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[PMID]:28747344
[Au] Autor:Burbage M; Keppler SJ; Montaner B; Mattila PK; Batista FD
[Ad] Endereço:Lymphocyte Interaction Laboratory, Francis Crick Institute, London NW1 1AT, United Kingdom.
[Ti] Título:The Small Rho GTPase TC10 Modulates B Cell Immune Responses.
[So] Source:J Immunol;199(5):1682-1695, 2017 09 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rho family GTPases regulate diverse cellular events, such as cell motility, polarity, and vesicle traffic. Although a wealth of data exists on the canonical Rho GTPases RhoA, Rac1, and Cdc42, several other family members remain poorly studied. In B cells, we recently demonstrated a critical role for Cdc42 in plasma cell differentiation. In this study, we focus on a close homolog of Cdc42, TC10 (also known as RhoQ), and investigate its physiological role in B cells. By generating a TC10-deficient mouse model, we show that despite reduced total B cell numbers, B cell development in these mice occurs normally through distinct developmental stages. Upon immunization, IgM levels were reduced and, upon viral infection, germinal center responses were defective in TC10-deficient mice. BCR signaling was mildly affected, whereas cell migration remained normal in TC10-deficient B cells. Furthermore, by generating a TC10/Cdc42 double knockout mouse model, we found that TC10 can compensate for the lack of Cdc42 in TLR-induced cell activation and proliferation, so the two proteins play partly redundant roles. Taken together, by combining in vivo and in vitro analysis using TC10-deficient mice, we define the poorly studied Rho GTPase TC10 as an immunomodulatory molecule playing a role in physiological B cell responses.
[Mh] Termos MeSH primário: Linfócitos B/imunologia
Infecções por Orthomyxoviridae/imunologia
Vaccinia/imunologia
Proteína cdc42 de Ligação ao GTP/metabolismo
Proteínas rho de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Proliferação Celular
Células Cultivadas
Centro Germinativo/imunologia
Imunomodulação
Ativação Linfocitária
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Receptores de Antígenos de Linfócitos B/metabolismo
Transdução de Sinais
Proteína cdc42 de Ligação ao GTP/genética
Proteínas rho de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cdc42 protein, mouse); 0 (Receptors, Antigen, B-Cell); EC 3.6.1.- (Rhoq protein, mouse); EC 3.6.5.2 (cdc42 GTP-Binding Protein); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1602167


  2 / 5241 MEDLINE  
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[PMID]:28468989
[Au] Autor:D'Avino PP
[Ad] Endereço:Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK ppd21@cam.ac.uk.
[Ti] Título:Citron kinase - renaissance of a neglected mitotic kinase.
[So] Source:J Cell Sci;130(10):1701-1708, 2017 May 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cell division controls the faithful segregation of genomic and cytoplasmic materials between the two nascent daughter cells. Members of the Aurora, Polo and cyclin-dependent (Cdk) kinase families are known to regulate multiple events throughout cell division, whereas another kinase, citron kinase (CIT-K), for a long time has been considered to function solely during cytokinesis, the last phase of cell division. CIT-K was originally proposed to regulate the ingression of the cleavage furrow that forms at the equatorial cortex of the dividing cell after chromosome segregation. However, studies in the last decade have clarified that this kinase is, instead, required for the organization of the midbody in late cytokinesis, and also revealed novel functions of CIT-K earlier in mitosis and in DNA damage control. Moreover, CIT-K mutations have recently been linked to the development of human microcephaly, and CIT-K has been identified as a potential target in cancer therapy. In this Commentary, I describe and re-evaluate the functions and regulation of CIT-K during cell division and its involvement in human disease. Finally, I offer my perspectives on the open questions and future challenges that are necessary to address, in order to fully understand this important and yet unjustly neglected mitotic kinase.
[Mh] Termos MeSH primário: Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Mitose
Proteínas Serina-Treonina Quinases/metabolismo
[Mh] Termos MeSH secundário: Animais
Citocinese
Seres Humanos
Modelos Biológicos
Transdução de Sinais
Proteínas rho de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); EC 2.7.1.- (citron-kinase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.6.5.2 (rho GTP-Binding Proteins)
[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.200253


  3 / 5241 MEDLINE  
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[PMID]:27770342
[Au] Autor:Komatsu H; Iguchi T; Masuda T; Hirata H; Ueda M; Kidogami S; Ogawa Y; Sato K; Hu Q; Nambara S; Saito T; Sakimura S; Uchi R; Ito S; Eguchi H; Sugimachi K; Eguchi H; Doki Y; Mori M; Mimori K
[Ad] Endereço:Department of Surgery, Kyushu University Beppu Hospital, Beppu, Japan.
[Ti] Título:Attenuated RND1 Expression Confers Malignant Phenotype and Predicts Poor Prognosis in Hepatocellular Carcinoma.
[So] Source:Ann Surg Oncol;24(3):850-859, 2017 Mar.
[Is] ISSN:1534-4681
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The RND1 gene encodes a protein that belongs to the Rho GTPase family, which regulates various cellular functions. Depletion of RND1 expression activates the oncogenic Ras signaling pathway. In this study, we aimed to clarify the clinical significance of RND1 expression in predicting prognosis and to investigate its biological role in human hepatocellular carcinoma (HCC). METHODS: The association between RND1 expression and clinical outcomes in patients with HCC was analyzed in three independent cohorts: 120 cases resected in our hospital; 370 cases in The Cancer Genome Atlas (TCGA); and 242 cases in GSE14520. Gene set enrichment analysis (GSEA) was also conducted. Finally, knockdown experiments were performed using small interfering RNA (siRNA) in vitro. RESULTS: In all cohorts, RND1 expression was decreased as cancer progressed, and was affected by promoter methylation. In our HCC cases, the 5-year overall survival (OS) and recurrence-free survival of patients with low RND1 expression was significantly poorer than those of patients with high RND1 expression. TCGA and GSE14520 analyses provided similar results for OS. Multivariate analysis indicated that RND1 expression was an independent prognostic factor for OS in all three cohorts. Additionally, GSEA showed an inverse correlation between RND1 expression and the Ras signaling activity. In vitro, knockdown of RND1 expression resulted in significant increases in proliferation, invasion, and chemoresistance to cisplatin in HCC cells. CONCLUSIONS: Reduced RND1 expression in HCC was associated with cancer progression, likely through regulation of the Ras signaling pathway, and may serve as a novel clinical biomarker for predicting prognosis in patients with HCC.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/genética
Neoplasias Hepáticas/genética
Proteínas rho de Ligação ao GTP/genética
Proteínas rho de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Idoso
Carcinoma Hepatocelular/patologia
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Metilação de DNA
Bases de Dados Genéticas
Progressão da Doença
Intervalo Livre de Doença
Resistência a Medicamentos Antineoplásicos/genética
Feminino
Seguimentos
Expressão Gênica
Técnicas de Silenciamento de Genes
Seres Humanos
Neoplasias Hepáticas/patologia
Masculino
Meia-Idade
Fenótipo
Prognóstico
Regiões Promotoras Genéticas
Transdução de Sinais/genética
Taxa de Sobrevida
Proteínas ras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RND1 protein, human); EC 3.6.5.2 (ras Proteins); EC 3.6.5.2 (rho GTP-Binding Proteins)
[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:161023
[St] Status:MEDLINE
[do] DOI:10.1245/s10434-016-5573-9


  4 / 5241 MEDLINE  
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[PMID]:29330353
[Au] Autor:Azizoglu DB; Braitsch C; Marciano DK; Cleaver O
[Ad] Endereço:Department of Molecular Biology, Center for Regenerative Science and Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
[Ti] Título:Afadin and RhoA control pancreatic endocrine mass via lumen morphogenesis.
[So] Source:Genes Dev;31(23-24):2376-2390, 2017 12 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proper lumen morphogenesis during pancreas development is critical to endocrine and exocrine cell fate. Recent studies showed that a central network of lumens (termed core), but not the surrounding terminal branches (termed periphery), produces most islet endocrine cells. To date, it remains unclear how pancreatic lumens form and remodel and which aspects of lumen morphogenesis influence cell fate. Importantly, models testing the function of the central lumen network as an endocrine niche are lacking. Here, we identify mechanisms underlying lumen formation and remodeling and show that central lumen network morphogenesis impacts pancreatic endocrine mass. We show that loss of the scaffolding protein Afadin disrupts de novo lumenogenesis and lumen continuity in the tip epithelium. Codepletion of the actomyosin regulator RhoA and Afadin results in defects in the central lumens and arrests lumen remodeling. This arrest leads to prolonged perdurance of the central lumen network over developmental time and expansion of the endocrine progenitor population and, eventually, endocrine mass. Our study uncovers essential roles of Afadin and RhoA in pancreatic central lumen morphogenesis, which subsequently determines endocrine cell mass.
[Mh] Termos MeSH primário: Proteínas dos Microfilamentos/metabolismo
Morfogênese/genética
Pâncreas/embriologia
Proteínas rho de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Membrana Celular/metabolismo
Células Endócrinas/citologia
Células Endócrinas/metabolismo
Células Endócrinas/ultraestrutura
Camundongos
Proteínas dos Microfilamentos/genética
Microscopia Eletrônica de Transmissão
Mutação
Pâncreas/citologia
Pâncreas/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 (Microfilament Proteins); 0 (afadin); EC 3.6.5.2 (RhoA protein, mouse); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180114
[St] Status:MEDLINE
[do] DOI:10.1101/gad.307637.117


  5 / 5241 MEDLINE  
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[PMID]:27770373
[Au] Autor:Gómez-Contreras P; Ramiro-Díaz JM; Sierra A; Stipp C; Domann FE; Weigel RJ; Lal G
[Ad] Endereço:Division of Surgical Oncology and Endocrine Surgery, Department of Surgery, University of Iowa, 200 Hawkins Drive, 4641 JCP, Iowa City, IA, 52242, USA.
[Ti] Título:Extracellular matrix 1 (ECM1) regulates the actin cytoskeletal architecture of aggressive breast cancer cells in part via S100A4 and Rho-family GTPases.
[So] Source:Clin Exp Metastasis;34(1):37-49, 2017 01.
[Is] ISSN:1573-7276
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:ECM1 overexpression is an independent predictor of poor prognosis in primary breast carcinomas, however the mechanisms by which ECM1 affects tumor progression have not been completely elucidated. ECM1 was silenced in the triple-negative breast cancer cell lines Hs578T and MDAMB231 using siRNA and the cells were evaluated for changes in morphology, migration, invasion and adhesion. Actin cytoskeleton alterations were evaluated by fluorescent staining and levels of activated Rho GTPases by pull down assays. ECM1 downregulation led to significantly diminished cell migration (p = 0.0005 for Hs578T and p = 0.02 for MDAMB231) and cell adhesion (p < 0.001 for Hs578T and p = 0.01 for MDAMB231). Cell invasion (matrigel) was reduced only in the Hs578T cells (p < 0.01). Silencing decreased the expression of the prometastatic molecules S100A4 and TGFßR2 in both cell lines and CD44 in Hs578T cells. ECM1-silenced cells also exhibited alterations in cell shape and showed bundles of F-actin across the cell (stress fibers) whereas NT-siRNA treated cells showed peripheral membrane ruffling. Downregulation of ECM1 was also associated with an increased F/G actin ratio, when compared to the cells transfected with NT siRNA (p < 0.001 for Hs578T and p < 0.00035 for MDAMB231) and a concomitant decline of activated Rho A in the Hs578T cells. Re-expression of S100A4 in ECM1-silenced cells rescued the phenotype in the Hs578T cells but not the MDAMB231 cells. We conclude that ECM1 is a key player in the metastatic process and regulates the actin cytoskeletal architecture of aggressive breast cancer cells at least in part via alterations in S100A4 and Rho A.
[Mh] Termos MeSH primário: Proteínas da Matriz Extracelular/genética
Proteínas Serina-Treonina Quinases/biossíntese
Receptores de Fatores de Crescimento Transformadores beta/biossíntese
Proteína A4 de Ligação a Cálcio da Família S100/biossíntese
Neoplasias de Mama Triplo Negativas/genética
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/genética
Adesão Celular/genética
Linhagem Celular Tumoral
Movimento Celular/genética
Colágeno
Combinação de Medicamentos
Matriz Extracelular/genética
Proteínas da Matriz Extracelular/biossíntese
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Receptores de Hialuronatos/genética
Laminina
Invasividade Neoplásica/genética
Invasividade Neoplásica/patologia
Proteínas Serina-Treonina Quinases/genética
Proteoglicanas
Receptores de Fatores de Crescimento Transformadores beta/genética
Proteína A4 de Ligação a Cálcio da Família S100/genética
Neoplasias de Mama Triplo Negativas/patologia
Proteínas rho de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Drug Combinations); 0 (ECM1 protein, human); 0 (Extracellular Matrix Proteins); 0 (Hyaluronan Receptors); 0 (Laminin); 0 (Proteoglycans); 0 (Receptors, Transforming Growth Factor beta); 0 (S100 Calcium-Binding Protein A4); 119978-18-6 (matrigel); 142662-27-9 (S100A4 protein, human); 9007-34-5 (Collagen); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.30 (transforming growth factor-beta type II receptor); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:180101
[Lr] Data última revisão:
180101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE
[do] DOI:10.1007/s10585-016-9827-5


  6 / 5241 MEDLINE  
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[PMID]:29207896
[Au] Autor:Chaker M; Minden A; Chen S; Weiss RH; Chini EN; Mahipal A; Azmi AS
[Ad] Endereço:a Department of Oncology , Wayne State University School of Medicine, Karmanos Cancer Institute , Detroit , MI , USA.
[Ti] Título:Rho GTPase effectors and NAD metabolism in cancer immune suppression.
[So] Source:Expert Opin Ther Targets;22(1):9-17, 2018 Jan.
[Is] ISSN:1744-7631
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Sustained proliferative signaling and de-regulated cellular bioenergetics are two of the chief hallmarks of cancer. Alterations in the Ras pathway and its downstream effectors are among the major drivers for uncontrolled cell growth in many cancers. The GTPases are one of the signaling molecules that activate crucial signal transducing pathways downstream of Ras through several effector proteins. The GTPases (GTP bound) interact with several effectors and modulate a number of different biological pathways including those that regulate cytoskeleton, cellular motility, cytokinesis, proliferation, apoptosis, transcription and nuclear signaling. Similarly, the altered glycolytic pathway, the so-called 'Warburg effect', rewires tumor cell metabolism to support the biosynthetic requirements of uncontrolled proliferation. There exists strong evidence for the critical role of the glycolytic pathway's rate limiting enzymes in promoting immunosuppression. Areas covered: We review the emerging roles of GTPase effector proteins particularly the p21 activated kinase 4 (PAK4) and nicotinamide biosynthetic pathway enzyme nicotinamide phosphoribosyltransferase (NAMPT) as signaling molecules in immune surveillance and the immune response. Expert opinion: In this expert opinion article we highlight the recent information on the role of GTPases and the metabolic enzymes on the immune microenvironment and propose some unique immune therapeutic opportunities.
[Mh] Termos MeSH primário: NAD/metabolismo
Neoplasias/imunologia
Proteínas rho de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Imunoterapia/métodos
NAD/imunologia
Neoplasias/terapia
Transdução de Sinais/imunologia
Microambiente Tumoral/imunologia
Proteínas rho de Ligação ao GTP/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0U46U6E8UK (NAD); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1080/14728222.2018.1413091


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[PMID]:28468978
[Au] Autor:Valdivia A; Goicoechea SM; Awadia S; Zinn A; Garcia-Mata R
[Ad] Endereço:Department of Biological Sciences, University of Toledo, Toledo, OH 43606.
[Ti] Título:Regulation of circular dorsal ruffles, macropinocytosis, and cell migration by RhoG and its exchange factor, Trio.
[So] Source:Mol Biol Cell;28(13):1768-1781, 2017 Jul 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Circular dorsal ruffles (CDRs) are actin-rich structures that form on the dorsal surface of many mammalian cells in response to growth factor stimulation. CDRs represent a unique type of structure that forms transiently and only once upon stimulation. The formation of CDRs involves a drastic rearrangement of the cytoskeleton, which is regulated by the Rho family of GTPases. So far, only Rac1 has been consistently associated with CDR formation, whereas the role of other GTPases in this process is either lacking or inconclusive. Here we show that RhoG and its exchange factor, Trio, play a role in the regulation of CDR dynamics, particularly by modulating their size. RhoG is activated by Trio downstream of PDGF in a PI3K- and Src-dependent manner. Silencing RhoG expression decreases the number of cells that form CDRs, as well as the area of the CDRs. The regulation of CDR area by RhoG is independent of Rac1 function. In addition, our results show the RhoG plays a role in the cellular functions associated with CDR formation, including macropinocytosis, receptor internalization, and cell migration. Taken together, our results reveal a novel role for RhoG in the regulation of CDRs and the cellular processes associated with their formation.
[Mh] Termos MeSH primário: Fatores de Troca do Nucleotídeo Guanina/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas rho de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Linhagem Celular
Estruturas da Membrana Celular/metabolismo
Estruturas da Membrana Celular/fisiologia
Movimento Celular/fisiologia
Citoesqueleto/metabolismo
Seres Humanos
Microtúbulos/metabolismo
Fosfatidilinositol 3-Quinases/metabolismo
Pinocitose/fisiologia
Ratos
Proteínas rac1 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Guanine Nucleotide Exchange Factors); 147605-13-8 (RHOG protein, human); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (TRIO protein, human); EC 3.6.5.2 (rac1 GTP-Binding Protein); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171212
[Lr] Data última revisão:
171212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-06-0412


  8 / 5241 MEDLINE  
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[PMID]:29040270
[Au] Autor:Wylie T; Garg R; Ridley AJ; Conte MR
[Ad] Endereço:Randall Division of Cell and Molecular Biophysics, King's College London, Guy's Campus, London, United Kingdom.
[Ti] Título:Analysis of the interaction of Plexin-B1 and Plexin-B2 with Rnd family proteins.
[So] Source:PLoS One;12(10):e0185899, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Rnd family of proteins, Rnd1, Rnd2 and Rnd3, are atypical Rho family GTPases, which bind to but do not hydrolyse GTP. They interact with plexins, which are receptors for semaphorins, and are hypothesised to regulate plexin signalling. We recently showed that each Rnd protein has a distinct profile of interaction with three plexins, Plexin-B1, Plexin-B2 and Plexin-B3, in mammalian cells, although it is unclear which region(s) of these plexins contribute to this specificity. Here we characterise the binary interactions of the Rnd proteins with the Rho-binding domain (RBD) of Plexin-B1 and Plexin-B2 using biophysical approaches. Isothermal titration calorimetry (ITC) experiments for each of the Rnd proteins with Plexin-B1-RBD and Plexin-B2-RBD showed similar association constants for all six interactions, although Rnd1 displayed a small preference for Plexin-B1-RBD and Rnd3 for Plexin-B2-RBD. Furthermore, mutagenic analysis of Rnd3 suggested similarities in its interaction with both Plexin-B1-RBD and Plexin-B2-RBD. These results suggest that Rnd proteins do not have a clear-cut specificity for different Plexin-B-RBDs, possibly implying the contribution of additional regions of Plexin-B proteins in conferring functional substrate selection.
[Mh] Termos MeSH primário: Proteínas do Tecido Nervoso/metabolismo
Moléculas de Adesão de Célula Nervosa/metabolismo
Receptores de Superfície Celular/metabolismo
Proteínas rho de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação
Células COS
Calorimetria/métodos
Cercopithecus aethiops
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Cinética
Mutação
Proteínas do Tecido Nervoso/genética
Moléculas de Adesão de Célula Nervosa/genética
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Receptores de Superfície Celular/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Termodinâmica
Proteínas rho de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nerve Tissue Proteins); 0 (Neural Cell Adhesion Molecules); 0 (PLXNB1 protein, human); 0 (PLXNB3 protein, human); 0 (RND1 protein, human); 0 (Receptors, Cell Surface); 0 (Recombinant Proteins); 0 (plexin B2 protein, human); EC 3.6.5.2 (RND2 protein, human); EC 3.6.5.2 (RND3 protein, human); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185899


  9 / 5241 MEDLINE  
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[PMID]:28953959
[Au] Autor:Kim J; Montagne K; Nemoto H; Ushida T; Furukawa KS
[Ad] Endereço:Department of Mechanical Engineering, Graduate School of Engineering, University of Tokyo, Tokyo, Japan.
[Ti] Título:Hypergravity down-regulates c-fos gene expression via ROCK/Rho-GTP and the PI3K signaling pathway in murine ATDC5 chondroprogenitor cells.
[So] Source:PLoS One;12(9):e0185394, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chondrocytes are known to be physiologically loaded with diverse physical factors such as compressive stress, shear stress and hydrostatic pressure. Although the effects of those mechanical stimuli onto various cell models have been widely studied, those of hypergravity have not yet been revealed clearly. Hereby, we hypothesized that the hypergravity affects relative positions of intracellular elements including nucleus and cytoskeletons due to their density differences, triggering mechanotransduction in the cell. The aim of this study was to investigate the effect of hypergravity on c-fos expression in the murine ATDC5 chondroprogenitor cells, as c-fos is a well known key regulator of cell proliferation and differentiation, including in chondrocytes. We first found that hypergravity down-regulated c-fos expression transiently via ROCK/Rho-GTP and PI3K signaling, and the down-regulation was suppressed by inhibition of actin polymerization.
[Mh] Termos MeSH primário: Condrócitos/citologia
Regulação para Baixo
Guanosina Trifosfato/metabolismo
Hipergravidade
Fosfatidilinositol 3-Quinases/metabolismo
Proteínas Proto-Oncogênicas c-fos/genética
Proteínas rho de Ligação ao GTP/metabolismo
Quinases Associadas a rho/metabolismo
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Androstadienos/farmacologia
Animais
Linhagem Celular
Condrócitos/efeitos dos fármacos
Condrócitos/metabolismo
Regulação para Baixo/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Camundongos
Modelos Biológicos
Proteínas Proto-Oncogênicas c-fos/metabolismo
Transdução de Sinais/efeitos dos fármacos
Células-Tronco/citologia
Células-Tronco/efeitos dos fármacos
Células-Tronco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Androstadienes); 0 (Proto-Oncogene Proteins c-fos); 86-01-1 (Guanosine Triphosphate); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (rho-Associated Kinases); EC 3.6.5.2 (rho GTP-Binding Proteins); XVA4O219QW (wortmannin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170928
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185394


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[PMID]:28920922
[Au] Autor:Koo JH; Kim TH; Park SY; Joo MS; Han CY; Choi CS; Kim SG
[Ad] Endereço:College of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University, Seoul, South Korea.
[Ti] Título:Gα13 ablation reprograms myofibers to oxidative phenotype and enhances whole-body metabolism.
[So] Source:J Clin Invest;127(10):3845-3860, 2017 Oct 02.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Skeletal muscle is a key organ in energy homeostasis owing to its high requirement for nutrients. Heterotrimeric G proteins converge signals from cell-surface receptors to potentiate or blunt responses against environmental changes. Here, we show that muscle-specific ablation of Gα13 in mice promotes reprogramming of myofibers to the oxidative type, with resultant increases in mitochondrial biogenesis and cellular respiration. Mechanistically, Gα13 and its downstream effector RhoA suppressed nuclear factor of activated T cells 1 (NFATc1), a chief regulator of myofiber conversion, by increasing Rho-associated kinase 2-mediated (Rock2-mediated) phosphorylation at Ser243. Ser243 phosphorylation of NFATc1 was reduced after exercise, but was higher in obese animals. Consequently, Gα13 ablation in muscles enhanced whole-body energy metabolism and increased insulin sensitivity, thus affording protection from diet-induced obesity and hepatic steatosis. Our results define Gα13 as a switch regulator of myofiber reprogramming, implying that modulations of Gα13 and its downstream effectors in skeletal muscle are a potential therapeutic approach to treating metabolic diseases.
[Mh] Termos MeSH primário: Metabolismo Energético
Fígado Gorduroso/metabolismo
Subunidades alfa G12-G13 de Proteínas de Ligação ao GTP/metabolismo
Miofibrilas/metabolismo
Obesidade/metabolismo
[Mh] Termos MeSH secundário: Animais
Fígado Gorduroso/genética
Subunidades alfa G12-G13 de Proteínas de Ligação ao GTP/genética
Camundongos
Camundongos Knockout
Miofibrilas/genética
Fatores de Transcrição NFATC/genética
Fatores de Transcrição NFATC/metabolismo
Obesidade/genética
Proteínas rho de Ligação ao GTP/genética
Proteínas rho de Ligação ao GTP/metabolismo
Quinases Associadas a rho/genética
Quinases Associadas a rho/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NFATC Transcription Factors); 0 (Nfatc1 protein, mouse); EC 2.7.11.1 (Rock2 protein, mouse); EC 2.7.11.1 (rho-Associated Kinases); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, G12-G13); EC 3.6.5.2 (RhoA protein, mouse); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE



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