Base de dados : MEDLINE
Pesquisa : A11.284.430.214.190.750.585.079 [Categoria DeCS]
Referências encontradas : 94 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 10 ir para página                        

  1 / 94 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29244804
[Au] Autor:Siller SS; Sharma H; Li S; Yang J; Zhang Y; Holtzman MJ; Winuthayanon W; Colognato H; Holdener BC; Li FQ; Takemaru KI
[Ad] Endereço:Medical Scientist Training Program (MSTP), Stony Brook University, Stony Brook, New York, United States of America.
[Ti] Título:Conditional knockout mice for the distal appendage protein CEP164 reveal its essential roles in airway multiciliated cell differentiation.
[So] Source:PLoS Genet;13(12):e1007128, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Multiciliated cells of the airways, brain ventricles, and female reproductive tract provide the motive force for mucociliary clearance, cerebrospinal fluid circulation, and ovum transport. Despite their clear importance to human biology and health, the molecular mechanisms underlying multiciliated cell differentiation are poorly understood. Prior studies implicate the distal appendage/transition fiber protein CEP164 as a central regulator of primary ciliogenesis; however, its role in multiciliogenesis remains unknown. In this study, we have generated a novel conditional mouse model that lacks CEP164 in multiciliated tissues and the testis. These mice show a profound loss of airway, ependymal, and oviduct multicilia and develop hydrocephalus and male infertility. Using primary cultures of tracheal multiciliated cells as a model system, we found that CEP164 is critical for multiciliogenesis, at least in part, via its regulation of small vesicle recruitment, ciliary vesicle formation, and basal body docking. In addition, CEP164 is necessary for the proper recruitment of another distal appendage/transition fiber protein Chibby1 (Cby1) and its binding partners FAM92A and FAM92B to the ciliary base in multiciliated cells. In contrast to primary ciliogenesis, CEP164 is dispensable for the recruitment of intraflagellar transport (IFT) components to multicilia. Finally, we provide evidence that CEP164 differentially controls the ciliary targeting of membrane-associated proteins, including the small GTPases Rab8, Rab11, and Arl13b, in multiciliated cells. Altogether, our studies unravel unique requirements for CEP164 in primary versus multiciliogenesis and suggest that CEP164 modulates the selective transport of membrane vesicles and their cargoes into the ciliary compartment in multiciliated cells. Furthermore, our mouse model provides a useful tool to gain physiological insight into diseases associated with defective multicilia.
[Mh] Termos MeSH primário: Cílios/fisiologia
Proteínas dos Microtúbulos/fisiologia
[Mh] Termos MeSH secundário: Animais
Corpos Basais/metabolismo
Diferenciação Celular/fisiologia
Células Cultivadas
Centríolos/metabolismo
Cílios/genética
Cílios/metabolismo
Células Epiteliais/citologia
Feminino
Masculino
Proteínas de Membrana/metabolismo
Camundongos
Camundongos Knockout
Proteínas dos Microtúbulos/genética
Proteínas dos Microtúbulos/metabolismo
Proteínas Nucleares/metabolismo
Transporte Proteico
Traqueia/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Microtubule Proteins); 0 (Nuclear Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007128


  2 / 94 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28698599
[Au] Autor:Reiter JF; Leroux MR
[Ad] Endereço:Department of Biochemistry and Biophysics and Cardiovascular Research Institute, University of California, San Francisco, San Francisco CA 94158, USA.
[Ti] Título:Genes and molecular pathways underpinning ciliopathies.
[So] Source:Nat Rev Mol Cell Biol;18(9):533-547, 2017 Sep.
[Is] ISSN:1471-0080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Motile and non-motile (primary) cilia are nearly ubiquitous cellular organelles. The dysfunction of cilia causes diseases known as ciliopathies. The number of reported ciliopathies (currently 35) is increasing, as is the number of established (187) and candidate (241) ciliopathy-associated genes. The characterization of ciliopathy-associated proteins and phenotypes has improved our knowledge of ciliary functions. In particular, investigating ciliopathies has helped us to understand the molecular mechanisms by which the cilium-associated basal body functions in early ciliogenesis, as well as how the transition zone functions in ciliary gating, and how intraflagellar transport enables cargo trafficking and signalling. Both basic biological and clinical studies are uncovering novel ciliopathies and the ciliary proteins involved. The assignment of these proteins to different ciliary structures, processes and ciliopathy subclasses (first order and second order) provides insights into how this versatile organelle is built, compartmentalized and functions in diverse ways that are essential for human health.
[Mh] Termos MeSH primário: Ciliopatias/genética
Ciliopatias/metabolismo
[Mh] Termos MeSH secundário: Animais
Corpos Basais/metabolismo
Cílios/metabolismo
Seres Humanos
Proteínas Associadas aos Microtúbulos/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Microtubule-Associated Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1038/nrm.2017.60


  3 / 94 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28666954
[Au] Autor:Stauber M; Boldt K; Wrede C; Weidemann M; Kellner M; Schuster-Gossler K; Kühnel MP; Hegermann J; Ueffing M; Gossler A
[Ad] Endereço:Institute for Molecular Biology, OE5250, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany; REBIRTH Cluster of Excellence, Hannover, Germany. Electronic address: stauber.m@web.de.
[Ti] Título:1700012B09Rik, a FOXJ1 effector gene active in ciliated tissues of the mouse but not essential for motile ciliogenesis.
[So] Source:Dev Biol;429(1):186-199, 2017 09 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In humans and mice, motile cilia occur on the surface of the embryonic ventral node, on respiratory and ependymal epithelia and in reproductive organs where they ensure normal left-right asymmetry of the organism, mucociliary clearance of airways, homeostasis of the cerebrospinal fluid and fertility. The genetic programme for the formation of motile cilia, thus critical for normal development and health, is switched on by the key transcription factor FOXJ1. In previous microarray screens for murine FOXJ1 effectors, we identified candidates for novel factors involved in motile ciliogenesis, including both genes that are well conserved throughout metazoa and beyond, like FOXJ1 itself, and genes without overt homologues outside higher vertebrates. Here we examine one of the novel murine FOXJ1 effectors, the uncharacterised 1700012B09Rik whose homologues appear to be restricted to higher vertebrates. In mouse embryos and adults, 1700012B09Rik is predominantly expressed in motile ciliated tissues in a FOXJ1-dependent manner. 1700012B09RIK protein localises to basal bodies of cilia in cultured cells. Detailed analysis of 1700012B09Rik knock-out mice reveals no impaired function of motile cilia or non-motile cilia. In conclusion, this novel FOXJ1 effector is associated mainly with motile cilia but - in contrast to other known FOXJ1 targets - its putative ciliary function is not essential for development or health in the mouse, consistent with a late emergence during evolution of motile ciliogenesis.
[Mh] Termos MeSH primário: Cílios/metabolismo
Fatores de Transcrição Forkhead/metabolismo
Morfogênese
[Mh] Termos MeSH secundário: Alelos
Animais
Corpos Basais/metabolismo
Feminino
Genes Reporter
Homozigoto
Masculino
Camundongos Knockout
Complexos Multiproteicos/metabolismo
Fenótipo
Transporte Proteico
Frações Subcelulares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (1700012B09Rik protein, mouse); 0 (FOXJ1 protein, mouse); 0 (Forkhead Transcription Factors); 0 (Multiprotein Complexes)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170702
[St] Status:MEDLINE


  4 / 94 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28625504
[Au] Autor:Van De Weghe JC; Rusterholz TDS; Latour B; Grout ME; Aldinger KA; Shaheen R; Dempsey JC; Maddirevula S; Cheng YH; Phelps IG; Gesemann M; Goel H; Birk OS; Alanzi T; Rawashdeh R; Khan AO; Bamshad MJ; Nickerson DA; Neuhauss SCF; Dobyns WB; Alkuraya FS; Roepman R; Bachmann-Gagescu R; Doherty D; University of Washington Center for Mendelian Genomics
[Ad] Endereço:Department of Pediatrics, University of Washington, Seattle, WA 98195, USA.
[Ti] Título:Mutations in ARMC9, which Encodes a Basal Body Protein, Cause Joubert Syndrome in Humans and Ciliopathy Phenotypes in Zebrafish.
[So] Source:Am J Hum Genet;101(1):23-36, 2017 Jul 06.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Joubert syndrome (JS) is a recessive neurodevelopmental disorder characterized by hypotonia, ataxia, abnormal eye movements, and variable cognitive impairment. It is defined by a distinctive brain malformation known as the "molar tooth sign" on axial MRI. Subsets of affected individuals have malformations such as coloboma, polydactyly, and encephalocele, as well as progressive retinal dystrophy, fibrocystic kidney disease, and liver fibrosis. More than 35 genes have been associated with JS, but in a subset of families the genetic cause remains unknown. All of the gene products localize in and around the primary cilium, making JS a canonical ciliopathy. Ciliopathies are unified by their overlapping clinical features and underlying mechanisms involving ciliary dysfunction. In this work, we identify biallelic rare, predicted-deleterious ARMC9 variants (stop-gain, missense, splice-site, and single-exon deletion) in 11 individuals with JS from 8 families, accounting for approximately 1% of the disorder. The associated phenotypes range from isolated neurological involvement to JS with retinal dystrophy, additional brain abnormalities (e.g., heterotopia, Dandy-Walker malformation), pituitary insufficiency, and/or synpolydactyly. We show that ARMC9 localizes to the basal body of the cilium and is upregulated during ciliogenesis. Typical ciliopathy phenotypes (curved body shape, retinal dystrophy, coloboma, and decreased cilia) in a CRISPR/Cas9-engineered zebrafish mutant model provide additional support for ARMC9 as a ciliopathy-associated gene. Identifying ARMC9 mutations as a cause of JS takes us one step closer to a full genetic understanding of this important disorder and enables future functional work to define the central biological mechanisms underlying JS and other ciliopathies.
[Mh] Termos MeSH primário: Anormalidades Múltiplas/genética
Proteínas do Domínio Armadillo/genética
Corpos Basais/metabolismo
Cerebelo/anormalidades
Ciliopatias/genética
Anormalidades do Olho/genética
Doenças Renais Císticas/genética
Mutação/genética
Retina/anormalidades
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Anormalidades Múltiplas/patologia
Animais
Proteínas do Domínio Armadillo/metabolismo
Sequência de Bases
Encéfalo/patologia
Cerebelo/patologia
Cílios/metabolismo
Ciliopatias/patologia
Diagnóstico por Imagem
Exoma/genética
Anormalidades do Olho/patologia
Predisposição Genética para Doença
Seres Humanos
Doenças Renais Císticas/patologia
Fenótipo
Retina/patologia
Análise de Sequência de DNA
Regulação para Cima/genética
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ARMC9 protein, human); 0 (ARMC9 protein, zebrafish); 0 (Armadillo Domain Proteins); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE


  5 / 94 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28476861
[Au] Autor:Lattao R; Kovács L; Glover DM
[Ad] Endereço:Department of Genetics, University of Cambridge, CB2 3EH, United Kingdom.
[Ti] Título:The Centrioles, Centrosomes, Basal Bodies, and Cilia of .
[So] Source:Genetics;206(1):33-53, 2017 May.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Centrioles play a key role in the development of the fly. They are needed for the correct formation of centrosomes, the organelles at the poles of the spindle that can persist as microtubule organizing centers (MTOCs) into interphase. The ability to nucleate cytoplasmic microtubules (MTs) is a property of the surrounding pericentriolar material (PCM). The centriole has a dual life, existing not only as the core of the centrosome but also as the basal body, the structure that templates the formation of cilia and flagellae. Thus the structure and functions of the centriole, the centrosome, and the basal body have an impact upon many aspects of development and physiology that can readily be modeled in Centrosomes are essential to give organization to the rapidly increasing numbers of nuclei in the syncytial embryo and for the spatially precise execution of cell division in numerous tissues, particularly during male meiosis. Although mitotic cell cycles can take place in the absence of centrosomes, this is an error-prone process that opens up the fly to developmental defects and the potential of tumor formation. Here, we review the structure and functions of the centriole, the centrosome, and the basal body in different tissues and cultured cells of , highlighting their contributions to different aspects of development and cell division.
[Mh] Termos MeSH primário: Corpos Basais
Centríolos/genética
Centrossomo
Cílios/genética
[Mh] Termos MeSH secundário: Animais
Drosophila melanogaster/genética
Meiose/genética
Microtúbulos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170507
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.116.198168


  6 / 94 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28428259
[Au] Autor:Nishijima Y; Hagiya Y; Kubo T; Takei R; Katoh Y; Nakayama K
[Ad] Endereço:Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan.
[Ti] Título:RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly.
[So] Source:Mol Biol Cell;28(12):1652-1666, 2017 Jun 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteins localized to the basal body and the centrosome play crucial roles in ciliary assembly and function. Although RABL2 and CEP19 are conserved in ciliated organisms and have been implicated in ciliary/flagellar functions, their roles are poorly understood. Here we show that RABL2 interacts with CEP19 and is recruited to the mother centriole and basal body in a CEP19-dependent manner and that CEP19 is recruited to the centriole probably via its binding to the centrosomal protein FGFR1OP. Disruption of the gene in results in the nonflagellated phenotype, suggesting a crucial role of RABL2 in ciliary/flagellar assembly. We also show that RABL2 interacts, in its GTP-bound state, with the intraflagellar transport (IFT)-B complex via the IFT74-IFT81 heterodimer and that the interaction is disrupted by a mutation found in male infertile mice ( mice) with a sperm flagella motility defect. Intriguingly, RABL2 binds to CEP19 and the IFT74-IFT81 heterodimer in a mutually exclusive manner. Furthermore, exogenous expression of the GDP-locked or -type RABL2 mutant in human cells results in mild defects in ciliary assembly. These results indicate that RABL2 localized to the basal body plays crucial roles in ciliary/flagellar assembly via its interaction with the IFT-B complex.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Cílios/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Corpos Basais/metabolismo
Transporte Biológico
Centríolos/metabolismo
Chlamydomonas reinhardtii/genética
Chlamydomonas reinhardtii/metabolismo
Flagelos/metabolismo
Células HEK293
Seres Humanos
Infertilidade Masculina/genética
Infertilidade Masculina/metabolismo
Masculino
Camundongos
Fenótipo
Ligação Proteica
Motilidade Espermática
Proteínas rab de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CEP19 protein, human); 0 (Cell Cycle Proteins); EC 3.6.1.- (RABL2A protein, human); EC 3.6.5.2 (rab GTP-Binding Proteins)
[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:170422
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E17-01-0017


  7 / 94 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28411364
[Au] Autor:Nechipurenko IV; Berciu C; Sengupta P; Nicastro D
[Ad] Endereço:Department of Biology and National Center for Behavioral Genomics, Brandeis University, Waltham, United States.
[Ti] Título:Centriolar remodeling underlies basal body maturation during ciliogenesis in .
[So] Source:Elife;6, 2017 Apr 15.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The primary cilium is nucleated by the mother centriole-derived basal body (BB) via as yet poorly characterized mechanisms. BBs have been reported to degenerate following ciliogenesis in the embryo, although neither BB architecture nor early ciliogenesis steps have been described in this organism. In a previous study (Doroquez et al., 2014), we described the three-dimensional morphologies of sensory neuron cilia in adult hermaphrodites at high resolution. Here, we use serial section electron microscopy and tomography of staged embryos to demonstrate that BBs remodel to support ciliogenesis in a subset of sensory neurons. We show that centriolar singlet microtubules are converted into BB doublets which subsequently grow asynchronously to template the ciliary axoneme, visualize degeneration of the centriole core, and define the developmental stage at which the transition zone is established. Our work provides a framework for future investigations into the mechanisms underlying BB remodeling.
[Mh] Termos MeSH primário: Caenorhabditis elegans/citologia
Caenorhabditis elegans/embriologia
Centríolos/metabolismo
Cílios/genética
Cílios/metabolismo
Biogênese de Organelas
[Mh] Termos MeSH secundário: Animais
Corpos Basais/metabolismo
Corpos Basais/ultraestrutura
Centríolos/ultraestrutura
Cílios/ultraestrutura
Tomografia com Microscopia Eletrônica
Microscopia Eletrônica
Células Receptoras Sensoriais/citologia
Células Receptoras Sensoriais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170416
[St] Status:MEDLINE


  8 / 94 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28411189
[Au] Autor:Serwas D; Su TY; Roessler M; Wang S; Dammermann A
[Ad] Endereço:Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter (VBC), A-1030 Vienna, Austria.
[Ti] Título:Centrioles initiate cilia assembly but are dispensable for maturation and maintenance in .
[So] Source:J Cell Biol;216(6):1659-1671, 2017 Jun 05.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cilia are cellular projections that assemble on centriole-derived basal bodies. While cilia assembly is absolutely dependent on centrioles, it is not known to what extent they contribute to downstream events. The nematode provides a unique opportunity to address this question, as centrioles do not persist at the base of mature cilia. Using fluorescence microscopy and electron tomography, we find that centrioles degenerate early during ciliogenesis. The transition zone and axoneme are not completely formed at this time, indicating that cilia maturation does not depend on intact centrioles. The hydrolethalus syndrome protein HYLS-1 is the only centriolar protein known to remain at the base of mature cilia and is required for intraflagellar transport trafficking. Surprisingly, targeted degradation of HYLS-1 after initiation of ciliogenesis does not affect ciliary structures. Taken together, our results indicate that while centrioles are essential to initiate cilia formation, they are dispensable for cilia maturation and maintenance.
[Mh] Termos MeSH primário: Corpos Basais/fisiologia
Caenorhabditis elegans/fisiologia
Centríolos/fisiologia
Neurogênese
Células Receptoras Sensoriais/fisiologia
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Axonema/fisiologia
Corpos Basais/metabolismo
Corpos Basais/ultraestrutura
Caenorhabditis elegans/genética
Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/ultraestrutura
Proteínas de Caenorhabditis elegans/metabolismo
Centríolos/metabolismo
Centríolos/ultraestrutura
Cílios/fisiologia
Tomografia com Microscopia Eletrônica
Microscopia de Fluorescência
Microscopia de Vídeo
Proteólise
Células Receptoras Sensoriais/metabolismo
Células Receptoras Sensoriais/ultraestrutura
Fatores de Tempo
Imagem com Lapso de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (HYLS-1 protein, C elegans)
[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:170416
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201610070


  9 / 94 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28342295
[Au] Autor:Prevo B; Scholey JM; Peterman EJG
[Ad] Endereço:Department of Cellular & Molecular Medicine, University of California San Diego, CA, USA.
[Ti] Título:Intraflagellar transport: mechanisms of motor action, cooperation, and cargo delivery.
[So] Source:FEBS J;284(18):2905-2931, 2017 Sep.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Intraflagellar transport (IFT) is a form of motor-dependent cargo transport that is essential for the assembly, maintenance, and length control of cilia, which play critical roles in motility, sensory reception, and signal transduction in virtually all eukaryotic cells. During IFT, anterograde kinesin-2 and retrograde IFT dynein motors drive the bidirectional transport of IFT trains that deliver cargo, for example, axoneme precursors such as tubulins as well as molecules of the signal transduction machinery, to their site of assembly within the cilium. Following its discovery in Chlamydomonas, IFT has emerged as a powerful model system for studying general principles of motor-dependent cargo transport and we now appreciate the diversity that exists in the mechanism of IFT within cilia of different cell types. The absence of heterotrimeric kinesin-2 function, for example, causes a complete loss of both IFT and cilia in Chlamydomonas, but following its loss in Caenorhabditis elegans, where its primary function is loading the IFT machinery into cilia, homodimeric kinesin-2-driven IFT persists and assembles a full-length cilium. Generally, heterotrimeric kinesin-2 and IFT dynein motors are thought to play widespread roles as core IFT motors, whereas homodimeric kinesin-2 motors are accessory motors that mediate different functions in a broad range of cilia, in some cases contributing to axoneme assembly or the delivery of signaling molecules but in many other cases their ciliary functions, if any, remain unknown. In this review, we focus on mechanisms of motor action, motor cooperation, and motor-dependent cargo delivery during IFT.
[Mh] Termos MeSH primário: Caenorhabditis elegans/metabolismo
Chlamydomonas/metabolismo
Cílios/metabolismo
Flagelos/metabolismo
[Mh] Termos MeSH secundário: Animais
Axonema/metabolismo
Axonema/ultraestrutura
Corpos Basais/metabolismo
Corpos Basais/ultraestrutura
Transporte Biológico
Caenorhabditis elegans/genética
Caenorhabditis elegans/ultraestrutura
Chlamydomonas/genética
Chlamydomonas/ultraestrutura
Cílios/ultraestrutura
Dineínas/química
Dineínas/genética
Dineínas/metabolismo
Flagelos/ultraestrutura
Regulação da Expressão Gênica
Cinesina/química
Cinesina/genética
Cinesina/metabolismo
Multimerização Proteica
Transdução de Sinais
Tubulina (Proteína)/química
Tubulina (Proteína)/genética
Tubulina (Proteína)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Tubulin); EC 3.6.4.2 (Dyneins); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170326
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14068


  10 / 94 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28263766
[Au] Autor:Himmelstein DS; Cajigas I; Bi C; Clark BS; Van Der Voort G; Kohtz JD
[Ad] Endereço:Department of Pediatrics, Feinberg School of Medicine, Northwestern University, Developmental Biology, Stanley Manne Children's Research Institute, Box 204, 2430 N. Halsted, Chicago, IL 60614, USA.
[Ti] Título:SHH E176/E177-Zn conformation is required for signaling at endogenous sites.
[So] Source:Dev Biol;424(2):221-235, 2017 04 15.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sonic hedgehog (SHH) is a master developmental regulator. In 1995, the SHH crystal structure predicted that SHH-E176 (human)/E177 (mouse) regulates signaling through a Zn -dependent mechanism. While Zn is known to be required for SHH protein stability, a regulatory role for SHH-E176 or Zn has not been described. Here, we show that SHH-E176/177 modulates Zn -dependent cross-linking in vitro and is required for endogenous signaling, in vivo. While ectopically expressed SHH-E176A is highly active, mice expressing SHH-E177A at endogenous sites (Shh ) are morphologically indistinguishable from mice lacking SHH (Shh ), with patterning defects in both embryonic spinal cord and forebrain. SHH-E177A distribution along the embryonic spinal cord ventricle is unaltered, suggesting that E177 does not control long-range transport. While SHH-E177A association with cilia basal bodies increases in embryonic ventral spinal cord, diffusely distributed SHH-E177A is not detected. Together, these results reveal a novel role for E177-Zn in regulating SHH signaling that may involve critical, cilia basal-body localized changes in cross-linking and/or conformation.
[Mh] Termos MeSH primário: Proteínas Hedgehog/química
Proteínas Hedgehog/metabolismo
Transdução de Sinais
Zinco/química
[Mh] Termos MeSH secundário: Animais
Anticorpos/química
Anticorpos/metabolismo
Especificidade de Anticorpos/imunologia
Corpos Basais/efeitos dos fármacos
Corpos Basais/metabolismo
Sequência de Bases
Cílios/efeitos dos fármacos
Cílios/metabolismo
Reagentes para Ligações Cruzadas/metabolismo
Embrião de Mamíferos/efeitos dos fármacos
Embrião de Mamíferos/metabolismo
Seres Humanos
Camundongos
Prosencéfalo/efeitos dos fármacos
Prosencéfalo/enzimologia
Prosencéfalo/metabolismo
Conformação Proteica
Multimerização Proteica/efeitos dos fármacos
Transdução de Sinais/efeitos dos fármacos
Medula Espinal/efeitos dos fármacos
Medula Espinal/embriologia
Medula Espinal/metabolismo
Zinco/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antibodies); 0 (Cross-Linking Reagents); 0 (Hedgehog Proteins); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170307
[St] Status:MEDLINE



página 1 de 10 ir para página                        
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde