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  1 / 1333 MEDLINE  
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[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 / 1333 MEDLINE  
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[PMID]:29293623
[Au] Autor:Unterbruner K; Matthes F; Schilling J; Nalavade R; Weber S; Winter J; Krauß S
[Ad] Endereço:Regulatory RNA-protein interactions in neurodegenerative diseases, German Center for Neurodegenerative Diseases (DZNE), Bonn, North Rhine-Westphalia, Germany.
[Ti] Título:MicroRNAs miR-19, miR-340, miR-374 and miR-542 regulate MID1 protein expression.
[So] Source:PLoS One;13(1):e0190437, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The MID1 ubiquitin ligase activates mTOR signaling and regulates mRNA translation. Misregulation of MID1 expression is associated with various diseases including midline malformation syndromes, cancer and neurodegenerative diseases. While this indicates that MID1 expression must be tightly regulated to prevent disease states specific mechanisms involved have not been identified. We examined miRNAs to determine mechanisms that regulate MID1 expression. MicroRNAs (miRNA) are small non-coding RNAs that recognize specific sequences in their target mRNAs. Upon binding, miRNAs typically downregulate expression of these targets. Here, we identified four miRNAs, miR-19, miR-340, miR-374 and miR-542 that bind to the 3'-UTR of the MID1 mRNA. These miRNAs not only regulate MID1 expression but also mTOR signaling and translation of disease associated mRNAs and could therefore serve as potential drugs for future therapy development.
[Mh] Termos MeSH primário: MicroRNAs/fisiologia
Proteínas dos Microtúbulos/metabolismo
Proteínas Nucleares/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Células HEK293
Seres Humanos
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (MicroRNAs); 0 (Microtubule Proteins); 0 (Mid1 protein, human); 0 (Nuclear Proteins); 0 (Transcription Factors)
[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:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190437


  3 / 1333 MEDLINE  
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[PMID]:28714291
[Au] Autor:Nicholson LK
[Ad] Endereço:Department of Molecular Biology & Genetics, Cornell University, Ithaca, NY, USA.
[Ti] Título:Mechanism of midline defect-causing mutation P151L in MID1 revealed.
[So] Source:FEBS J;284(14):2167-2169, 2017 07.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The P151L mutation in the B-box1 domain of MID1 causes midline defects in X-linked Opitz G Syndrome. MID1 is known to be a key regulator of phosphatase PP2A through formation of a complex with its catalytic (PP2Ac) and regulatory (α4) subunits. Wright et al. show that this mutation retains B-box1 domain structure and E3 ligase activity (star) but blocks interaction with α4, indicating disruption of the MID1-α4-PP2Ac complex.
[Mh] Termos MeSH primário: Proteínas dos Microtúbulos/química
Proteína Fosfatase 2/química
[Mh] Termos MeSH secundário: Seres Humanos
Hipertelorismo/genética
Masculino
Mutação
Fatores de Transcrição/química
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Microtubule Proteins); 0 (Transcription Factors); EC 3.1.3.16 (Protein Phosphatase 2)
[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:170718
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14149


  4 / 1333 MEDLINE  
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[PMID]:28694105
[Au] Autor:Liu XH; Yang YF; Fang HY; Wang XH; Zhang MF; Wu DC
[Ad] Endereço:Department of Emergency, The Third Affiliated Hospital of Sun Yat-sen University, Guangzhou, China.
[Ti] Título:CEP131 indicates poor prognosis and promotes cell proliferation and migration in hepatocellular carcinoma.
[So] Source:Int J Biochem Cell Biol;90:1-8, 2017 Sep.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Centrosomal proteins have been implicated in the progression of human diseases. CEP131 plays important roles in centrosome duplication and genome stability, but its role in cancers remains largely unknown. Here, we showed that CEP131 expression was increased in hepatocellular carcinoma (HCC), compared to the paracarcinoma tissues, at both mRNA and protein levels. High CEP131 expression was closely associated with tumor size (P=0.020), tumor capsule (P=0.043), TNM stage (P=0.007) and tumor differentiation (P=0.019). Furthermore, patients with high expression of CEP131 were accompanied with worse overall and disease-free survivals in our and TCGA cohorts consisting of a total of 802 cases. The prognostic value of CEP131 was further confirmed by stratified survival analysis. Multivariate cox regression model indicated that CEP131 was an independent factor for overall survival (hazard ratio=1.762, 95% confident interval: 1.443-2.151, P<0.001). In vitro data demonstrated that nucleophosmin (NPM) physically bound to CEP131 and maintained its protein stability. Overexpression of CEP131 in HCC cell lines enhanced cell proliferation and migration, whereas the knockdown of CEP131 led to the opposite phenotypes. Further studies demonstrated that CEP131 exhibited oncogenic activity via activation of PI3K/AKT signaling pathway. Taken together, our findings suggest CEP131 serves as a potential prognostic biomarker in HCC, and functions as an oncogene in this deadly disease.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/diagnóstico
Carcinoma Hepatocelular/patologia
Proteínas de Ciclo Celular/metabolismo
Movimento Celular
Neoplasias Hepáticas/diagnóstico
Neoplasias Hepáticas/patologia
Proteínas dos Microtúbulos/metabolismo
[Mh] Termos MeSH secundário: Carcinoma Hepatocelular/metabolismo
Ativação Enzimática
Feminino
Seres Humanos
Neoplasias Hepáticas/metabolismo
Masculino
Meia-Idade
Proteínas Nucleares/metabolismo
Fosfatidilinositol 3-Quinases/metabolismo
Prognóstico
Estabilidade Proteica
Proteínas Proto-Oncogênicas c-akt/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CEP131 protein, human); 0 (Cell Cycle Proteins); 0 (Microtubule Proteins); 0 (Nuclear Proteins); 117896-08-9 (nucleophosmin); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[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:170712
[St] Status:MEDLINE


  5 / 1333 MEDLINE  
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[PMID]:28652389
[Au] Autor:Howes SC; Geyer EA; LaFrance B; Zhang R; Kellogg EH; Westermann S; Rice LM; Nogales E
[Ad] Endereço:Biophysics Graduate Group, University of California, Berkeley, Berkeley, CA.
[Ti] Título:Structural differences between yeast and mammalian microtubules revealed by cryo-EM.
[So] Source:J Cell Biol;216(9):2669-2677, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microtubules are polymers of αß-tubulin heterodimers essential for all eukaryotes. Despite sequence conservation, there are significant structural differences between microtubules assembled in vitro from mammalian or budding yeast tubulin. Yeast MTs were not observed to undergo compaction at the interdimer interface as seen for mammalian microtubules upon GTP hydrolysis. Lack of compaction might reflect slower GTP hydrolysis or a different degree of allosteric coupling in the lattice. The microtubule plus end-tracking protein Bim1 binds yeast microtubules both between αß-tubulin heterodimers, as seen for other organisms, and within tubulin dimers, but binds mammalian tubulin only at interdimer contacts. At the concentrations used in cryo-electron microscopy, Bim1 causes the compaction of yeast microtubules and induces their rapid disassembly. Our studies demonstrate structural differences between yeast and mammalian microtubules that likely underlie their differing polymerization dynamics. These differences may reflect adaptations to the demands of different cell size or range of physiological growth temperatures.
[Mh] Termos MeSH primário: Microscopia Crioeletrônica
Microtúbulos/ultraestrutura
Proteínas de Saccharomyces cerevisiae/ultraestrutura
Saccharomyces cerevisiae/ultraestrutura
Tubulina (Proteína)/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Proteínas de Ciclo Celular/metabolismo
Proteínas de Ciclo Celular/ultraestrutura
Guanosina Trifosfato/metabolismo
Hidrólise
Proteínas dos Microtúbulos/metabolismo
Proteínas dos Microtúbulos/ultraestrutura
Microtúbulos/genética
Microtúbulos/metabolismo
Simulação de Dinâmica Molecular
Ligação Proteica
Multimerização Proteica
Estrutura Quaternária de Proteína
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Relação Estrutura-Atividade
Sus scrofa
Tubulina (Proteína)/genética
Tubulina (Proteína)/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BIM1 protein, S cerevisiae); 0 (Cell Cycle Proteins); 0 (Microtubule Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Tubulin); 86-01-1 (Guanosine Triphosphate)
[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:170628
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201612195


  6 / 1333 MEDLINE  
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[PMID]:28548391
[Au] Autor:Wright KM; Du H; Massiah MA
[Ad] Endereço:Department of Chemistry and Center of Biomolecular Science, George Washington University, DC, USA.
[Ti] Título:Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.
[So] Source:FEBS J;284(14):2183-2193, 2017 Jul.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations of human MID1 are associated with X-linked Opitz G Syndrome (XLOS), which is characterized by midline birth defects. XLOS-observed mutations within the MID1 B-box1 domain are associated with cleft lip/palate, wide-spaced eyes and hyperspadias. Three of the four XLOS-observed mutations in the B-box1 domain results in unfolding but the structural and functional effects of the P151L mutation is not characterized. Here, we demonstrate that the P151L mutation does not disrupt the overall tertiary structure of the B-box1 domain and the adjacent domains. In fact, MID1 E3 ligase activity is slightly enhanced. However, the P151L mutation disrupted the ability of MID1 to catalyze the poly-ubiquitination of alpha4, a novel regulator of PP2A. This observation is consistent with results observed with the other three structure-destabilizing B-box1 mutations in targeting alpha4 but not PP2A. Alpha4 is shown to bind and sequester the catalytic subunit of PP2A and protect it from MID1-mediated ubiquitination and as a result, an increase in alpha4 can contribute to an increase in PP2A, playing a greater role in midline development during embryogenesis.
[Mh] Termos MeSH primário: Fissura Palatina/genética
Fissura Palatina/metabolismo
Esôfago/anormalidades
Doenças Genéticas Ligadas ao Cromossomo X/genética
Doenças Genéticas Ligadas ao Cromossomo X/metabolismo
Hipertelorismo/genética
Hipertelorismo/metabolismo
Hipospadia/genética
Hipospadia/metabolismo
Proteínas dos Microtúbulos/química
Proteínas dos Microtúbulos/metabolismo
Mutação
Proteínas Nucleares/química
Proteínas Nucleares/metabolismo
Processamento de Proteína Pós-Traducional
Fatores de Transcrição/química
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Fissura Palatina/patologia
Esôfago/metabolismo
Esôfago/patologia
Doenças Genéticas Ligadas ao Cromossomo X/patologia
Seres Humanos
Hipertelorismo/patologia
Hipospadia/patologia
Proteínas dos Microtúbulos/genética
Proteínas dos Microtúbulos/ultraestrutura
Modelos Moleculares
Proteínas Nucleares/genética
Proteínas Nucleares/ultraestrutura
Domínios Proteicos
Proteína Fosfatase 2/metabolismo
Estrutura Terciária de Proteína
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Fatores de Transcrição/genética
Fatores de Transcrição/ultraestrutura
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Microtubule Proteins); 0 (Mid1 protein, human); 0 (Nuclear Proteins); 0 (Transcription Factors); EC 3.1.3.16 (Protein Phosphatase 2)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14121


  7 / 1333 MEDLINE  
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[PMID]:28490474
[Au] Autor:Forth S; Kapoor TM
[Ad] Endereço:Laboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY 10065.
[Ti] Título:The mechanics of microtubule networks in cell division.
[So] Source:J Cell Biol;216(6):1525-1531, 2017 Jun 05.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The primary goal of a dividing somatic cell is to accurately and equally segregate its genome into two new daughter cells. In eukaryotes, this process is performed by a self-organized structure called the mitotic spindle. It has long been appreciated that mechanical forces must be applied to chromosomes. At the same time, the network of microtubules in the spindle must be able to apply and sustain large forces to maintain spindle integrity. Here we consider recent efforts to measure forces generated within microtubule networks by ensembles of key proteins. New findings, such as length-dependent force generation, protein clustering by asymmetric friction, and entropic expansion forces will help advance models of force generation needed for spindle function and maintaining integrity.
[Mh] Termos MeSH primário: Divisão Celular
Mecanotransdução Celular
Microtúbulos/fisiologia
Fuso Acromático/fisiologia
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Proteínas dos Microtúbulos/metabolismo
Microtúbulos/metabolismo
Fuso Acromático/metabolismo
Estresse Mecânico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Microtubule Proteins)
[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:170512
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201612064


  8 / 1333 MEDLINE  
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[PMID]:28393201
[Au] Autor:Li X; Yang B; Wang L; Chen L; Luo X; Liu L
[Ad] Endereço:Department of Hematology, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, P.R. China.
[Ti] Título:SPAG6 regulates cell apoptosis through the TRAIL signal pathway in myelodysplastic syndromes.
[So] Source:Oncol Rep;37(5):2839-2846, 2017 May.
[Is] ISSN:1791-2431
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Myelodysplastic syndromes (MDSs) are a group of malignant clone hematopoietic stem-cell diseases, and the evolution and progression of MDS depend on the abnormal apoptosis of bone marrow cells. Our previous studies have indicated that sperm-associated antigen 6 (SPAG6), located in the uniparental disomy regions of myeloid cells, is overexpressed in patients with MDS as compared to controls, and SPAG6 can inhibit apoptosis of SKM-1. However, the concrete mechanism is still unclear. In the present study, it was found that the TNF-related apoptosis-inducing ligand (TRAIL)signal pathway was activated when the expression of SPAG6 was inhibited by SPAG6-shRNA lentivirus in SKM-1 cells. Additionally, the results of flow cytometry, Cell Counting Kit-8 assay and western blot analysis implied that the TRAIL signal pathway could be inhibited by a high expression of SPAG6. However, SPAG6 cannot influence the expression of TRAIL death receptors, except for FADD. Additionally the interaction between FADD and TRAIL death receptors also increased in SKM-1 cells infected with SPAG6-shRNA lentivirus. Thus, our study demonstrates that SPAG6 may regulate apoptosis in SKM-1 through the TRAIL signal pathway, indicating that SPAG6 could be a potential therapeutic target.
[Mh] Termos MeSH primário: Proteína de Domínio de Morte Associada a Fas/metabolismo
Proteínas dos Microtúbulos/genética
Síndromes Mielodisplásicas/genética
Receptores do Ligante Indutor de Apoptose Relacionado a TNF/metabolismo
Ligante Indutor de Apoptose Relacionado a TNF/metabolismo
[Mh] Termos MeSH secundário: Apoptose
Linhagem Celular Tumoral
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Células K562
Proteínas dos Microtúbulos/metabolismo
Síndromes Mielodisplásicas/metabolismo
RNA Interferente Pequeno/genética
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (FADD protein, human); 0 (Fas-Associated Death Domain Protein); 0 (Microtubule Proteins); 0 (RNA, Small Interfering); 0 (Receptors, TNF-Related Apoptosis-Inducing Ligand); 0 (SPAG6 protein, human); 0 (TNF-Related Apoptosis-Inducing Ligand); 0 (TNFSF10 protein, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE
[do] DOI:10.3892/or.2017.5540


  9 / 1333 MEDLINE  
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[PMID]:28374483
[Au] Autor:Arumugam S; Kaur A
[Ad] Endereço:European Molecular Biology Laboratory Australia Node for Single Molecule Science and ARC Centre of Excellence in Advanced Molecular Imaging, School of Medical Sciences, University of New South Wales, Sydney, 2052, New South Wales, Australia.
[Ti] Título:The Lipids of the Early Endosomes: Making Multimodality Work.
[So] Source:Chembiochem;18(12):1053-1060, 2017 Jun 19.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Early endosomes are dynamic intracellular compartments that fuse with incoming endocytic carrier vesicles and associated cargoes from the plasma membrane. It has been long known that the chemical structures of lipids confer striking properties and rich biochemistry on bilayers. Although the organisational principles of the plasma membrane are relatively better understood, understanding endosomal membranes has been challenging. It has become increasingly apparent that endosomal membranes, because of their lipid compositions and interactions, use distinct lipid chemistries. We discuss the biochemical and biophysical phenomena in play at the early endosomal membrane. We focus on cholesterol, phosphoinositides, and phosphatidylserine and their clear roles in endosome functions. We discuss the various principles and mechanisms underpinning how these lipids are implicated at the functional level in the working of endosomes, and we summarise early endosomes as a multimodal organelle employing distinct lipid-specific mechanisms.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Colesterol/metabolismo
Endossomos/metabolismo
Fosfatidilinositóis/metabolismo
Fosfatidilserinas/metabolismo
Vesículas Transportadoras/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/ultraestrutura
Endocitose/genética
Endossomos/ultraestrutura
Células Eucarióticas/metabolismo
Células Eucarióticas/ultraestrutura
Regulação da Expressão Gênica
Seres Humanos
Proteínas dos Microtúbulos/genética
Proteínas dos Microtúbulos/metabolismo
Receptores de Esteroides/genética
Receptores de Esteroides/metabolismo
Transdução de Sinais
Vesículas Transportadoras/ultraestrutura
Proteínas rab de Ligação ao GTP/genética
Proteínas rab de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Microtubule Proteins); 0 (Phosphatidylinositols); 0 (Phosphatidylserines); 0 (Receptors, Steroid); 0 (oxysterol binding protein); 97C5T2UQ7J (Cholesterol); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700046


  10 / 1333 MEDLINE  
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[PMID]:28356353
[Au] Autor:Kupke T; Malsam J; Schiebel E
[Ad] Endereço:From the Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany and.
[Ti] Título:A ternary membrane protein complex anchors the spindle pole body in the nuclear envelope in budding yeast.
[So] Source:J Biol Chem;292(20):8447-8458, 2017 May 19.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In budding yeast ( e) the multilayered spindle pole body (SPB) is embedded in the nuclear envelope (NE) at fusion sites of the inner and outer nuclear membrane. The SPB is built from 18 different proteins, including the three integral membrane proteins Mps3, Ndc1, and Mps2. These membrane proteins play an essential role in the insertion of the new SPB into the NE. How the huge core structure of the SPB is anchored in the NE has not been investigated thoroughly until now. The present model suggests that the NE protein Mps2 interacts via Bbp1 with Spc29, one of the coiled-coil proteins forming the central plaque of the SPB. To test this model, we purified and reconstituted the Mps2-Bbp1 complex from yeast and incorporated the complex into liposomes. We also demonstrated that Mps2-Bbp1 directly interacts with Mps3 and Ndc1. We then purified Spc29 and reconstituted the ternary Mps2-Bbp1-Spc29 complex, proving that Bbp1 can simultaneously interact with Mps2 and Spc29 and in this way link the central plaque of the SPB to the nuclear envelope. Interestingly, Bbp1 induced oligomerization of Spc29, which may represent an early step in SPB duplication. Together, this analysis provides important insights into the interaction network that inserts the new SPB into the NE and indicates that the Mps2-Bbp1 complex is the central unit of the SPB membrane anchor.
[Mh] Termos MeSH primário: Complexos Multiproteicos/metabolismo
Membrana Nuclear/metabolismo
Multimerização Proteica/fisiologia
Saccharomyces cerevisiae/metabolismo
Corpos Polares do Fuso/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Proteínas dos Microtúbulos/genética
Proteínas dos Microtúbulos/metabolismo
Proteínas Associadas aos Microtúbulos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Complexos Multiproteicos/genética
Membrana Nuclear/genética
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Corpos Polares do Fuso/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BBP1 protein, S cerevisiae); 0 (MPS2 protein, S cerevisiae); 0 (Membrane Proteins); 0 (Microtubule Proteins); 0 (Microtubule-Associated Proteins); 0 (Mps3 protein, S cerevisiae); 0 (Multiprotein Complexes); 0 (NDC1 protein, S cerevisiae); 0 (Nuclear Pore Complex Proteins); 0 (Nuclear Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Spc29 protein, S cerevisiae)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170608
[Lr] Data última revisão:
170608
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.780601



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