Base de dados : MEDLINE
Pesquisa : D12.776.543.990.049 [Categoria DeCS]
Referências encontradas : 65 [refinar]
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  1 / 65 MEDLINE  
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[PMID]:26703368
[Au] Autor:Elsayed LE; Drouet V; Usenko T; Mohammed IN; Hamed AA; Elseed MA; Salih MA; Koko ME; Mohamed AY; Siddig RA; Elbashir MI; Ibrahim ME; Durr A; Stevanin G; Lesage S; Ahmed AE; Brice A
[Ad] Endereço:Inserm U1127, CNRS UMR7225, Sorbonne Universités, UPMC Université Paris 06, UMR_S1127, Institut du Cerveau et de la Moelle épinière, Paris, France.
[Ti] Título:A Novel Nonsense Mutation in DNAJC6 Expands the Phenotype of Autosomal-Recessive Juvenile-Onset Parkinson's Disease.
[So] Source:Ann Neurol;79(2):335-7, 2016 Feb.
[Is] ISSN:1531-8249
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Auxilinas/metabolismo
Fibroblastos/metabolismo
Proteínas de Choque Térmico HSP40/genética
Transtornos Parkinsonianos/genética
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Masculino
[Pt] Tipo de publicação:COMMENT; LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Auxilins); 0 (HSP40 Heat-Shock Proteins)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151226
[St] Status:MEDLINE
[do] DOI:10.1002/ana.24591


  2 / 65 MEDLINE  
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[PMID]:26702604
[Au] Autor:Olgiati S; Quadri M; Mandemakers W; Bonifati V
[Ad] Endereço:Department of Clinical Genetics, Erasmus MC, Rotterdam, the Netherlands.
[Ti] Título:Reply.
[So] Source:Ann Neurol;79(2):337-8, 2016 Feb.
[Is] ISSN:1531-8249
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Auxilinas/metabolismo
Fibroblastos/metabolismo
Proteínas de Choque Térmico HSP40/genética
Transtornos Parkinsonianos/genética
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Masculino
[Pt] Tipo de publicação:COMMENT; LETTER
[Nm] Nome de substância:
0 (Auxilins); 0 (HSP40 Heat-Shock Proteins)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160215
[Lr] Data última revisão:
160215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151226
[St] Status:MEDLINE
[do] DOI:10.1002/ana.24587


  3 / 65 MEDLINE  
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[PMID]:26538028
[Au] Autor:Ding J; Segarra VA; Chen S; Cai H; Lemmon SK; Ferro-Novick S
[Ad] Endereço:Department of Cellular and Molecular Medicine, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093-0668.
[Ti] Título:Auxilin facilitates membrane traffic in the early secretory pathway.
[So] Source:Mol Biol Cell;27(1):127-36, 2016 Jan 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Coat protein complexes contain an inner shell that sorts cargo and an outer shell that helps deform the membrane to give the vesicle its shape. There are three major types of coated vesicles in the cell: COPII, COPI, and clathrin. The COPII coat complex facilitates vesicle budding from the endoplasmic reticulum (ER), while the COPI coat complex performs an analogous function in the Golgi. Clathrin-coated vesicles mediate traffic from the cell surface and between the trans-Golgi and endosome. While the assembly and structure of these coat complexes has been extensively studied, the disassembly of COPII and COPI coats from membranes is less well understood. We describe a proteomic and genetic approach that connects the J-domain chaperone auxilin, which uncoats clathrin-coated vesicles, to COPII and COPI coat complexes. Consistent with a functional role for auxilin in the early secretory pathway, auxilin binds to COPII and COPI coat subunits. Furthermore, ER-Golgi and intra-Golgi traffic is delayed at 15°C in swa2Δ mutant cells, which lack auxilin. In the case of COPII vesicles, we link this delay to a defect in vesicle fusion. We propose that auxilin acts as a chaperone and/or uncoating factor for transport vesicles that act in the early secretory pathway.
[Mh] Termos MeSH primário: Auxilinas/genética
Auxilinas/metabolismo
Vesículas Revestidas por Clatrina/metabolismo
[Mh] Termos MeSH secundário: Vesículas Revestidas pelo Complexo de Proteína do Envoltório/genética
Vesículas Revestidas pelo Complexo de Proteína do Envoltório/metabolismo
Clatrina/metabolismo
Vesículas Revestidas por Clatrina/genética
Retículo Endoplasmático/metabolismo
Complexo de Golgi/metabolismo
Proteínas de Membrana/metabolismo
Transporte Proteico/fisiologia
Proteômica
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Via Secretória/fisiologia
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Auxilins); 0 (Clathrin); 0 (Membrane Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Vesicular Transport Proteins)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151106
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E15-09-0631


  4 / 65 MEDLINE  
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Barbosa, Egberto Reis
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[PMID]:26528954
[Au] Autor:Olgiati S; Quadri M; Fang M; Rood JP; Saute JA; Chien HF; Bouwkamp CG; Graafland J; Minneboo M; Breedveld GJ; Zhang J; Verheijen FW; Boon AJ; Kievit AJ; Jardim LB; Mandemakers W; Barbosa ER; Rieder CR; Leenders KL; Wang J; Bonifati V; International Parkinsonism Genetics Network
[Ad] Endereço:Department of Clinical Genetics, Erasmus MC, Rotterdam, the Netherlands.
[Ti] Título:DNAJC6 Mutations Associated With Early-Onset Parkinson's Disease.
[So] Source:Ann Neurol;79(2):244-56, 2016 Feb.
[Is] ISSN:1531-8249
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: DNAJC6 mutations were recently described in two families with autosomal recessive juvenile parkinsonism (onset age < 11), prominent atypical signs, poor or absent response to levodopa, and rapid progression (wheelchair-bound within ∼10 years from onset). Here, for the first time, we report DNAJC6 mutations in early-onset Parkinson's disease (PD). METHODS: The DNAJC6 open reading frame was analyzed in 274 patients with early-onset sporadic or familial PD. Selected variants were followed up by cosegregation, homozygosity mapping, linkage analysis, whole-exome sequencing, and protein studies. RESULTS: We identified two families with different novel homozygous DNAJC6 mutations segregating with PD. In each family, the DNAJC6 mutation was flanked by long runs of homozygosity within highest linkage peaks. Exome sequencing did not detect additional pathogenic variants within the linkage regions. In both families, patients showed severely decreased steady-state levels of the auxilin protein in fibroblasts. We also identified a sporadic patient carrying two rare noncoding DNAJC6 variants possibly effecting RNA splicing. All these cases fulfilled the criteria for a clinical diagnosis of early-onset PD, had symptoms onset in the third-to-fifth decade, and slow disease progression. Response to dopaminergic therapies was prominent, but, in some patients, limited by psychiatric side effects. The phenotype overlaps that of other monogenic forms of early-onset PD. INTERPRETATION: Our findings delineate a novel form of hereditary early-onset PD. Screening of DNAJC6 is warranted in all patients with early-onset PD compatible with autosomal recessive inheritance. Our data provide further evidence for the involvement of synaptic vesicles endocytosis and trafficking in PD pathogenesis.
[Mh] Termos MeSH primário: Auxilinas/metabolismo
Fibroblastos/metabolismo
Proteínas de Choque Térmico HSP40/genética
Transtornos Parkinsonianos/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idade de Início
Idoso
Idoso de 80 Anos ou mais
Feminino
Seres Humanos
Masculino
Meia-Idade
Mutação
Transtornos Parkinsonianos/metabolismo
Fenótipo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Auxilins); 0 (DNAJC6 protein, human); 0 (HSP40 Heat-Shock Proteins)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160215
[Lr] Data última revisão:
160215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151104
[St] Status:MEDLINE
[do] DOI:10.1002/ana.24553


  5 / 65 MEDLINE  
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[PMID]:26392261
[Au] Autor:Xiao J; Li C; Xu S; Xing L; Xu Y; Chong K
[Ad] Endereço:Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China (J.X., C.L., S.X., L.X., Y.X., K.C.);National Center for Plant Gene Research, Beijing 100093, China (K.C.); andUniversity of the Chinese Academy of Sciences, Beijing 100049, China (J
[Ti] Título:JACALIN-LECTIN LIKE1 Regulates the Nuclear Accumulation of GLYCINE-RICH RNA-BINDING PROTEIN7, Influencing the RNA Processing of FLOWERING LOCUS C Antisense Transcripts and Flowering Time in Arabidopsis.
[So] Source:Plant Physiol;169(3):2102-17, 2015 Nov.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lectins selectively recognize sugars or glycans for defense in living cells, but less is known about their roles in the development process and the functional network with other factors. Here, we show that Arabidopsis (Arabidopsis thaliana) JACALIN-LECTIN LIKE1 (AtJAC1) functions in flowering time control. Loss of function of AtJAC1 leads to precocious flowering, whereas overexpression of AtJAC1 causes delayed flowering. AtJAC1 influences flowering through regulation of the key flowering repressor gene FLOWERING LOCUS C (FLC). Genetic analysis revealed that AtJAC1's function is mostly dependent on GLYCINE-RICH RNA-BINDING PROTEIN7 (GRP7), an upstream regulator of FLC. Biochemical and cell biological data indicated that AtJAC1 interacted physically with GRP7 specifically in the cytoplasm. AtJAC1 influences the nucleocytoplasmic distribution of GRP7, with predominant nuclear localization of GRP7 when AtJAC1 function is lost but retention of GRP7 in the cytoplasm when AtJAC1 is overexpressed. A temporal inducible assay suggested that AtJAC1's regulation of flowering could be compromised by the nuclear accumulation of GRP7. In addition, GRP7 binds to the antisense precursor messenger RNA of FLC through a conserved RNA motif. Loss of GRP7 function leads to the elevation of total FLC antisense transcripts and reduced proximal-distal polyadenylation ratio, as well as histone methylation changes in the FLC gene body region and increased total functional sense FLC transcript. Attenuating the direct binding of GRP7 with competing artificial RNAs leads to changes of FLC antisense precursor messenger RNA processing and flowering transition. Taken together, our study indicates that AtJAC1 coordinates with GRP7 in shaping plant development through the regulation of RNA processing in Arabidopsis.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/genética
Auxilinas/metabolismo
Regulação da Expressão Gênica de Plantas
Histonas/metabolismo
Proteínas de Domínio MADS/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/citologia
Arabidopsis/fisiologia
Proteínas de Arabidopsis/genética
Auxilinas/genética
Cromatina/genética
Cromatina/metabolismo
Flores/citologia
Flores/genética
Flores/fisiologia
Expressão Gênica
Glicina/metabolismo
Histonas/genética
Proteínas de Domínio MADS/genética
Metilação
Mutagênese Insercional
Lectinas de Plantas/metabolismo
Poliadenilação
RNA Antissenso/genética
RNA Antissenso/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/genética
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ATGRP7 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Auxilins); 0 (Chromatin); 0 (F9E10.5 protein, Arabidopsis); 0 (FLF protein, Arabidopsis); 0 (Histones); 0 (MADS Domain Proteins); 0 (Plant Lectins); 0 (RNA, Antisense); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (jacalin); TE7660XO1C (Glycine)
[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:150923
[St] Status:MEDLINE
[do] DOI:10.1104/pp.15.00801


  6 / 65 MEDLINE  
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[PMID]:26367107
[Au] Autor:Dannhauser PN; Platen M; Böning H; Schaap IA
[Ad] Endereço:Institute of Cell Biology, Centre of Anatomy, Hannover Medical School, 30625 Hannover, Germany.
[Ti] Título:Durable protein lattices of clathrin that can be functionalized with nanoparticles and active biomolecules.
[So] Source:Nat Nanotechnol;10(11):954-7, 2015 Nov.
[Is] ISSN:1748-3395
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Biological molecules that self-assemble and interact with other molecules are attractive building blocks for engineering biological devices. DNA has been widely used for the creation of nanomaterials, but the use of proteins remains largely unexplored. Here, we show that clathrin can form homogeneous and extended two-dimensional lattices on a variety of substrates, including glass, metal, carbon and plastic. Clathrin is a three-legged protein complex with unique self-assembling properties and is relevant in the formation of membrane transport vesicles in eukaryotic cells. We used a fragment of the adaptor protein epsin to immobilize clathrin lattices on the substrates. The lattices span multiple square millimetres with a regular periodicity of 30 nm and can be functionalized via modified subunits of clathrin with either inorganic nanoparticles or active enzymes. The lattices can be stored for months after crosslinking and stabilization with uranyl acetate. They could be dehydrated and rehydrated without loss of function, offering potential applications in sensing and as biosynthetic reactors.
[Mh] Termos MeSH primário: Materiais Biocompatíveis/química
Clatrina/química
Proteínas Imobilizadas/química
Nanoestruturas/química
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/química
Animais
Auxilinas/química
Bovinos
Ouro/química
Modelos Moleculares
Nanopartículas/química
Nanopartículas/ultraestrutura
Nanoestruturas/ultraestrutura
Nanotecnologia
Compostos Organometálicos/química
Estabilidade Proteica
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (Auxilins); 0 (Biocompatible Materials); 0 (Clathrin); 0 (Immobilized Proteins); 0 (Organometallic Compounds); 0 (epsin); 285PN2K1AO (uranyl acetate); 7440-57-5 (Gold)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150915
[St] Status:MEDLINE
[do] DOI:10.1038/nnano.2015.206


  7 / 65 MEDLINE  
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[PMID]:26345367
[Au] Autor:Park BC; Yim YI; Zhao X; Olszewski MB; Eisenberg E; Greene LE
[Ad] Endereço:Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
[Ti] Título:The clathrin-binding and J-domains of GAK support the uncoating and chaperoning of clathrin by Hsc70 in the brain.
[So] Source:J Cell Sci;128(20):3811-21, 2015 Oct 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cyclin-G-associated kinase (GAK), the ubiquitously expressed J-domain protein, is essential for the chaperoning and uncoating of clathrin that is mediated by Hsc70 (also known as HSPA8). Adjacent to the C-terminal J-domain that binds to Hsc70, GAK has a clathrin-binding domain that is linked to an N-terminal kinase domain through a PTEN-like domain. Knocking out GAK in fibroblasts caused inhibition of clathrin-dependent trafficking, which was rescued by expressing a 62-kDa fragment of GAK, comprising just the clathrin-binding and J-domains. Expressing this fragment as a transgene in mice rescued the lethality and the histological defects caused by knocking out GAK in the liver or in the brain. Furthermore, when both GAK and auxilin (also known as DNAJC6), the neuronal-specific homolog of GAK, were knocked out in the brain, mice expressing the 62-kDa GAK fragment were viable, lived a normal life-span and had no major behavior abnormalities. However, these mice were about half the size of wild-type mice. Therefore, the PTEN-like domains of GAK and auxilin are not essential for Hsc70-dependent chaperoning and uncoating of clathrin, but depending on the tissue, these domains appear to increase the efficiency of these co-chaperones.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Clatrina/metabolismo
Proteínas de Choque Térmico HSC70/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
[Mh] Termos MeSH secundário: Animais
Auxilinas/genética
Auxilinas/metabolismo
Clatrina/genética
Proteínas de Choque Térmico HSC70/genética
Camundongos
Camundongos Knockout
Ligação Proteica
Estrutura Terciária de Proteína
Transporte Proteico/fisiologia
Proteínas Serina-Treonina Quinases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Auxilins); 0 (Clathrin); 0 (HSC70 Heat-Shock Proteins); 0 (Hspa8 protein, mouse); EC 2.7.11.1 (GAK protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150909
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.171058


  8 / 65 MEDLINE  
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[PMID]:26031938
[Au] Autor:Troisi EM; Rockman ME; Nguyen PP; Oliver EE; Hines JK
[Ad] Endereço:Department of Chemistry, Lafayette College, Easton, PA, USA.
[Ti] Título:Swa2, the yeast homolog of mammalian auxilin, is specifically required for the propagation of the prion variant [URE3-1].
[So] Source:Mol Microbiol;97(5):926-41, 2015 Sep.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Yeast prions require a core set of chaperone proteins including Sis1, Hsp70 and Hsp104 to generate new amyloid templates for stable propagation, yet emerging studies indicate that propagation of some prions requires additional chaperone activities, demonstrating chaperone specificity beyond the common amyloid requirements. To comprehensively assess such prion-specific requirements for the propagation of the [URE3] prion variant [URE3-1], we screened 12 yeast cytosolic J-proteins, and here we report a novel role for the J-protein Swa2/Aux1. Swa2 is the sole yeast homolog of the mammalian protein auxilin, which, like Swa2, functions in vesicle-mediated endocytosis by disassembling the structural lattice formed by the protein clathrin. We found that, in addition to Sis1, [URE3-1] is specifically dependent upon Swa2, but not on any of the 11 other J-proteins. Further, we show that [URE3-1] propagation requires both a functional J-domain and the tetratricopeptide repeat (TPR) domain, but surprisingly does not require Swa2-clathrin binding. Because the J-domain of Swa2 can be replaced with the J-domains of other proteins, our data strongly suggest that prion-chaperone specificity arises from the Swa2 TPR domain and supports a model where Swa2 acts through Hsp70, most likely to provide additional access points for Hsp104 to promote prion template generation.
[Mh] Termos MeSH primário: Glutationa Peroxidase/metabolismo
Fosfoproteínas/química
Fosfoproteínas/metabolismo
Príons/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Transporte Vesicular/química
Proteínas de Transporte Vesicular/metabolismo
[Mh] Termos MeSH secundário: Amiloide/metabolismo
Animais
Auxilinas/genética
Proteínas de Choque Térmico HSP70/genética
Proteínas de Choque Térmico HSP70/metabolismo
Proteínas de Choque Térmico/genética
Proteínas de Choque Térmico/metabolismo
Seres Humanos
Chaperonas Moleculares/metabolismo
Fosfoproteínas/genética
Dobramento de Proteína
Estrutura Terciária de Proteína
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Transporte Vesicular/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amyloid); 0 (Auxilins); 0 (HSP70 Heat-Shock Proteins); 0 (Heat-Shock Proteins); 0 (Molecular Chaperones); 0 (Phosphoproteins); 0 (Prions); 0 (SWA2 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Vesicular Transport Proteins); 143012-44-6 (HsP104 protein, S cerevisiae); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.11.1.9 (URE2 protein, S cerevisiae)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150603
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13076


  9 / 65 MEDLINE  
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[PMID]:25233425
[Au] Autor:Kalli AC; Sansom MS
[Ad] Endereço:*Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
[Ti] Título:Interactions of peripheral proteins with model membranes as viewed by molecular dynamics simulations.
[So] Source:Biochem Soc Trans;42(5):1418-24, 2014 Oct.
[Is] ISSN:1470-8752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Many cellular signalling and related events are triggered by the association of peripheral proteins with anionic lipids in the cell membrane (e.g. phosphatidylinositol phosphates or PIPs). This association frequently occurs via lipid-binding modules, e.g. pleckstrin homology (PH), C2 and four-point-one, ezrin, radixin, moesin (FERM) domains, present in peripheral and cytosolic proteins. Multiscale simulation approaches that combine coarse-grained and atomistic MD simulations may now be applied with confidence to investigate the molecular mechanisms of the association of peripheral proteins with model bilayers. Comparisons with experimental data indicate that such simulations can predict specific peripheral protein-lipid interactions. We discuss the application of multiscale MD simulation and related approaches to investigate the association of peripheral proteins which contain PH, C2 or FERM-binding modules with lipid bilayers of differing phospholipid composition, including bilayers containing multiple PIP molecules.
[Mh] Termos MeSH primário: Auxilinas/metabolismo
Bicamadas Lipídicas/metabolismo
Modelos Moleculares
PTEN Fosfo-Hidrolase/metabolismo
Fosfatos de Fosfatidilinositol/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
Talina/metabolismo
[Mh] Termos MeSH secundário: Animais
Auxilinas/química
Bovinos
Ciona intestinalis
Seres Humanos
Bicamadas Lipídicas/química
Simulação de Dinâmica Molecular
PTEN Fosfo-Hidrolase/química
Fosfatos de Fosfatidilinositol/química
Monoéster Fosfórico Hidrolases/química
Estrutura Terciária de Proteína
Transporte Proteico
Talina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Auxilins); 0 (Lipid Bilayers); 0 (Phosphatidylinositol Phosphates); 0 (TLN1 protein, human); 0 (Talin); EC 3.1.3.- (voltage-sensor-containing phosphatase, Ciona intestinalis); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (PTEN protein, human)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140919
[St] Status:MEDLINE
[do] DOI:10.1042/BST20140144


  10 / 65 MEDLINE  
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[PMID]:24815030
[Au] Autor:Böcking T; Aguet F; Rapoport I; Banzhaf M; Yu A; Zeeh JC; Kirchhausen T
[Ad] Endereço:Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Centre for Vascular Research, University of New South Wales, Sydney NSW 2052 Australia. Electronic address: till.boecking@unsw.edu.au.
[Ti] Título:Key interactions for clathrin coat stability.
[So] Source:Structure;22(6):819-29, 2014 Jun 10.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Clathrin-coated vesicles are major carriers of vesicular traffic in eukaryotic cells. This endocytic pathway relies on cycles of clathrin coat assembly and Hsc70-mediated disassembly. Here we identify histidine residues as major determinants of lattice assembly and stability. They are located at the invariant interface between the proximal and distal segments of clathrin heavy chains, in triskelions centered on two adjacent vertices of the coated-vesicle lattice. Mutation of these histidine residues to glutamine alters the pH dependence of coat stability. We then describe single-particle fluorescence imaging experiments in which we follow the effect of these histidine mutations on susceptibility to Hsc70-dependent uncoating. Coats destabilized by these mutations require fewer Hsc70 molecules to initiate disassembly, as predicted by a model in which Hsc70 traps conformational distortions during the auxilin- and Hsc70:ATP-mediated uncoating reaction.
[Mh] Termos MeSH primário: Cadeias Pesadas de Clatrina/química
Cadeias Leves de Clatrina/química
[Mh] Termos MeSH secundário: Animais
Auxilinas/química
Sítios de Ligação
Bovinos
Cadeias Pesadas de Clatrina/genética
Cadeias Pesadas de Clatrina/ultraestrutura
Cadeias Leves de Clatrina/genética
Cadeias Leves de Clatrina/ultraestrutura
Vesículas Revestidas por Clatrina/química
Vesículas Revestidas por Clatrina/ultraestrutura
Proteínas de Choque Térmico HSC70/química
Histidina/química
Concentração de Íons de Hidrogênio
Modelos Moleculares
Complexos Multiproteicos/química
Mutação
Estabilidade Proteica
Ratos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Auxilins); 0 (Clathrin Light Chains); 0 (HSC70 Heat-Shock Proteins); 0 (Multiprotein Complexes); 0 (Recombinant Proteins); 114899-12-6 (Clathrin Heavy Chains); 4QD397987E (Histidine)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140513
[St] Status:MEDLINE



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