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[PMID]: 28468990 [Au] Autor: Yu CJ; Lee FJ [Ad] Endereço: Department of Cell and Molecular Biology, College of Medicine, Chang Gung University, Linkou, Tao-Yuan 33302, Taiwan. [Ti] Título: Multiple activities of Arl1 GTPase in the trans-Golgi network. [So] Source: J Cell Sci;130(10):1691-1699, 2017 05 15. [Is] ISSN: 1477-9137 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: ADP-ribosylation factors (Arfs) and ADP-ribosylation factor-like proteins (Arls) are highly conserved small GTPases that function as main regulators of vesicular trafficking and cytoskeletal reorganization. Arl1, the first identified member of the large Arl family, is an important regulator of Golgi complex structure and function in organisms ranging from yeast to mammals. Together with its effectors, Arl1 has been shown to be involved in several cellular processes, including endosomal trans-Golgi network and secretory trafficking, lipid droplet and salivary granule formation, innate immunity and neuronal development, stress tolerance, as well as the response of the unfolded protein. In this Commentary, we provide a comprehensive summary of the Arl1-dependent cellular functions and a detailed characterization of several Arl1 effectors. We propose that involvement of Arl1 in these diverse cellular functions reflects the fact that Arl1 is activated at several late-Golgi sites, corresponding to specific molecular complexes that respond to and integrate multiple signals. We also provide insight into how the GTP-GDP cycle of Arl1 is regulated, and highlight a newly discovered mechanism that controls the sophisticated regulation of Arl1 activity at the Golgi complex. [Mh] Termos MeSH primário: Fatores de Ribosilação do ADP/metabolismo GTP Fosfo-Hidrolases/metabolismo Proteínas de Membrana/metabolismo Rede trans-Golgi/metabolismo [Mh] Termos MeSH secundário: Animais Membrana Celular/metabolismo Seres Humanos Transporte Proteico Vesículas Transportadoras/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; REVIEW [Nm] Nome de substância: 0 (Membrane Proteins); EC 3.6.1.- (ADP-ribosylation factor related proteins); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.2 (ADP-Ribosylation Factors) [Em] Mês de entrada: 1802 [Cu] Atualização por classe: 180223 [Lr] Data última revisão: 180223 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170505 [St] Status: MEDLINE [do] DOI: 10.1242/jcs.201319

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[PMID]: 29186191 [Au] Autor: O'Donoghue EJ; Sirisaengtaksin N; Browning DF; Bielska E; Hadis M; Fernandez-Trillo F; Alderwick L; Jabbari S; Krachler AM [Ad] Endereço: Institute of Microbiology and Infection, School of Biosciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom. [Ti] Título: Lipopolysaccharide structure impacts the entry kinetics of bacterial outer membrane vesicles into host cells. [So] Source: PLoS Pathog;13(11):e1006760, 2017 Nov. [Is] ISSN: 1553-7374 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Outer membrane vesicles are nano-sized microvesicles shed from the outer membrane of Gram-negative bacteria and play important roles in immune priming and disease pathogenesis. However, our current mechanistic understanding of vesicle-host cell interactions is limited by a lack of methods to study the rapid kinetics of vesicle entry and cargo delivery to host cells. Here, we describe a highly sensitive method to study the kinetics of vesicle entry into host cells in real-time using a genetically encoded, vesicle-targeted probe. We found that the route of vesicular uptake, and thus entry kinetics and efficiency, are shaped by bacterial cell wall composition. The presence of lipopolysaccharide O antigen enables vesicles to bypass clathrin-mediated endocytosis, which enhances both their entry rate and efficiency into host cells. Collectively, our findings highlight the composition of the bacterial cell wall as a major determinant of secretion-independent delivery of virulence factors during Gram-negative infections. [Mh] Termos MeSH primário: Bactérias Gram-Negativas/metabolismo Infecções por Bactérias Gram-Negativas/microbiologia Lipopolissacarídeos/metabolismo Vesículas Transportadoras/microbiologia [Mh] Termos MeSH secundário: Parede Celular/química Parede Celular/metabolismo Endocitose Bactérias Gram-Negativas/química Infecções por Bactérias Gram-Negativas/metabolismo Interações Hospedeiro-Patógeno Seres Humanos Cinética Lipopolissacarídeos/química Vesículas Transportadoras/metabolismo Fatores de Virulência/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Lipopolysaccharides); 0 (Virulence Factors) [Em] Mês de entrada: 1801 [Cu] Atualização por classe: 180109 [Lr] Data última revisão: 180109 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 171130 [St] Status: MEDLINE [do] DOI: 10.1371/journal.ppat.1006760

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[PMID]: 29049733 [Au] Autor: Keller KE; Bradley JM; Sun YY; Yang YF; Acott TS [Ad] Endereço: Casey Eye Institute, Oregon Health & Science University, Portland, Oregon, United States. [Ti] Título: Tunneling Nanotubes are Novel Cellular Structures That Communicate Signals Between Trabecular Meshwork Cells. [So] Source: Invest Ophthalmol Vis Sci;58(12):5298-5307, 2017 Oct 01. [Is] ISSN: 1552-5783 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Purpose: The actin cytoskeleton of trabecular meshwork (TM) cells plays a role in regulating aqueous humor outflow. Many studies have investigated stress fibers, but F-actin also assembles into other supramolecular structures including filopodia. Recently, specialized filopodia called tunneling nanotubes (TNTs) have been described, which communicate molecular signals and organelles directly between cells. Here, we investigate TNT formation by TM cells. Methods: Human TM cells were labeled separately with the fluorescent dyes, DiO and DiD, or with mitochondrial dye. Fixed or live TM cells were imaged using confocal microscopy. Image analysis software was used to track fluorescent vesicles and count the number and length of filopodia. The number of fluorescently labeled vesicles transferred between cells was counted in response to specific inhibitors of the actin cytoskeleton. Human TM tissue was stained with phalloidin. Results: Live-cell confocal imaging of cultured TM cells showed transfer of fluorescently labeled vesicles and mitochondria via TNTs. In TM tissue, a long (160 µm) actin-rich cell process bridged an intertrabecular space and did not adhere to the substratum. Treatment of TM cells with CK-666, an Arp2/3 inhibitor, significantly decreased the number and length of filopodia, decreased transfer of fluorescently labeled vesicles and induced thick stress fibers compared to vehicle control. Conversely, inhibiting stress fibers using Y27632 increased transfer of vesicles and induced long cell processes. Conclusions: Identification of TNTs provides a means by which TM cells can directly communicate with each other over long distances. This may be particularly important to overcome limitations of diffusion-based signaling in the aqueous humor fluid environment. [Mh] Termos MeSH primário: Comunicação Celular/fisiologia Nanotubos Pseudópodes/fisiologia Transdução de Sinais/fisiologia Malha Trabecular/citologia Vesículas Transportadoras/fisiologia [Mh] Termos MeSH secundário: Complexo 2-3 de Proteínas Relacionadas à Actina/antagonistas & inibidores Actinas/antagonistas & inibidores Actinas/metabolismo Adolescente Adulto Amidas/farmacologia Criança Pré-Escolar Inibidores Enzimáticos/farmacologia Corantes Fluorescentes/metabolismo Seres Humanos Indóis/farmacologia Microscopia Confocal Meia-Idade Piridinas/farmacologia Coloração e Rotulagem Malha Trabecular/fisiologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actin-Related Protein 2-3 Complex); 0 (Actins); 0 (Amides); 0 (CK-0944666); 0 (Enzyme Inhibitors); 0 (Fluorescent Dyes); 0 (Indoles); 0 (Pyridines); 138381-45-0 (Y 27632) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171029 [Lr] Data última revisão: 171029 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 171020 [St] Status: MEDLINE [do] DOI: 10.1167/iovs.17-22732

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[PMID]: 28910396 [Au] Autor: Merrill NM; Schipper JL; Karnes JB; Kauffman AL; Martin KR; MacKeigan JP [Ad] Endereço: Van Andel Institute Graduate School, Grand Rapids, Michigan, United States of America. [Ti] Título: PI3K-C2α knockdown decreases autophagy and maturation of endocytic vesicles. [So] Source: PLoS One;12(9):e0184909, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Phosphoinositide 3-kinase (PI3K) family members are involved in diverse cellular fates including cell growth, proliferation, and survival. While many molecular details are known about the Class I and III PI3Ks, less is known about the Class II PI3Ks. To explore the function of all eight PI3K isoforms in autophagy, we knock down each gene individually and measure autophagy. We find a significant decrease in autophagy following siRNA-mediated PIK3C2A (encoding the Class 2 PI3K, PI3K-C2α) knockdown. This defective autophagy is rescued by exogenous PI3K-C2α, but not kinase-dead PI3K-C2α. Using confocal microscopy, we probe for markers of endocytosis and autophagy, revealing that PI3K-C2α colocalizes with markers of endocytosis. Though endocytic uptake is intact, as demonstrated by transferrin labeling, PIK3C2A knockdown results in vesicle accumulation at the recycling endosome. We isolate distinct membrane sources and observe that PI3K-C2α interacts with markers of endocytosis and autophagy, notably ATG9. Knockdown of either PIK3C2A or ATG9A/B, but not PI3KC3, results in an accumulation of transferrin-positive clathrin coated vesicles and RAB11-positive vesicles at the recycling endosome. Taken together, these results support a role for PI3K-C2α in the proper maturation of endosomes, and suggest that PI3K-C2α may be a critical node connecting the endocytic and autophagic pathways. [Mh] Termos MeSH primário: Biomarcadores/metabolismo Endossomos/metabolismo Fosfatidilinositol 3-Quinases/genética Vesículas Transportadoras/metabolismo [Mh] Termos MeSH secundário: Autofagia Linhagem Celular Proliferação Celular Endocitose Técnicas de Silenciamento de Genes Seres Humanos Fosfatidilinositol 3-Quinases/metabolismo RNA Interferente Pequeno/metabolismo Transdução de Sinais [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Biomarkers); 0 (RNA, Small Interfering); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.1.137 (PIK3C2A protein, human) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171012 [Lr] Data última revisão: 171012 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170915 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0184909

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[PMID]: 28683137 [Au] Autor: Shukla A; Bhattacharyya A; Kuppusamy L; Srivas M; Thattai M [Ad] Endereço: School of Computer Science and Engineering, Vellore Institute of Technology, Vellore, India. [Ti] Título: Discovering vesicle traffic network constraints by model checking. [So] Source: PLoS One;12(7):e0180692, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: A eukaryotic cell contains multiple membrane-bound compartments. Transport vesicles move cargo between these compartments, just as trucks move cargo between warehouses. These processes are regulated by specific molecular interactions, as summarized in the Rothman-Schekman-Sudhof model of vesicle traffic. The whole structure can be represented as a transport graph: each organelle is a node, and each vesicle route is a directed edge. What constraints must such a graph satisfy, if it is to represent a biologically realizable vesicle traffic network? Graph connectedness is an informative feature: 2-connectedness is necessary and sufficient for mass balance, but stronger conditions are required to ensure correct molecular specificity. Here we use Boolean satisfiability (SAT) and model checking as a framework to discover and verify graph constraints. The poor scalability of SAT model checkers often prevents their broad application. By exploiting the special structure of the problem, we scale our model checker to vesicle traffic systems with reasonably large numbers of molecules and compartments. This allows us to test a range of hypotheses about graph connectivity, which can later be proved in full generality by other methods. [Mh] Termos MeSH primário: Compartimento Celular Modelos Biológicos Vesículas Transportadoras/metabolismo [Mh] Termos MeSH secundário: Transporte Biológico Proteínas SNARE/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (SNARE Proteins) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171006 [Lr] Data última revisão: 171006 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170707 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0180692

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[PMID]: 28666116 [Au] Autor: Mandadapu KK; Hurley JH [Ad] Endereço: Department of Chemical and Biomolecular Engineering, University of California, Berkeley, Berkeley, CA 94720, USA; Chemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: kranthi@berkeley.edu. [Ti] Título: Friction at the BAR Leads to Membrane Breakup. [So] Source: Cell;170(1):14-16, 2017 06 29. [Is] ISSN: 1097-4172 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: A long-standing question in cell biology is how endocytic vesicles and tubules detach from the plasma membrane in the absence of constriction by dynamin. In this issue of Cell, Simunovic et al. describe an elegant biophysical model in which friction between lipids and BAR-domain proteins drives the scission of elongating membrane tubules. [Mh] Termos MeSH primário: Endocitose Fricção [Mh] Termos MeSH secundário: Membrana Celular Dinaminas Vesículas Transportadoras [Pt] Tipo de publicação: JOURNAL ARTICLE; COMMENT [Nm] Nome de substância: EC 3.6.5.5 (Dynamins) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170920 [Lr] Data última revisão: 170920 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170701 [St] Status: MEDLINE

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[PMID]: 28527761 [Au] Autor: Volgers C; Benedikter BJ; Grauls GE; Savelkoul PHM; Stassen FRM [Ad] Endereço: School of Nutrition and Translational Research in Metabolism (NUTRIM), Department of Medical Microbiology, Maastricht University Medical Center+, Maastricht, The Netherlands. [Ti] Título: Bead-based flow-cytometry for semi-quantitative analysis of complex membrane vesicle populations released by bacteria and host cells. [So] Source: Microbiol Res;200:25-32, 2017 Jul. [Is] ISSN: 1618-0623 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: During infection, the release of nano-sized membrane vesicle is a process which is common both for bacteria and host cells. Host cell-derived membrane vesicles can be involved in innate and adaptive immunity whereas bacterial membrane vesicles can contribute to bacterial pathogenicity. To study the contribution of both membrane vesicle populations during infection is highly complicated as most vesicles fall within a similar size range of 30-300nm. Specialized techniques for purification are required and often no single technique complies on its own. Moreover, techniques for vesicle quantification are either complicated to use or do not distinguish between host cell-derived and bacterial membrane vesicle subpopulations. Here we demonstrate a bead-based platform that allows a semi-quantitatively analysis by flow-cytometry of bacterial and host-cell derived membrane vesicles. We show this method can be used to study heterogeneous and complex vesicle populations composed of bacterial and host-cell membrane vesicles. The easy accessible design of the protocol makes it also highly suitable for screening procedures to assess how intrinsic and environmental factors affect vesicle release. [Mh] Termos MeSH primário: Bactérias/citologia Linhagem Celular/citologia Citometria de Fluxo/métodos Vesículas Transportadoras/química [Mh] Termos MeSH secundário: Anticorpos Linhagem Celular/microbiologia Membrana Celular Contagem de Colônia Microbiana Epitopos Seres Humanos Macrófagos/citologia Macrófagos/imunologia Macrófagos/microbiologia Moraxella (Branhamella) catarrhalis/classificação Pseudomonas aeruginosa/citologia Vesículas Transportadoras/imunologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antibodies); 0 (Epitopes) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170925 [Lr] Data última revisão: 170925 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170522 [St] Status: MEDLINE

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[PMID]: 28442535 [Au] Autor: Yamada M; Tanaka-Takiguchi Y; Hayashi M; Nishina M; Goshima G [Ad] Endereço: Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan. [Ti] Título: Multiple kinesin-14 family members drive microtubule minus end-directed transport in plant cells. [So] Source: J Cell Biol;216(6):1705-1714, 2017 Jun 05. [Is] ISSN: 1540-8140 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Minus end-directed cargo transport along microtubules (MTs) is exclusively driven by the molecular motor dynein in a wide variety of cell types. Interestingly, during evolution, plants have lost the genes encoding dynein; the MT motors that compensate for dynein function are unknown. Here, we show that two members of the kinesin-14 family drive minus end-directed transport in plants. Gene knockout analyses of the moss revealed that the plant-specific class VI kinesin-14, KCBP, is required for minus end-directed transport of the nucleus and chloroplasts. Purified KCBP directly bound to acidic phospholipids and unidirectionally transported phospholipid liposomes along MTs in vitro. Thus, minus end-directed transport of membranous cargoes might be driven by their direct interaction with this motor protein. Newly nucleated cytoplasmic MTs represent another known cargo exhibiting minus end-directed motility, and we identified the conserved class I kinesin-14 (ATK) as the motor involved. These results suggest that kinesin-14 motors were duplicated and developed as alternative MT-based minus end-directed transporters in land plants. [Mh] Termos MeSH primário: Bryopsida/metabolismo Cinesina/metabolismo Microtúbulos/metabolismo Proteínas Motores Moleculares/metabolismo Células Vegetais/metabolismo Proteínas de Plantas/metabolismo Plantas Geneticamente Modificadas/metabolismo [Mh] Termos MeSH secundário: Bryopsida/citologia Bryopsida/genética Núcleo Celular/metabolismo Cloroplastos/metabolismo Cinesina/genética Microscopia de Vídeo Proteínas Motores Moleculares/genética Fosfolipídeos/metabolismo Proteínas de Plantas/genética Plantas Geneticamente Modificadas/citologia Plantas Geneticamente Modificadas/genética Transporte Proteico Transdução de Sinais Fatores de Tempo Vesículas Transportadoras/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; VIDEO-AUDIO MEDIA [Nm] Nome de substância: 0 (Molecular Motor Proteins); 0 (Phospholipids); 0 (Plant Proteins); EC 3.6.4.4 (Kinesin) [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: 170427 [St] Status: MEDLINE [do] DOI: 10.1083/jcb.201610065

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[PMID]: 28422978 [Au] Autor: Haag C; Pohlmann T; Feldbrügge M [Ad] Endereço: Heinrich Heine University Düsseldorf, Institute for Microbiology, Cluster of Excellence on Plant Sciences, Düsseldorf, Germany. [Ti] Título: The ESCRT regulator Did2 maintains the balance between long-distance endosomal transport and endocytic trafficking. [So] Source: PLoS Genet;13(4):e1006734, 2017 Apr. [Is] ISSN: 1553-7404 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: In highly polarised cells, like fungal hyphae, early endosomes function in both endocytosis as well as long-distance transport of various cargo including mRNA and protein complexes. However, knowledge on the crosstalk between these seemingly different trafficking processes is scarce. Here, we demonstrate that the ESCRT regulator Did2 coordinates endosomal transport in fungal hyphae of Ustilago maydis. Loss of Did2 results in defective vacuolar targeting, less processive long-distance transport and abnormal shuttling of early endosomes. Importantly, the late endosomal protein Rab7 and vacuolar protease Prc1 exhibit increased shuttling on these aberrant endosomes suggesting defects in endosomal maturation and identity. Consistently, molecular motors fail to attach efficiently explaining the disturbed processive movement. Furthermore, the endosomal mRNP linker protein Upa1 is hardly present on endosomes resulting in defects in long-distance mRNA transport. In conclusion, the ESCRT regulator Did2 coordinates precise maturation of endosomes and thus provides the correct membrane identity for efficient endosomal long-distance transport. [Mh] Termos MeSH primário: Complexos Endossomais de Distribuição Requeridos para Transporte/genética Endossomos/genética Transporte Proteico/genética Transporte de RNA/genética Proteínas de Saccharomyces cerevisiae/genética Ustilago/genética [Mh] Termos MeSH secundário: Catepsina A/genética Polaridade Celular/genética Endocitose/genética Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo Endossomos/metabolismo Hifas/genética Hifas/crescimento & desenvolvimento Hifas/metabolismo RNA Mensageiro/metabolismo Saccharomyces cerevisiae/genética Saccharomyces cerevisiae/crescimento & desenvolvimento Proteínas de Saccharomyces cerevisiae/metabolismo Vesículas Transportadoras/genética Vesículas Transportadoras/metabolismo Ustilago/crescimento & desenvolvimento Proteínas rab de Ligação ao GTP/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (DID2 protein, S cerevisiae); 0 (Endosomal Sorting Complexes Required for Transport); 0 (RNA, Messenger); 0 (Saccharomyces cerevisiae Proteins); 152989-05-4 (rab7 protein); EC 3.4.16.5 (Cathepsin A); EC 3.4.16.5 (PRC1 protein, S cerevisiae); EC 3.6.5.2 (rab GTP-Binding Proteins) [Em] Mês de entrada: 1706 [Cu] Atualização por classe: 170601 [Lr] Data última revisão: 170601 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170420 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pgen.1006734

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[PMID]: 28404745 [Au] Autor: Dalton LE; Bean BDM; Davey M; Conibear E [Ad] Endereço: Centre for Molecular Medicine and Therapeutics, BC Children's Hospital, University of British Columbia, Vancouver, BC V5Z 4H4, Canada. [Ti] Título: Quantitative high-content imaging identifies novel regulators of Neo1 trafficking at endosomes. [So] Source: Mol Biol Cell;28(11):1539-1550, 2017 Jun 01. [Is] ISSN: 1939-4586 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: P4-ATPases are a family of putative phospholipid flippases that regulate lipid membrane asymmetry, which is important for vesicle formation. Two yeast flippases, Drs2 and Neo1, have nonredundant functions in the recycling of the synaptobrevin-like v-SNARE Snc1 from early endosomes. Drs2 activity is needed to form vesicles and regulate its own trafficking, suggesting that flippase activity and localization are linked. However, the role of Neo1 in endosomal recycling is not well characterized. To identify novel regulators of Neo1 trafficking and activity at endosomes, we first identified mutants with impaired recycling of a Snc1-based reporter and subsequently used high-content microscopy to classify these mutants based on the localization of Neo1 or its binding partners, Mon2 and Dop1. This analysis identified a role for Arl1 in stabilizing the Mon2/Dop1 complex and uncovered a new function for Vps13 in early endosome recycling and Neo1 localization. We further showed that the cargo-selective sorting nexin Snx3 is required for Neo1 trafficking and identified an Snx3 sorting motif in the Neo1 N-terminus. Of importance, the Snx3-dependent sorting of Neo1 was required for the correct sorting of another Snx3 cargo protein, suggesting that the incorporation of Neo1 into recycling tubules may influence their formation. [Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo Proteínas de Transporte/metabolismo Endossomos/metabolismo Proteínas de Membrana Transportadoras/metabolismo Proteínas de Transferência de Fosfolipídeos/metabolismo Proteínas de Saccharomyces cerevisiae/metabolismo [Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética Proteínas de Membrana Transportadoras/genética Proteínas de Transferência de Fosfolipídeos/genética Transporte Proteico/fisiologia Proteínas SNARE/metabolismo Saccharomyces cerevisiae/metabolismo Proteínas de Saccharomyces cerevisiae/genética Nexinas de Classificação/metabolismo Vesículas Transportadoras/metabolismo Proteínas de Transporte Vesicular/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Carrier Proteins); 0 (Membrane Transport Proteins); 0 (Phospholipid Transfer Proteins); 0 (SNARE Proteins); 0 (SNX3 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Sorting Nexins); 0 (Vesicular Transport Proteins); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.3.1 (NEO1 protein, S cerevisiae) [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: 170414 [St] Status: MEDLINE [do] DOI: 10.1091/mbc.E16-11-0772

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