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[PMID]:27798680
[Au] Autor:Noble JW; Hunter DV; Roskelley CD; Chan EK; Mills J
[Ad] Endereço:Department of Biology, Trinity Western University, Langley, British Columbia, Canada.
[Ti] Título:Loukoumasomes Are Distinct Subcellular Structures from Rods and Rings and Are Structurally Associated with MAP2 and the Nuclear Envelope in Retinal Cells.
[So] Source:PLoS One;11(10):e0165162, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:"Rods and rings" (RR) and loukoumasomes are similarly shaped, subcellular macromolecular structures with as yet unknown function. RR, so named because of their shape, are formed in response to inhibition in the GTP or CTP synthetic pathways and are highly enriched in the two key enzymes of the nucleotide synthetic pathway. Loukoumasomes also occur as linear and toroidal bodies and were initially inferred to be the same as RR, largely due to their shared shape and size and the fact that it was unclear if they shared the same subcomponents. In human retinoblastoma tissue and cells we have observed toroidal, perinuclear, macromolecular structures of similar size and antigenicity to those previously reported in neurons (neuronal-loukoumasomes). To further characterize the subcomponents of the retinal-loukoumasomes, confocal analysis following immunocytochemical staining for alpha-tubulin, beta-III tubulin and detyrosinated tubulin was performed. These studies indicate that retinal-loukoumasomes are enriched for beta-III tubulin and other tubulins associated with microtubules. Immunofluorescence together with the in situ proximity ligation assay (PLA), confirmed that beta-III tubulin colocalized with detyrosinated tubulin within loukoumasomes. Our results indicate that these tissues contain only loukoumasomes because these macromolecular structures are immunoreactive with an anti-tubulin antibody but are not recognized by the prototype anti-RR/inosine monophosphate dehydrogenase (IMPDH) antibody (It2006). To further compare the RR and retinal-loukoumasomes, retinoblastoma cells were exposed to the IMPDH-inhibitor ribavirin, a drug known to induce the formation of RR. In contrast to RR, the production of retinal-loukoumasomes was unaffected. Coimmunostaining of Y79 cells for beta-III tubulin and IMPDH indicate that these cells, when treated with ribavirin, can contain both retinal-loukoumasomes and RR and that these structures are antigenically distinct. Subcellular fractionation studies indicate that ribavirin increased the RR subcomponent, IMPDH, in the nuclear fraction of Y79 cells from 21.3 ± 5.8% (0 mM ribavirin) to 122.8 ± 7.9% (1 mM ribavirin) while the subcellular localization of the retinal-loukoumasome subcomponent tubulin went unaltered. Further characterization of retinal-loukoumasomes in retinoblastoma cells reveals that they are intimately associated with lamin folds within the nuclear envelope. Using immunofluorescence and the in situ PLA in this cell type, we have observed colocalization of beta-III tubulin with MAP2. As MAP2 is a microtubule-associated protein implicated in microtubule crosslinking, this supports a role for microtubule crosslinkers in the formation of retinal-loukoumasomes. Together, these results suggest that loukoumasomes and RR are distinct subcellular macromolecular structures, formed by different cellular processes and that there are other loukoumasome-like structures within retinal tissues and cells.
[Mh] Termos MeSH primário: Estruturas Citoplasmáticas/metabolismo
Proteínas Associadas aos Microtúbulos/metabolismo
Microtúbulos/metabolismo
Membrana Nuclear/metabolismo
Retina/citologia
Retina/metabolismo
[Mh] Termos MeSH secundário: Neurônios Adrenérgicos/metabolismo
Animais
Linhagem Celular Tumoral
Seres Humanos
Imuno-Histoquímica
Laminas/metabolismo
Ligação Proteica
Transporte Proteico
Ratos
Retinoblastoma/metabolismo
Ribavirina/farmacologia
Tubulina (Proteína)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lamins); 0 (MAP2 protein, human); 0 (Microtubule-Associated Proteins); 0 (Tubulin); 49717AWG6K (Ribavirin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170616
[Lr] Data última revisão:
170616
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0165162


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[PMID]:27753025
[Au] Autor:Aucamp J; Bronkhorst AJ; Pretorius PJ
[Ad] Endereço:Centre for Human Metabolomics, Biochemistry Division, North-West University, Potchefstroom, 2520, South Africa. aucampj@telkomsa.net.
[Ti] Título:A Historical and Evolutionary Perspective on Circulating Nucleic Acids and Extracellular Vesicles: Circulating Nucleic Acids as Homeostatic Genetic Entities.
[So] Source:Adv Exp Med Biol;924:91-95, 2016.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The quantitative and qualitative differences of circulating nucleic acids (cirNAs) between healthy and diseased individuals have motivated researchers to utilize these differences in the diagnosis and prognosis of various pathologies. The position maintained here is that reviewing the rather neglected early work associated with cirNAs and extracellular vesicles (EVs) is required to fully describe the nature of cirNAs. This review consists of an empirically up-to-date schematic summary of the major events that developed and integrated the concepts of heredity, genetic information and cirNAs. This reveals a clear pattern implicating cirNA as a homeostatic entity or messenger of genetic information. The schematic summary paints a picture of how cirNAs may serve as homeostatic genetic entities that promote synchrony of both adaptation and damage in tissues and organs depending on the source of the message.
[Mh] Termos MeSH primário: Exossomos/genética
Vesículas Extracelulares/genética
Homeostase
Ácidos Nucleicos/genética
[Mh] Termos MeSH secundário: Evolução Biológica
Estruturas Citoplasmáticas/metabolismo
DNA/sangue
DNA/genética
DNA/secreção
Seres Humanos
Lipopolissacarídeos/secreção
Ácidos Nucleicos/sangue
Ácidos Nucleicos/secreção
RNA/sangue
RNA/genética
RNA/secreção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Lipopolysaccharides); 0 (Nucleic Acids); 63231-63-0 (RNA); 9007-49-2 (DNA)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161019
[St] Status:MEDLINE


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[PMID]:27753017
[Au] Autor:Garcia-Arranz M; Garcia-Olmo D; Vega-Clemente L; Stroun M; Gahan PB
[Ad] Endereço:Cell Therapy Laboratory, Instituto de Investigación Sanitaria-Fundación Jiménez Díaz, Avda Reyes Católicos 2, 28040, Madrid, Spain. maga65@gmail.com.
[Ti] Título:Non-dividing Cell Virtosomes Affect In Vitro and In Vivo Tumour Cell Replication.
[So] Source:Adv Exp Med Biol;924:43-45, 2016.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In vitro studies of partially purified virtosomes from rat liver showed inhibition of cell multiplication in four normal and two tumour cell lines. In vivo, the liver virtosomes slowed tumour growth and limited metastases in rats bearing DHD/K12-PROb cell initiated tumours.
[Mh] Termos MeSH primário: Proliferação Celular
Estruturas Citoplasmáticas/metabolismo
Neoplasias/metabolismo
Carga Tumoral
[Mh] Termos MeSH secundário: Animais
Divisão Celular
Linhagem Celular
Linhagem Celular Tumoral
Células Cultivadas
Estruturas Citoplasmáticas/transplante
Seres Humanos
Fígado/citologia
Fígado/metabolismo
Masculino
Camundongos
Metástase Neoplásica
Neoplasias/patologia
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161019
[St] Status:MEDLINE


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[PMID]:27018836
[Au] Autor:Santos HP; Barcellos MS; Reis AB; Dolder H; Lino-Neto J
[Ad] Endereço:Departamento de Biologia Geral, Universidade Federal de Viçosa-UFV, Minas Gerais, Brazil.
[Ti] Título:Sperm morphology of Muscidifurax uniraptor (Hymenoptera: Chalcidoidea: Pteromalidae).
[So] Source:Arthropod Struct Dev;45(3):307-10, 2016 May.
[Is] ISSN:1873-5495
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sperm morphology of the parasitoid Muscidifurax uniraptor was investigated under light and transmission electron microscopy. M. uniraptor sperm are filiform, spiraled, approximately 150 µm in length, with a distinctive head, hooded by an extracellular sheath and a flagellum. This extracellular layer, from which many filaments radiate, measures approximately 90 nm in thickness and covers a small acrosome and the anterior nuclear region. The acrosome is composed of an acrosomal vesicle and a perforatorium with its base inserted in the nuclear tip. The nucleus is filled with homogeneously compacted chromatin. The centriolar adjunct extends towards the anterior portion in a spiral around the nucleus for 3.5 µm in length. The two mitochondrial derivatives begin exactly at the centriole adjunct base and, in cross-section, have a circular shape with equal areas that are smaller than the axoneme diameter. It is coiled, with 9 + 9 + 2 microtubules and begins from the centriole, just below the nuclear base. The axoneme is connected to the mitochondrial derivatives by two small irregularly shaped masses. Between the derivatives and the axoneme, the 'center-flagellar material' is observed. Overall, these characteristics are recognized in other Chalcidoidea, especially in the eurytomids, but together they form a set of species-specific data.
[Mh] Termos MeSH primário: Espermatozoides/ultraestrutura
Vespas/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Estruturas Citoplasmáticas/ultraestrutura
Masculino
Microscopia Eletrônica de Transmissão
Especificidade da Espécie
Vespas/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170118
[Lr] Data última revisão:
170118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160329
[St] Status:MEDLINE


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[PMID]:26511517
[Au] Autor:Qiao Q; Wu H
[Ad] Endereço:Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, 02115, USA.
[Ti] Título:Supramolecular organizing centers (SMOCs) as signaling machines in innate immune activation.
[So] Source:Sci China Life Sci;58(11):1067-72, 2015 Nov.
[Is] ISSN:1869-1889
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:Innate immunity offers the first line of defense against infections and other types of danger such as tumorigenesis. Its discovery provides tremendous therapeutic opportunities for numerous human diseases. Delving into the structural basis of signal transduction by innate immune receptors, our lab has recently helped to establish the new paradigm in which innate immune receptors transduce ligand-binding signals through formation of higher-order assemblies containing intracellular adapters, signaling enzymes and their substrates. These large signalosome assemblies may be visible under light microscopy as punctate structures in the µm scale, connecting to the underlying molecular structures in the nm scale. They drive proximity-induced enzyme activation, and provide a mechanism for signaling amplification by nucleated polymerization. These supramolecular signaling complexes also open new questions on their cellular organization and mode of regulation, pose challenges to our methodology, and afford valuable implications in drug discovery against these medically important pathways.
[Mh] Termos MeSH primário: Estruturas Citoplasmáticas/imunologia
Imunidade Inata/imunologia
Complexos Multiproteicos/imunologia
Transdução de Sinais/imunologia
[Mh] Termos MeSH secundário: Animais
Estruturas Citoplasmáticas/química
Estruturas Citoplasmáticas/ultraestrutura
Seres Humanos
Microscopia Confocal
Microscopia Eletrônica
Modelos Moleculares
Complexos Multiproteicos/química
Complexos Multiproteicos/ultraestrutura
Polimerização
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Multiprotein Complexes)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151030
[St] Status:MEDLINE
[do] DOI:10.1007/s11427-015-4951-z


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[PMID]:26119829
[Au] Autor:García-Vázquez FA; Hernández-Caravaca I; Matás C; Soriano-Úbeda C; Abril-Sánchez S; Izquierdo-Rico MJ
[Ad] Endereço:Department of Physiology, Faculty of Veterinary Science, International Excellence Campus for Higher Education and Research "Campus Mare Nostrum", University of Murcia, Murcia 30100, Spain.
[Ti] Título:Morphological study of boar sperm during their passage through the female genital tract.
[So] Source:J Reprod Dev;61(5):407-13, 2015.
[Is] ISSN:1348-4400
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Once deposited in the female tract, sperm face a series of challenges that must be overcome to ensure the presence of an adequate normal sperm population close to the site of fertilization. Our aim was to evaluate the influence of the uterine milieu on boar sperm morphology. In experiment 1, sperm morphology was evaluated in the backflow (60 min after insemination) and within the uterotubal junction (UTJ) (collected ~24 h after insemination) following intrauterine sperm deposition (n = 6) and compared with the morphology of the sperm in the insemination dose. In experiment 2, the influence of the uterine fluid (UF) on sperm morphological modifications was evaluated. For this purpose, ejaculated (n = 4) and epididymal (n = 4) sperm were in vitro incubated with or without UF for 2 and 24 h. In both experiments, sperm were classified as normal, having a cytoplasmic droplet (proximal or distal) or having tail defects. The results of experiment 1 pointed to an increase in morphologically abnormal sperm collected in the backflow (27.70%) and a reduction of the same in the UTJ (2.12%) compared with the insemination dose (17.75%) (P < 0.05). In experiment 2, incubation of ejaculated sperm with UF did not provoke any morphological modifications; however, when epididymal sperm were incubated with UF, a pronounced increase in the percentage of normal sperm was evident after 24 h compared with the initial dose (from 25.77% to 53.58%, P < 0.05), mainly due to distal cytoplasmatic droplet shedding (53.22 vs. 20.20%). In conclusion, almost all the sperm that colonize the UTJ had a normal morphology, with part of the abnormal sperm having been discarded in the backflow and part selected/modified on their way to the oviduct. UF seems to influence cytoplasmic distal droplet removal, as demonstrated previously in seminal plasma.
[Mh] Termos MeSH primário: Secreções Corporais/fisiologia
Tubas Uterinas/fisiologia
Transporte Espermático
Espermatozoides/citologia
Sus scrofa/fisiologia
Útero/fisiologia
[Mh] Termos MeSH secundário: Matadouros
Animais
Animais Endogâmicos
Secreções Corporais/secreção
Forma Celular
Senescência Celular
Cruzamentos Genéticos
Estruturas Citoplasmáticas
Ejaculação
Epididimo/citologia
Tubas Uterinas/secreção
Feminino
Inseminação Artificial/veterinária
Masculino
Análise do Sêmen/veterinária
Espanha
Espermatozoides/fisiologia
Útero/secreção
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150630
[St] Status:MEDLINE
[do] DOI:10.1262/jrd.2014-170


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[PMID]:26081257
[Au] Autor:Pecci A; Necchi V; Barozzi S; Vitali A; Boveri E; Elena C; Bernasconi P; Noris P; Solcia E
[Ad] Endereço:Department of Internal Medicine, IRCCS Policlinico San Matteo Foundation and University of Pavia, Pavia, Italy. alessandro.pecci@unipv.it.
[Ti] Título:Particulate cytoplasmic structures with high concentration of ubiquitin-proteasome accumulate in myeloid neoplasms.
[So] Source:J Hematol Oncol;8:71, 2015 Jun 18.
[Is] ISSN:1756-8722
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Increased plasma levels of proteasome have been associated with various neoplasms, especially myeloid malignancies. Little is known of the cellular origin and release mechanisms of such proteasome. We recently identified and characterized a novel particulate cytoplasmic structure (PaCS) showing selective accumulation of ubiquitin-proteasome system (UPS) components. PaCSs have been reported in some epithelial neoplasms and in two genetic disorders characterized by hematopoietic cell dysplasia and increased risk of leukemia. However, no information is available about PaCSs in hematopoietic neoplasms. METHODS: PaCSs were investigated by ultrastructural, immunogold, and immunofluorescence analysis of bone marrow (BM) biopsies and peripheral blood (PB) cell preparations of 33 consecutive, untreated, or relapsed patients affected by different hematopoietic neoplasms. BM and PB samples from individuals with non-neoplastic BM or healthy donors were studied as controls. Granulocytes and platelet proteasome content was measured by immunoblotting and plasma proteasome levels by ELISA. RESULTS: PaCSs with typical, selective immunoreactivity for polyubiquitinated proteins and proteasome were widespread in granulocytic cells, megakaryocytes, and platelets of patients with myeloproliferative neoplasms (MPN). In acute myeloid leukemia and myelodysplastic syndromes (MDS), PaCSs were only occasionally detected in blast cells and were found consistently in cells showing granulocytic and megakaryocytic maturation. Conversely, PaCSs were poorly represented or absent in non-neoplastic hematopoietic tissue or lymphoid neoplasms. In MPN granulocytes and platelets, the presence of PaCSs was associated with increased amounts of proteasome in cell lysates. PaCSs were often localized in cytoplasmic blebs generating PaCSs-filled plasma membrane vesicles observable in the BM intercellular space. In MPN and MDS, accumulation of PaCSs was associated with significant increase in plasma proteasome. Immunogold analysis showed that PaCSs of myeloid neoplasia selectively concentrated the chaperone proteins Hsp40, Hsp70, and Hsp90. CONCLUSIONS: PaCSs accumulate in cells of myeloid neoplasms in a lineage- and maturation-restricted manner; in particular, they are widespread in granulocytic and megakaryocytic lineages of MPN patients. PaCSs development was associated with excess accumulation of polyubiquitinated proteins, proteasome, and chaperone molecules, indicating impairment of the UPS-dependent protein homeostasis and a possible link with Hsp90-related leukemogenesis. A mechanism of PaCSs discharge by leukemic cells could contribute to increased plasma proteasome of MPN and MDS.
[Mh] Termos MeSH primário: Transtornos Mieloproliferativos/genética
Complexo de Endopeptidases do Proteassoma/genética
Ubiquitina/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Pré-Escolar
Estruturas Citoplasmáticas
Feminino
Seres Humanos
Masculino
Meia-Idade
Transtornos Mieloproliferativos/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ubiquitin); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[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:150618
[St] Status:MEDLINE
[do] DOI:10.1186/s13045-015-0169-6


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[PMID]:25952156
[Au] Autor:Vanoli A; Necchi V; Barozzi S; Manca R; Pecci A; Solcia E
[Ad] Endereço:Pathologic Anatomy Section, Department of Diagnostic Medicine, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy.
[Ti] Título:Chaperone molecules concentrate together with the ubiquitin-proteasome system inside particulate cytoplasmic structures: possible role in metabolism of misfolded proteins.
[So] Source:Histochem Cell Biol;144(2):179-84, 2015 Aug.
[Is] ISSN:1432-119X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Ubiquitin-proteasome system (UPS) proteins and proteolytic activity are localized in a recently identified cytoplasmic structure characterized by accumulation of barrel-like particles, which is known as the particulate cytoplasmic structure (PaCS). PaCSs have been detected in neoplastic, preneoplastic, chronically infected, and fetal cells, which produce high amounts of misfolded proteins to be degraded by the UPS. Chaperone molecules are crucial in the early stages of handling misfolded proteins; therefore, we searched for these molecules in PaCSs. Heat shock proteins (Hsp), Hsp90, Hsp70, Hsp40, and Bcl-2-associated athanogene (Bag)3 chaperones, although not Bag6, were selectively concentrated into PaCSs of several cell lines and ex vivo fetal or neoplastic cells. Present findings point to PaCSs as an integrated, active UPS center well equipped for metabolism of misfolded proteins, especially in cells under physiological (fetal development) or pathological (neoplasia or inflammation) stress.
[Mh] Termos MeSH primário: Estruturas Citoplasmáticas/metabolismo
Proteínas de Choque Térmico/análise
Chaperonas Moleculares/análise
Complexo de Endopeptidases do Proteassoma/metabolismo
Dobramento de Proteína
Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Estruturas Citoplasmáticas/química
Proteínas de Choque Térmico/metabolismo
Seres Humanos
Imuno-Histoquímica
Lactente
Chaperonas Moleculares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (BAG2 protein, human); 0 (Heat-Shock Proteins); 0 (Molecular Chaperones); 0 (Ubiquitin); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150509
[St] Status:MEDLINE
[do] DOI:10.1007/s00418-015-1327-1


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[PMID]:25889896
[Au] Autor:Braun AC; Olayioye MA
[Ad] Endereço:University of Stuttgart, Institute of Cell Biology and Immunology, Allmandring 31, 70569 Stuttgart, Germany.
[Ti] Título:Rho regulation: DLC proteins in space and time.
[So] Source:Cell Signal;27(8):1643-51, 2015 Aug.
[Is] ISSN:1873-3913
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Rho GTPases function as molecular switches that connect changes of the external environment to intracellular signaling pathways. They are active at various subcellular sites and require fast and tight regulation to fulfill their role as transducers of extracellular stimuli. New imaging technologies visualizing the active states of Rho proteins in living cells elucidated the necessity of precise spatiotemporal activation of the GTPases. The local regulation of Rho proteins is coordinated by the interaction with different guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) that turn on and off GTPase signaling to downstream effectors. GEFs and GAPs thus serve as critical signaling nodes that specify the amplitude and duration of a particular Rho signaling pathway. Despite their importance in Rho regulation, the molecular aspects underlying the spatiotemporal control of the regulators themselves are still largely elusive. In this review we will focus on the Deleted in Liver Cancer (DLC) family of RhoGAP proteins and summarize the evidence gathered over the past years revealing their different subcellular localizations that might account for isoform-specific functions. We will also highlight the importance of their tightly controlled expression in the context of neoplastic transformation.
[Mh] Termos MeSH primário: Proteínas Ativadoras de GTPase/metabolismo
Transdução de Sinais
Proteínas Supressoras de Tumor/metabolismo
Proteínas rho de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/enzimologia
Núcleo Celular/enzimologia
Extensões da Superfície Celular/enzimologia
Transformação Celular Neoplásica/genética
Transformação Celular Neoplásica/metabolismo
Estruturas Citoplasmáticas/enzimologia
Proteínas Ativadoras de GTPase/genética
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Fatores de Troca de Nucleotídeo Guanina Rho/metabolismo
Fatores de Tempo
Proteínas Supressoras de Tumor/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (DLC1 protein, human); 0 (GTPase-Activating Proteins); 0 (Rho Guanine Nucleotide Exchange Factors); 0 (STARD13 protein, human); 0 (Tumor Suppressor Proteins); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150526
[Lr] Data última revisão:
150526
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150419
[St] Status:MEDLINE


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[PMID]:25759479
[Au] Autor:Astro V; de Curtis I
[Ad] Endereço:San Raffaele University and San Raffaele Scientific Institute, Cell Adhesion Laboratory, via Olgettina 58, 20132 Milano, Italy.
[Ti] Título:Plasma membrane-associated platforms: dynamic scaffolds that organize membrane-associated events.
[So] Source:Sci Signal;8(367):re1, 2015 Mar 10.
[Is] ISSN:1937-9145
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Specialized regions of the plasma membrane dedicated to diverse cellular processes, such as vesicle exocytosis, extracellular matrix remodeling, and cell migration, share a few cytosolic scaffold proteins that associate to form large plasma membrane-associated platforms (PMAPs). PMAPs organize signaling events and trafficking of membranes and molecules at specific membrane domains. On the basis of the intrinsic disorder of the proteins constituting the core of these PMAPs and of the dynamics of these structures at the periphery of motile cells, we propose a working model for the assembly and turnover of these platforms.
[Mh] Termos MeSH primário: Estruturas da Membrana Celular/fisiologia
Estruturas Citoplasmáticas/fisiologia
Proteínas Intrinsicamente Desordenadas/metabolismo
Proteínas de Membrana Transportadoras/fisiologia
Modelos Biológicos
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Estruturas da Membrana Celular/metabolismo
Estruturas Citoplasmáticas/metabolismo
Exocitose/genética
Exocitose/fisiologia
Proteínas da Matriz Extracelular/metabolismo
Adesões Focais/metabolismo
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Extracellular Matrix Proteins); 0 (Intrinsically Disordered Proteins); 0 (Membrane Transport Proteins)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150312
[St] Status:MEDLINE
[do] DOI:10.1126/scisignal.aaa3312



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