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Pesquisa : D08.811.277.040.330 [Categoria DeCS]
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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


  2 / 7939 MEDLINE  
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[PMID]:28453723
[Au] Autor:Blanca Ramírez M; Lara Ordóñez AJ; Fdez E; Madero-Pérez J; Gonnelli A; Drouyer M; Chartier-Harlin MC; Taymans JM; Bubacco L; Greggio E; Hilfiker S
[Ad] Endereço:Institute of Parasitology and Biomedicine 'López-Neyra', Consejo Superior de Investigaciones Científicas (CSIC), 18016 Granada, Spain.
[Ti] Título:GTP binding regulates cellular localization of Parkinson's disease-associated LRRK2.
[So] Source:Hum Mol Genet;26(14):2747-2767, 2017 07 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations in leucine-rich repeat kinase 2 (LRRK2) comprise the most common cause of familial Parkinson's disease (PD), and sequence variants modify risk for sporadic PD. Previous studies indicate that LRRK2 interacts with microtubules (MTs) and alters MT-mediated vesicular transport processes. However, the molecular determinants within LRRK2 required for such interactions have remained unknown. Here, we report that most pathogenic LRRK2 mutants cause relocalization of LRRK2 to filamentous structures which colocalize with a subset of MTs, and an identical relocalization is seen upon pharmacological LRRK2 kinase inhibition. The pronounced colocalization with MTs does not correlate with alterations in LRRK2 kinase activity, but rather with increased GTP binding. Synthetic mutations which impair GTP binding, as well as LRRK2 GTP-binding inhibitors profoundly interfere with the abnormal localization of both pathogenic mutant as well as kinase-inhibited LRRK2. Conversely, addition of a non-hydrolyzable GTP analog to permeabilized cells enhances the association of pathogenic or kinase-inhibited LRRK2 with MTs. Our data elucidate the mechanism underlying the increased MT association of select pathogenic LRRK2 mutants or of pharmacologically kinase-inhibited LRRK2, with implications for downstream MT-mediated transport events.
[Mh] Termos MeSH primário: Guanosina Trifosfato/metabolismo
Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina/metabolismo
Doença de Parkinson/metabolismo
[Mh] Termos MeSH secundário: GTP Fosfo-Hidrolases/metabolismo
Proteínas de Ligação ao GTP/genética
Proteínas de Ligação ao GTP/metabolismo
Variação Genética
Guanosina Trifosfato/genética
Células HEK293
Seres Humanos
Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina/antagonistas & inibidores
Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina/genética
Microtúbulos/genética
Microtúbulos/metabolismo
Mutação
Doença de Parkinson/genética
Fosforilação
Inibidores de Proteínas Quinases/farmacologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Kinase Inhibitors); 86-01-1 (Guanosine Triphosphate); EC 2.7.11.1 (LRRK2 protein, human); EC 2.7.11.1 (Leucine-Rich Repeat Serine-Threonine Protein Kinase-2); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (GTP-Binding Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180225
[Lr] Data última revisão:
180225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx161


  3 / 7939 MEDLINE  
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[PMID]:29413990
[Au] Autor:Kelly J; Murphy JE
[Ad] Endereço:Mitochondrial Biology & Radiation Research Centre, Dept. of Life Sciences, Institute of Technology Sligo, Ash Lane, Sligo, Ireland. Electronic address: janiskelly@mail.itsligo.ie.
[Ti] Título:Mitochondrial gene expression changes in cultured human skin cells following simulated sunlight irradiation.
[So] Source:J Photochem Photobiol B;179:167-174, 2018 Feb.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Exposure of skin to simulated sunlight irradiation (SSI) has being extensively researched and shown to be the main cause for changes in the skin including changes in cellular function and generation of reactive oxygen species (ROS). This oxidative stress can subsequently exert downstream effects and the subcellular compartments most affected by this oxidative stress are mitochondria. The importance of functional mitochondrial morphology is apparent as morphological defects are related to many human diseases including diabetes mellitus, liver disease, neurodegenerative diseases, aging and cancer. OBJECTIVE: The main objective of this study was to evaluate solar radiation-induced changes in mitochondrial gene expression in human skin cells using a Q-Sun solar simulator to deliver a close match to the intensity of summer sunlight. METHODS: Spontaneously immortalised human skin epidermal keratinocytes (HaCaT) and Human Dermal Fibroblasts (HDFn) were divided into two groups. Group A were irradiated once and Group B twice 7days apart; following irradiation, mitochondrial gene expression was evaluated 1, 4 and 7days post primary exposure for group A and 1, 4, 7 and 14days post-secondary exposure for group B. RESULTS: Both the epidermal and dermal cells displayed significant reduced expression of the genes analysed for mitochondrial morphology and function; however, epidermal cells displayed this reduction post SSI earlier then dermal cells at multiple time points. CONCLUSION: The data presented here reinforces the fact that epidermal cells, while displaying a heightened sensitivity to sunlight, are less prone to changes in gene expression, while dermal cells, which appear to be more resilient are possibly more prone to genomic instability and mitochondrial damage.
[Mh] Termos MeSH primário: Expressão Gênica/efeitos da radiação
Mitocôndrias/genética
Luz Solar
[Mh] Termos MeSH secundário: ATPases Associadas a Diversas Atividades Celulares/genética
ATPases Associadas a Diversas Atividades Celulares/metabolismo
Linhagem Celular
Derme/citologia
Epiderme/citologia
GTP Fosfo-Hidrolases/genética
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Queratinócitos/citologia
Queratinócitos/metabolismo
Queratinócitos/efeitos da radiação
Metaloendopeptidases/genética
Metaloendopeptidases/metabolismo
Mitocôndrias/efeitos da radiação
Proteínas de Transporte da Membrana Mitocondrial/genética
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Superóxido Dismutase/genética
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Membrane Transport Proteins); 0 (Mitochondrial Proteins); 0 (Reactive Oxygen Species); EC 1.15.1.1 (Superoxide Dismutase); EC 1.15.1.1 (superoxide dismutase 2); EC 3.4.24.- (Metalloendopeptidases); EC 3.4.24.- (YME1L1 protein, human); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (MFN2 protein, human); EC 3.6.1.- (OPA1 protein, human); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities); EC 3.6.5.- (Mfn1 protein, human)
[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:180208
[St] Status:MEDLINE


  4 / 7939 MEDLINE  
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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]:29241732
[Au] Autor:Park YS; Choi SE; Koh HC
[Ad] Endereço:Department of Pharmacology, College of Medicine, Hanyang University, Seoul, Republic of Korea; Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul, Republic of Korea.
[Ti] Título:PGAM5 regulates PINK1/Parkin-mediated mitophagy via DRP1 in CCCP-induced mitochondrial dysfunction.
[So] Source:Toxicol Lett;284:120-128, 2018 Mar 01.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mitochondrial dynamics and mitophagy are critical processes for regulating mitochondrial homeostasis. Phosphoglycerate mutase family member 5 (PGAM5) is a mitochondrial protein that plays crucial roles in apoptosis and necroptosis, but the roles of PGAM5 in mitochondrial dynamics and mitophagy remain unclear. In this study, we investigated the role of PGAM5 in carbonyl cyanide m-chlorophenylhydrazone (CCCP)-induced mitochondrial damage and the correlation between mitochondrial dynamics and mitophagy using SH-SY5Y cells. We found that CCCP decreased mitochondrial membrane potential, resulting in mitochondrial dysfunction. CCCP increased PGAM5, dynamin-related protein 1 (DRP1), and optic atrophy 1 (OPA1) expression of the mitochondrial fraction in a time-dependent manner. Knockdown of PGAM5 inhibited DRP1 translocation without a change in OPA1 expression in CCCP-treated cells. Furthermore, knockdown of PGAM5 and DRP1 significantly blocked the increase of PTEN-induced putative protein kinase 1 (PINK1) and Parkin expression in the mitochondrial fraction of CCCP-treated cells. Interestingly, CCCP did not alter PINK1/Parkin expression in the mitochondrial fraction of OPA1 knockdown cells. Inhibiting mitophagy by PGAM5 knockdown accelerated CCCP-induced apoptosis. CCCP treatment also results in PINK1 stabilization on the mitochondrial membrane, which subsequently increases Parkin recruitment from the cytosol to abnormal mitochondria. In addition, we found that CCCP increased the level of mitochondrial LC3II, indicating that Parkin recruitment of PINK1 is a result of mitophagy. We propose that activation of PGAM5 is associated with DRP1 recruitment and PINK1 stabilization, which contribute to the modulation of mitophagy in CCCP-treated cells with mitochondrial dysfunction. In conclusion, we demonstrated that PGAM5 regulates PINK1-Parkin-mediated mitophagy, which can exert a neuroprotective effect against CCCP-induced apoptosis.
[Mh] Termos MeSH primário: Carbonil Cianeto m-Clorofenil Hidrazona/toxicidade
GTP Fosfo-Hidrolases/metabolismo
Proteínas Associadas aos Microtúbulos/metabolismo
Degradação Mitocondrial/efeitos dos fármacos
Proteínas Mitocondriais/metabolismo
Fosfoproteínas Fosfatases/metabolismo
Proteínas Quinases/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
GTP Fosfo-Hidrolases/genética
Técnicas de Silenciamento de Genes
Seres Humanos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Proteínas Associadas aos Microtúbulos/genética
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Mitocôndrias/patologia
Proteínas Mitocondriais/genética
Fosfoproteínas Fosfatases/genética
Proteínas Quinases/genética
Ubiquitina-Proteína Ligases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Microtubule-Associated Proteins); 0 (Mitochondrial Proteins); 555-60-2 (Carbonyl Cyanide m-Chlorophenyl Hydrazone); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (parkin protein); EC 2.7.- (Protein Kinases); EC 2.7.11.1 (PTEN-induced putative kinase); EC 3.1.3.16 (PGAM5 protein, human); EC 3.1.3.16 (Phosphoprotein Phosphatases); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.5 (DNM1L protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE


  6 / 7939 MEDLINE  
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Quevedo, J
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[PMID]:28463235
[Au] Autor:Scaini G; Fries GR; Valvassori SS; Zeni CP; Zunta-Soares G; Berk M; Soares JC; Quevedo J
[Ad] Endereço:Translational Psychiatry Program, Department of Psychiatry and Behavioral Sciences, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX, USA.
[Ti] Título:Perturbations in the apoptotic pathway and mitochondrial network dynamics in peripheral blood mononuclear cells from bipolar disorder patients.
[So] Source:Transl Psychiatry;7(5):e1111, 2017 May 02.
[Is] ISSN:2158-3188
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bipolar disorder (BD) is a severe psychiatric disorder characterized by phasic changes of mood and can be associated with progressive structural brain change and cognitive decline. The numbers and sizes of glia and neurons are reduced in several brain areas, suggesting the involvement of apoptosis in the pathophysiology of BD. Because the changes in mitochondrial dynamics are closely related with the early process of apoptosis and the specific processes of apoptosis and mitochondrial dynamics in BD have not been fully elucidated, we measured the apoptotic pathway and the expression of mitochondrial fission/fusion proteins from BD patients and healthy controls. We recruited 16 patients with BD type I and sixteen well-matched healthy controls and investigated protein levels of several pro-apoptotic and anti-apoptotic factors, as well as the expression of mitochondrial fission/fusion proteins in peripheral blood mononuclear cells (PBMCs). Our results showed that the levels of the anti-apoptotic proteins Bcl-xL, survivin and Bcl-xL/Bak dimer were significantly decreased, while active caspase-3 protein levels were significantly increased in PBMCs from BD patients. Moreover, we observed the downregulation of the mitochondrial fusion-related proteins Mfn2 and Opa1 and the upregulation of the fission protein Fis1 in PBMCs from BD patients, both in terms of gene expression and protein levels. We also showed a significantly decrease in the citrate synthase activity. Finally, we found a positive correlation between Mfn2 and Opa1 with mitochondrial content markers, as well as a negative correlation between mitochondrial fission/fusion proteins and apoptotic markers. Overall, data reported here are consistent with the working hypothesis that apoptosis may contribute to cellular dysfunction, brain volume loss and progressive cognitive in BD. Moreover, we show an important relationship between mitochondrial dynamics and the cell death pathway activation in BD patients, supporting the link between mitochondrial dysfunction and the pathophysiology of BD.
[Mh] Termos MeSH primário: Apoptose/genética
Transtorno Bipolar/metabolismo
Leucócitos Mononucleares/metabolismo
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Adulto
Proteínas Reguladoras de Apoptose/genética
Transtorno Bipolar/sangue
Transtorno Bipolar/fisiopatologia
Caspase 3/metabolismo
Morte Celular
Feminino
GTP Fosfo-Hidrolases/genética
Expressão Gênica/genética
Seres Humanos
Proteínas Inibidoras de Apoptose/metabolismo
Masculino
Proteínas de Membrana/genética
Dinâmica Mitocondrial/genética
Proteínas Mitocondriais/genética
Neurônios/metabolismo
Regulação para Cima/genética
Proteína bcl-X/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoptosis Regulatory Proteins); 0 (BIRC5 protein, human); 0 (FIS1 protein, human); 0 (Inhibitor of Apoptosis Proteins); 0 (Membrane Proteins); 0 (Mitochondrial Proteins); 0 (bcl-X Protein); EC 3.4.22.- (CASP3 protein, human); EC 3.4.22.- (Caspase 3); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (MFN2 protein, human); EC 3.6.1.- (OPA1 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1038/tp.2017.83


  7 / 7939 MEDLINE  
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[PMID]:29247648
[Au] Autor:Deng B; Zhu X; Zhao Y; Zhang D; Pannu A; Chen L; Niu W
[Ad] Endereço:Department of Immunology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Key Laboratory of Hormones and Development (Ministry of Health), Tianjin Metabolic Diseases Hospital, Tianjin Medical University, Tianjin, 300070, China.
[Ti] Título:PKC and Rab13 mediate Ca signal-regulated GLUT4 traffic.
[So] Source:Biochem Biophys Res Commun;495(2):1956-1963, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Exercise/muscle contraction increases cell surface glucose transporter 4 (GLUT4), leading to glucose uptake to regulate blood glucose level. Elevating cytosolic Ca mediates this effect, but the detailed mechanism is not clear yet. We used calcium ionophore ionomycin to raise intracellular cytosolic Ca level to explore the underlying mechanism. We showed that in L6 myoblast muscle cells stably expressing GLUT4myc, ionomycin increased cell surface GLUT4myc levels and the phosphorylation of AS160, TBC1D1. siPKCα and siPKCθ but not siPKCδ and siPKCε inhibited the ionomycin-increased cell surface GLUT4myc level. siPKCα, siPKCθ inhibited the phosphorylation of AS160 and TBC1D1 induced by ionomycin. siPKCα and siPKCθ prevented ionomycin-inhibited endocytosis of GLUT4myc. siPKCθ, but not siPKCα inhibited ionomycin-stimulated exocytosis of GLUT4myc. siRab13 but not siRab8a, siRab10 and siRab14 inhibited the exocytosis of GLUT4myc promoted by ionomycin. In summary, ionomycin-promoted exocytosis of GLUT4 is partly reversed by siPKCθ, whereas ionomycin-inhibited endocytosis of GLUT4 requires both siPKCα and siPKCθ. PKCα and PKCθ contribute to ionomycin-induced phosphorylation of AS160 and TBC1D1. Rab13 is required for ionomycin-regulated GLUT4 exocytosis.
[Mh] Termos MeSH primário: Sinalização do Cálcio/fisiologia
Endocitose/fisiologia
Exocitose/fisiologia
GTP Fosfo-Hidrolases/metabolismo
Transportador de Glucose Tipo 4/metabolismo
Mioblastos/fisiologia
Proteína Quinase C/metabolismo
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Ionóforos de Cálcio/administração & dosagem
Sinalização do Cálcio/efeitos dos fármacos
Linhagem Celular
Endocitose/efeitos dos fármacos
Exocitose/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Regulação da Expressão Gênica/fisiologia
Ionomicina/administração & dosagem
Mioblastos/efeitos dos fármacos
Transporte Proteico/fisiologia
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Ionophores); 0 (Glucose Transporter Type 4); 0 (Slc2a4 protein, rat); 56092-81-0 (Ionomycin); EC 2.7.11.13 (Protein Kinase C); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (Rab13 protein, rat); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE


  8 / 7939 MEDLINE  
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[PMID]:28463110
[Au] Autor:Gong B; Shen W; Xiao W; Meng Y; Meng A; Jia S
[Ad] Endereço:State Key Laboratory of Membrane Biology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.
[Ti] Título:The Sec14-like phosphatidylinositol transfer proteins Sec14l3/SEC14L2 act as GTPase proteins to mediate Wnt/Ca signaling.
[So] Source:Elife;6, 2017 05 02.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The non-canonical Wnt/Ca signaling pathway plays important roles in embryonic development, tissue formation and diseases. However, it is unclear how the Wnt ligand-stimulated, G protein-coupled receptor Frizzled activates phospholipases for calcium release. Here, we report that the zebrafish/human phosphatidylinositol transfer protein Sec14l3/SEC14L2 act as GTPase proteins to transduce Wnt signals from Frizzled to phospholipase C (PLC). Depletion of attenuates Wnt/Ca responsive activity and causes convergent and extension (CE) defects in zebrafish embryos. Biochemical analyses in mammalian cells indicate that Sec14l3-GDP forms complex with Frizzled and Dishevelled; Wnt ligand binding of Frizzled induces translocation of Sec14l3 to the plasma membrane; and then Sec14l3-GTP binds to and activates phospholipase Cδ4a (Plcδ4a); subsequently, Plcδ4a initiates phosphatidylinositol-4,5-bisphosphate (PIP ) signaling, ultimately stimulating calcium release. Furthermore, Plcδ4a can act as a GTPase-activating protein to accelerate the hydrolysis of Sec14l3-bound GTP to GDP. Our data provide a new insight into GTPase protein-coupled Wnt/Ca signaling transduction.
[Mh] Termos MeSH primário: Sinalização do Cálcio
Proteínas de Transporte/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Lipoproteínas/metabolismo
Proteínas de Transferência de Fosfolipídeos/metabolismo
Transativadores/metabolismo
Via de Sinalização Wnt
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Receptores Frizzled/metabolismo
Seres Humanos
Fosfolipases Tipo C/metabolismo
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Frizzled Receptors); 0 (Lipoproteins); 0 (Phospholipid Transfer Proteins); 0 (SEC14L2 protein, human); 0 (SEC14L3 protein, human); 0 (Trans-Activators); EC 3.1.4.- (Type C Phospholipases); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180211
[Lr] Data última revisão:
180211
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


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[PMID]:28471452
[Au] Autor:Chowdhury SR; Ray U; Chatterjee BP; Roy SS
[Ad] Endereço:Cell Biology and Physiology Division, CSIR-Indian Institute of Chemical Biology, Council of Scientific and Industrial Research, Kolkata, India.
[Ti] Título:Targeted apoptosis in ovarian cancer cells through mitochondrial dysfunction in response to Sambucus nigra agglutinin.
[So] Source:Cell Death Dis;8(5):e2762, 2017 May 04.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ovarian carcinoma (OC) patients encounter the severe challenge of clinical management owing to lack of screening measures, chemoresistance and finally dearth of non-toxic therapeutics. Cancer cells deploy various defense strategies to sustain the tumor microenvironment, among which deregulated apoptosis remains a versatile promoter of cancer progression. Although recent research has focused on identifying agents capable of inducing apoptosis in cancer cells, yet molecules efficiently breaching their survival advantage are yet to be classified. Here we identify lectin, Sambucus nigra agglutinin (SNA) to exhibit selectivity towards identifying OC by virtue of its specific recognition of α-2, 6-linked sialic acids. Superficial binding of SNA to the OC cells confirm the hyper-sialylated status of the disease. Further, SNA activates the signaling pathways of AKT and ERK1/2, which eventually promotes de-phosphorylation of dynamin-related protein-1 (Drp-1). Upon its translocation to the mitochondrial fission loci Drp-1 mediates the central role of switch in the mitochondrial phenotype to attain fragmented morphology. We confirmed mitochondrial outer membrane permeabilization resulting in ROS generation and cytochrome-c release into the cytosol. SNA response resulted in an allied shift of the bioenergetics profile from Warburg phenotype to elevated mitochondrial oxidative phosphorylation, altogether highlighting the involvement of mitochondrial dysfunction in restraining cancer progression. Inability to replenish the SNA-induced energy crunch of the proliferating cancer cells on the event of perturbed respiratory outcome resulted in cell cycle arrest before G2/M phase. Our findings position SNA at a crucial juncture where it proves to be a promising candidate for impeding progression of OC. Altogether we unveil the novel aspect of identifying natural molecules harboring the inherent capability of targeting mitochondrial structural dynamics, to hold the future for developing non-toxic therapeutics for treating OC.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Mitocôndrias/metabolismo
Dinâmica Mitocondrial/efeitos dos fármacos
Lectinas de Plantas/farmacologia
Proteínas Inativadoras de Ribossomos/farmacologia
[Mh] Termos MeSH secundário: Sobrevivência Celular/efeitos dos fármacos
Citocromos c/metabolismo
Citosol/metabolismo
Feminino
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Microscopia Confocal
Proteínas Associadas aos Microtúbulos/metabolismo
Proteínas Mitocondriais/metabolismo
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
Neoplasias Ovarianas/metabolismo
Neoplasias Ovarianas/patologia
Proteínas Proto-Oncogênicas c-akt/antagonistas & inibidores
Proteínas Proto-Oncogênicas c-akt/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Pontos de Checagem da Fase S do Ciclo Celular/efeitos dos fármacos
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Microtubule-Associated Proteins); 0 (Mitochondrial Proteins); 0 (Plant Lectins); 0 (Reactive Oxygen Species); 0 (Sambucus nigra lectins); 9007-43-6 (Cytochromes c); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 3.2.2.22 (Ribosome Inactivating Proteins); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.5 (DNM1L protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2017.77


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[PMID]:28465429
[Au] Autor:Wesolowski J; Weber MM; Nawrotek A; Dooley CA; Calderon M; St Croix CM; Hackstadt T; Cherfils J; Paumet F
[Ad] Endereço:Department of Microbiology and Immunology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.
[Ti] Título: Hijacks ARF GTPases To Coordinate Microtubule Posttranslational Modifications and Golgi Complex Positioning.
[So] Source:MBio;8(3), 2017 May 02.
[Is] ISSN:2150-7511
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The intracellular bacterium develops in a parasitic compartment called the inclusion. Posttranslationally modified microtubules encase the inclusion, controlling the positioning of Golgi complex fragments around the inclusion. The molecular mechanisms by which coopts the host cytoskeleton and the Golgi complex to sustain its infectious compartment are unknown. Here, using a genetically modified strain, we discovered that both posttranslationally modified microtubules and Golgi complex positioning around the inclusion are controlled by the chlamydial inclusion protein CT813/CTL0184/InaC and host ARF GTPases. CT813 recruits ARF1 and ARF4 to the inclusion membrane, where they induce posttranslationally modified microtubules. Similarly, both ARF isoforms are required for the repositioning of Golgi complex fragments around the inclusion. We demonstrate that CT813 directly recruits ARF GTPases on the inclusion membrane and plays a pivotal role in their activation. Together, these results reveal that uses CT813 to hijack ARF GTPases to couple posttranslationally modified microtubules and Golgi complex repositioning at the inclusion. is an important cause of morbidity and a significant economic burden in the world. However, how develops its intracellular compartment, the so-called inclusion, is poorly understood. Using genetically engineered mutants, we discovered that the effector protein CT813 recruits and activates host ADP-ribosylation factor 1 (ARF1) and ARF4 to regulate microtubules. In this context, CT813 acts as a molecular platform that induces the posttranslational modification of microtubules around the inclusion. These cages are then used to reposition the Golgi complex during infection and promote the development of the inclusion. This study provides the first evidence that ARF1 and ARF4 play critical roles in controlling posttranslationally modified microtubules around the inclusion and that hijacks this novel function of ARF to reposition the Golgi complex.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Chlamydia trachomatis/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Complexo de Golgi/metabolismo
Microtúbulos/metabolismo
[Mh] Termos MeSH secundário: Fator 1 de Ribosilação do ADP/metabolismo
Fatores de Ribosilação do ADP/metabolismo
Actinas
Proteínas de Bactérias/genética
Chlamydia trachomatis/genética
Complexo de Golgi/ultraestrutura
Células HeLa
Interações Hospedeiro-Patógeno
Seres Humanos
Corpos de Inclusão/microbiologia
Microtúbulos/genética
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Bacterial Proteins); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.2 (ADP-Ribosylation Factor 1); EC 3.6.5.2 (ADP-Ribosylation Factors); EC 3.6.5.2 (ARF4 protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180126
[Lr] Data última revisão:
180126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE



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