence time-lapse microscopy, we show that the centriole translocates from the cell body to the dendrite tip in the sensory neurons. The centriolar protein SAS-5 interacts with the dynein light-chain LC8 and conditional mutations of cytoplasmic dynein-1 block centriole translocation and ciliogenesis. The components of the central tube are essential for the biogenesis of centrioles, which later drive ciliogenesis in the dendrite; however, the centriole loses these components at the late stage of centriole translocation and subsequently recruits transition zone and intraflagellar transport proteins. Together, our results provide a comprehensive model of ciliogenesis in sensory neurons and reveal the importance of the dynein-dependent centriole translocation in this process.
[Mh] Termos MeSH primário: Centríolos/fisiologia
Cílios/fisiologia
Células Receptoras Sensoriais/fisiologia
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans
Proteínas de Caenorhabditis elegans/metabolismo
Proteínas de Ciclo Celular/metabolismo
Dineínas/metabolismo
Morfogênese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Cell Cycle Proteins); 0 (SAS-5 protein, C elegans); EC 3.6.4.2 (Dyneins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180106
[Lr] Data última revisão:
180106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201796883


  3 / 3564 MEDLINE  
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[PMID]:28747439
[Au] Autor:Dewey EB; Johnston CA
[Ad] Endereço:Department of Biology, University of New Mexico, Albuquerque, NM 87131.
[Ti] Título:Diverse mitotic functions of the cytoskeletal cross-linking protein Shortstop suggest a role in Dynein/Dynactin activity.
[So] Source:Mol Biol Cell;28(19):2555-2568, 2017 Sep 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proper assembly and orientation of the bipolar mitotic spindle is critical to the fidelity of cell division. Mitotic precision fundamentally contributes to cell fate specification, tissue development and homeostasis, and chromosome distribution within daughter cells. Defects in these events are thought to contribute to several human diseases. The underlying mechanisms that function in spindle morphogenesis and positioning remain incompletely defined, however. Here we describe diverse roles for the actin-microtubule cross-linker Shortstop (Shot) in mitotic spindle function in Shot localizes to mitotic spindle poles, and its knockdown results in an unfocused spindle pole morphology and a disruption of proper spindle orientation. Loss of Shot also leads to chromosome congression defects, cell cycle progression delay, and defective chromosome segregation during anaphase. These mitotic errors trigger apoptosis in epithelial tissue, and blocking this apoptotic response results in a marked induction of the epithelial-mesenchymal transition marker MMP-1. The actin-binding domain of Shot directly interacts with Actin-related protein-1 (Arp-1), a key component of the Dynein/Dynactin complex. Knockdown of Arp-1 phenocopies Shot loss universally, whereas chemical disruption of F-actin does so selectively. Our work highlights novel roles for Shot in mitosis and suggests a mechanism involving Dynein/Dynactin activation.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Proteínas de Drosophila/fisiologia
Proteínas dos Microfilamentos/metabolismo
Proteínas dos Microfilamentos/fisiologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Anáfase
Animais
Ciclo Celular
Cromossomos/metabolismo
Citoesqueleto/patologia
Drosophila/metabolismo
Proteínas de Drosophila/genética
Complexo Dinactina/metabolismo
Dineínas/metabolismo
Proteínas dos Microfilamentos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Microtúbulos/metabolismo
Mitose/fisiologia
Ligação Proteica
Fuso Acromático/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Drosophila Proteins); 0 (Dynactin Complex); 0 (Microfilament Proteins); 0 (Microtubule-Associated Proteins); 0 (shot protein, Drosophila); EC 3.6.4.2 (Dyneins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180106
[Lr] Data última revisão:
180106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E17-04-0219


  4 / 3564 MEDLINE  
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[PMID]:29016643
[Au] Autor:Sarlah A; Vilfan A
[Ad] Endereço:Faculty of Mathematics and Physics, University of Ljubljana, Ljubljana, Slovenia.
[Ti] Título:Minimum requirements for motility of a processive motor protein.
[So] Source:PLoS One;12(10):e0185948, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Motor proteins generally have a two-way coupling between the ATP hydrolysis site, the lever movement and the binding affinity for their track, which allows them to perform efficient stepping. Here we explore the minimal requirements for directed motility based on simpler schemes in which the binding/unbinding from the track is decoupled from the ATPase cycle. We show that a directed power stroke alone is not sufficient for motility, but combined with an asymmetry in force-induced unbinding rates it can generate stepping. The energetic efficiency of such stepping is limited to approximately 20%. We conclude that the allosteric coupling between the ATP hydrolysis and the track binding is not strictly necessary for motility, but it greatly improves its efficiency.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/química
Trifosfato de Adenosina/química
Dineínas/química
Modelos Químicos
Modelos Moleculares
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/metabolismo
Trifosfato de Adenosina/metabolismo
Regulação Alostérica
Sítio Alostérico
Dineínas/metabolismo
Hidrólise
Cinética
Movimento (Física)
Multimerização Proteica
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.2 (Dyneins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185948


  5 / 3564 MEDLINE  
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[PMID]:28922373
[Au] Autor:King A; Li L; Wong DM; Liu R; Bamford R; Strasser A; Tarlinton DM; Heierhorst J
[Ad] Endereço:Molecular Genetics Unit, St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
[Ti] Título:Dynein light chain regulates adaptive and innate B cell development by distinctive genetic mechanisms.
[So] Source:PLoS Genet;13(9):e1007010, 2017 Sep.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mechanistic differences in the development and function of adaptive, high-affinity antibody-producing B-2 cells and innate-like, "natural" antibody-producing B-1a cells remain poorly understood. Here we show that the multi-functional dynein light chain (DYNLL1/LC8) plays important roles in the establishment of B-1a cells in the peritoneal cavity and in the ongoing development of B-2 lymphoid cells in the bone marrow of mice. Epistasis analyses indicate that Dynll1 regulates B-1a and early B-2 cell development in a single, linear pathway with its direct transcriptional activator ASCIZ (ATMIN/ZNF822), and that the two genes also have complementary functions during late B-2 cell development. The B-2 cell defects caused by loss of DYNLL1 were associated with lower levels of the anti-apoptotic protein BCL-2, and could be supressed by deletion of pro-apoptotic BIM which is negatively regulated by both DYNLL1 and BCL-2. Defects in B cell development caused by loss of DYNLL1 could also be partially suppressed by a pre-arranged SWHEL Igm-B cell receptor transgene. In contrast to the rescue of B-2 cell numbers, the B-1a cell deficiency in Dynll1-deleted mice could not be suppressed by the loss of Bim, and was further compounded by the SWHEL transgene. Conversely, oncogenic MYC expression, which is synthetic lethal with Dynll1 deletion in B-2 cells, did not further reduce B-1a cell numbers in Dynll1-defcient mice. Finally, we found that the ASCIZ-DYNLL1 axis was also required for the early-juvenile development of aggressive MYC-driven and p53-deficient B cell lymphomas. These results identify ASCIZ and DYNLL1 as the core of a transcriptional circuit that differentially regulates the development of the B-1a and B-2 B lymphoid cell lineages and plays a critical role in lymphomagenesis.
[Mh] Termos MeSH primário: Linfócitos B/metabolismo
Dineínas/genética
Linfoma de Células B/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Animais
Linfócitos B/imunologia
Linhagem da Célula/genética
Dineínas/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Linfócitos/metabolismo
Linfócitos/patologia
Linfoma de Células B/patologia
Camundongos
Cavidade Peritoneal
Proteínas Proto-Oncogênicas c-myc/genética
Fatores de Transcrição/metabolismo
Proteína Supressora de Tumor p53/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATMIN protein, mouse); 0 (Proto-Oncogene Proteins c-myc); 0 (Transcription Factors); 0 (Tumor Suppressor Protein p53); EC 3.6.4.2 (DYNLL1 protein, mouse); EC 3.6.4.2 (Dyneins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007010


  6 / 3564 MEDLINE  
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[PMID]:28892495
[Au] Autor:Yamamoto R; Obbineni JM; Alford LM; Ide T; Owa M; Hwang J; Kon T; Inaba K; James N; King SM; Ishikawa T; Sale WS; Dutcher SK
[Ad] Endereço:Department of Biological Sciences, Graduate School of Science, Osaka University, Osaka, Japan.
[Ti] Título:Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms.
[So] Source:PLoS Genet;13(9):e1006996, 2017 Sep.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytoplasmic assembly of ciliary dyneins, a process known as preassembly, requires numerous non-dynein proteins, but the identities and functions of these proteins are not fully elucidated. Here, we show that the classical Chlamydomonas motility mutant pf23 is defective in the Chlamydomonas homolog of DYX1C1. The pf23 mutant has a 494 bp deletion in the DYX1C1 gene and expresses a shorter DYX1C1 protein in the cytoplasm. Structural analyses, using cryo-ET, reveal that pf23 axonemes lack most of the inner dynein arms. Spectral counting confirms that DYX1C1 is essential for the assembly of the majority of ciliary inner dynein arms (IDA) as well as a fraction of the outer dynein arms (ODA). A C-terminal truncation of DYX1C1 shows a reduction in a subset of these ciliary IDAs. Sucrose gradients of cytoplasmic extracts show that preassembled ciliary dyneins are reduced compared to wild-type, which suggests an important role in dynein complex stability. The role of PF23/DYX1C1 remains unknown, but we suggest that DYX1C1 could provide a scaffold for macromolecular assembly.
[Mh] Termos MeSH primário: Proteínas de Algas/genética
Axonema/genética
Chlamydomonas reinhardtii/genética
Proteínas do Tecido Nervoso/genética
Proteínas Nucleares/genética
[Mh] Termos MeSH secundário: Animais
Axonema/química
Cílios/química
Cílios/genética
Citoplasma/genética
Citoplasma/metabolismo
Dineínas/química
Dineínas/genética
Flagelos/genética
Seres Humanos
Mutação
Proteínas do Tecido Nervoso/química
Proteínas Nucleares/química
Domínios Proteicos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (DYX1C1 protein, human); 0 (Nerve Tissue Proteins); 0 (Nuclear Proteins); EC 3.6.4.2 (Dyneins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006996


  7 / 3564 MEDLINE  
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[PMID]:28886386
[Au] Autor:DeSantis ME; Cianfrocco MA; Htet ZM; Tran PT; Reck-Peterson SL; Leschziner AE
[Ad] Endereço:Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
[Ti] Título:Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein.
[So] Source:Cell;170(6):1197-1208.e12, 2017 Sep 07.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulation is central to the functional versatility of cytoplasmic dynein, a motor involved in intracellular transport, cell division, and neurodevelopment. Previous work established that Lis1, a conserved regulator of dynein, binds to its motor domain and induces a tight microtubule-binding state in dynein. The work we present here-a combination of biochemistry, single-molecule assays, and cryoelectron microscopy-led to the surprising discovery that Lis1 has two opposing modes of regulating dynein, being capable of inducing both low and high affinity for the microtubule. We show that these opposing modes depend on the stoichiometry of Lis1 binding to dynein and that this stoichiometry is regulated by the nucleotide state of dynein's AAA3 domain. The low-affinity state requires Lis1 to also bind to dynein at a novel conserved site, mutation of which disrupts Lis1's function in vivo. We propose a new model for the regulation of dynein by Lis1.
[Mh] Termos MeSH primário: 1-Alquil-2-acetilglicerofosfocolina Esterase/metabolismo
Dineínas/metabolismo
Proteínas Associadas aos Microtúbulos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: 1-Alquil-2-acetilglicerofosfocolina Esterase/química
Trifosfato de Adenosina/metabolismo
Sequência de Aminoácidos
Microscopia Crioeletrônica
Dineínas/química
Seres Humanos
Proteínas Associadas aos Microtúbulos/química
Modelos Moleculares
Proteínas Motores Moleculares/metabolismo
Domínios Proteicos
Proteínas de Saccharomyces cerevisiae/química
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (KIP2 protein, S cerevisiae); 0 (Microtubule-Associated Proteins); 0 (Molecular Motor Proteins); 0 (Saccharomyces cerevisiae Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.1.1.47 (1-Alkyl-2-acetylglycerophosphocholine Esterase); EC 3.1.1.47 (PAFAH1B1 protein, S cerevisiae); EC 3.1.1.47 (PAFAH1B1 protein, human); EC 3.6.4.2 (Dyneins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE


  8 / 3564 MEDLINE  
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[PMID]:28883039
[Au] Autor:Huynh W; Vale RD
[Ad] Endereço:Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA.
[Ti] Título:Disease-associated mutations in human BICD2 hyperactivate motility of dynein-dynactin.
[So] Source:J Cell Biol;216(10):3051-3060, 2017 Oct 02.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bicaudal D2 (BICD2) joins dynein with dynactin into a ternary complex (termed DDB) capable of processive movement. Point mutations in the gene have been identified in patients with a dominant form of spinal muscular atrophy, but how these mutations cause disease is unknown. To investigate this question, we have developed in vitro motility assays with purified DDB and BICD2's membrane vesicle partner, the GTPase Rab6a. Rab6a-GTP, either in solution or bound to artificial liposomes, released BICD2 from an autoinhibited state and promoted robust dynein-dynactin transport. In these assays, BICD2 mutants showed an enhanced ability to form motile DDB complexes. Increased retrograde transport by BICD2 mutants also was observed in cells using an inducible organelle transport assay. When overexpressed in rat hippocampal neurons, the hyperactive BICD2 mutants decreased neurite growth. Our results reveal that dominant mutations in BICD2 hyperactivate DDB motility and suggest that an imbalance of minus versus plus end-directed microtubule motility in neurons may underlie spinal muscular atrophy.
[Mh] Termos MeSH primário: Complexo Dinactina/metabolismo
Dineínas/metabolismo
Proteínas Associadas aos Microtúbulos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Mutação Puntual
[Mh] Termos MeSH secundário: Animais
Transporte Biológico Ativo/genética
Linhagem Celular
Complexo Dinactina/genética
Dineínas/genética
Hipocampo/metabolismo
Hipocampo/patologia
Seres Humanos
Camundongos
Complexos Multiproteicos/genética
Complexos Multiproteicos/metabolismo
Atrofia Muscular Espinal/genética
Atrofia Muscular Espinal/metabolismo
Atrofia Muscular Espinal/patologia
Neuritos/metabolismo
Neuritos/patologia
Ratos
Suínos
Proteínas rab de Ligação ao GTP/genética
Proteínas rab de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BICD2 protein, human); 0 (Dynactin Complex); 0 (Microtubule-Associated Proteins); 0 (Multiprotein Complexes); 0 (Rab6 protein); EC 3.6.4.2 (Dyneins); EC 3.6.5.2 (rab GTP-Binding Proteins)
[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:170909
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201703201


  9 / 3564 MEDLINE  
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[PMID]:28850609
[Au] Autor:Kobayashi T; Miyashita T; Murayama T; Toyoshima YY
[Ad] Endereço:Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Meguro-ku, Tokyo, Japan.
[Ti] Título:Dynactin has two antagonistic regulatory domains and exerts opposing effects on dynein motility.
[So] Source:PLoS One;12(8):e0183672, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dynactin is a dynein-regulating protein that increases the processivity of dynein movement on microtubules. Recent studies have shown that a tripartite complex of dynein-dynactin-Bicaudal D2 is essential for highly processive movement. To elucidate the regulation of dynein motility by dynactin, we focused on two isoforms (A and B) of dynactin 1 (DCTN1), the largest subunit of dynactin that contains both microtubule- and dynein-binding domains. The only difference between the primary structures of the two isoforms is that DCTN1B lacks the K-rich domain, a cluster of basic residues. We measured dynein motility by single molecule observation of recombinant dynein and dynactin. Whereas the tripartite complex containing DCTN1A exhibited highly processive movement, the complex containing DCTN1B dissociated from microtubules with no apparent processive movement. This inhibitory effect of DCTN1B was caused by reductions of the microtubule-binding affinities of both dynein and dynactin, which was attributed to the coiled-coil 1 domain of DCTN1. In DCTN1A, the K-rich domain antagonized these inhibitory effects. Therefore, dynactin has two antagonistic domains and promotes or suppresses dynein motility to accomplish correct localization and functions of dynein within a cell.
[Mh] Termos MeSH primário: Complexo Dinactina/metabolismo
Dineínas/metabolismo
Isoformas de Proteínas/metabolismo
[Mh] Termos MeSH secundário: Células HEK293
Seres Humanos
Microtúbulos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dynactin Complex); 0 (Protein Isoforms); EC 3.6.4.2 (Dyneins)
[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:170830
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183672


  10 / 3564 MEDLINE  
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[PMID]:28835466
[Au] Autor:Kraft LM; Lackner LL
[Ad] Endereço:Department of Molecular Biosciences, Northwestern University, Evanston, IL.
[Ti] Título:Mitochondria-driven assembly of a cortical anchor for mitochondria and dynein.
[So] Source:J Cell Biol;216(10):3061-3071, 2017 Oct 02.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Interorganelle contacts facilitate communication between organelles and impact fundamental cellular functions. In this study, we examine the assembly of the MECA (mitochondria-endoplasmic reticulum [ER]-cortex anchor), which tethers mitochondria to the ER and plasma membrane. We find that the assembly of Num1, the core component of MECA, requires mitochondria. Once assembled, Num1 clusters persistently anchor mitochondria to the cell cortex. Num1 clusters also function to anchor dynein to the plasma membrane, where dynein captures and walks along astral microtubules to help orient the mitotic spindle. We find that dynein is anchored by Num1 clusters that have been assembled by mitochondria. When mitochondrial inheritance is inhibited, Num1 clusters are not assembled in the bud, and defects in dynein-mediated spindle positioning are observed. The mitochondria-dependent assembly of a dual-function cortical anchor provides a mechanism to integrate the positioning and inheritance of the two essential organelles and expands the function of organelle contact sites.
[Mh] Termos MeSH primário: Proteínas do Citoesqueleto/metabolismo
Dineínas/metabolismo
Retículo Endoplasmático/metabolismo
Mitocôndrias/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Fuso Acromático/metabolismo
[Mh] Termos MeSH secundário: Proteínas do Citoesqueleto/genética
Dineínas/genética
Retículo Endoplasmático/genética
Mitocôndrias/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Fuso Acromático/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytoskeletal Proteins); 0 (NUM1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.4.2 (Dyneins)
[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:170825
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201702022



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