Base de dados : MEDLINE
Pesquisa : D08.811.277.040.330.300.400.400.150 [Categoria DeCS]
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[PMID]:28604748
[Au] Autor:Do MT; Chai TF; Casey PJ; Wang M
[Ad] Endereço:Program in Cancer and Stem Cell Biology, Duke-NUS Graduate Medical School, Singapore.
[Ti] Título:Isoprenylcysteine carboxylmethyltransferase function is essential for RAB4A-mediated integrin ß3 recycling, cell migration and cancer metastasis.
[So] Source:Oncogene;36(41):5757-5767, 2017 Oct 12.
[Is] ISSN:1476-5594
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Isoprenylcysteine carboxylmethyltransferase (ICMT) catalyzes the post-translational modification of RAB GTPases that contain C-terminal CXC motifs. However, the functional impact of this modification on RAB proteins has not been actively explored. We found that inhibition of ICMT significantly reduced cell migration in vitro and cancer invasion and metastasis in vivo. This role of ICMT was found to be mediated by RAB4A, an essential regulator of the fast recycling of integrin ß3. Integrin ß3 regulates cell polarity and migration when localized appropriately to the plasma membrane, thereby having an essential role in cancer metastasis. ICMT catalyzed carboxylmethylation is critical for RAB4A activation and interaction with effectors, its localization to endosomes and recycling vesicles, and hence important for RAB4A-dependent integrin ß3 recycling to plasma membrane. These findings bring attention to the effects of C-terminal carboxylmethylation on RAB GTPases and provide a rationale for targeting ICMT in the treatment of metastatic cancer.
[Mh] Termos MeSH primário: Integrina beta3/genética
Neoplasias/genética
Metiltransferases de Proteína/genética
Proteínas rab4 de Ligação ao GTP/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Movimento Celular/genética
Polaridade Celular
Galinhas
Endossomos/enzimologia
Seres Humanos
Integrina beta3/metabolismo
Camundongos
Invasividade Neoplásica/genética
Invasividade Neoplásica/patologia
Metástase Neoplásica
Neoplasias/fisiopatologia
Metiltransferases de Proteína/metabolismo
Processamento de Proteína Pós-Traducional
Proteínas rab4 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin beta3); EC 2.1.1.- (Protein Methyltransferases); EC 2.1.1.100 (protein-S-isoprenylcysteine O-methyltransferase); EC 3.6.5.2 (rab4 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:170613
[St] Status:MEDLINE
[do] DOI:10.1038/onc.2017.183


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[PMID]:28191740
[Au] Autor:Blaszczyk M; Gajewska M; Milewska M; Grzelkowska-Kowalczyk K
[Ad] Endereço:Faculty of Veterinary Medicine, Department of Physiological Sciences, Warsaw University of Life Sciences (SGGW), Nowoursynowska 159, Warsaw 02-776, Poland.
[Ti] Título:Insulin-dependent cytoplasmic distribution of Rab4a in mouse adipocytes is inhibited by interleukin-6, -8, and -15.
[So] Source:Cell Biol Int;41(4):457-463, 2017 Apr.
[Is] ISSN:1095-8355
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The purpose of the study was to examine the effect of interleukins, IL-6, IL-8, and IL-15, on insulin-mediated redistribution of Rab4a, an early endosome marker, in mouse 3T3-L1 adipocytes. The interleukins did not affect cell viability; however, cell number was slightly but significantly higher in cultures exposed to IL-8 and IL-15. IL-8 and IL-15 decreased lipid storage in adipocytes, whereas IL-6 had no effect. Rab4A showed cytoplasmic localization, and in control unstimulated adipocytes it was found primarily nearby nucleus, that was supported by cellular fluorescence distribution profile, and by calculated indices, that is, high percentage of near-nuclear area fluorescence and a low mean peripheral cytoplasmic fluorescence/mean near-nuclear fluorescence ratio. Insulin stimulation (100 nmol/l, 30 min) altered the cytoplasmic localization of Rab4a in control adipocytes, which was manifested by its redistribution towards plasma membrane. This effect of insulin was prevented in adipocytes exposed to IL-6, IL-8, or IL-15. We concluded that insulin-dependent Rab4a redistribution, probably reflecting stimulation of vesicle-mediated transport, is inhibited in adipocytes subjected to differentiation in the presence of IL-6, IL-8, or IL-15. Such alterations may be involved in the mechanisms contributing to development of insulin resistance associated with inflammation; however, further studies in this field are required.
[Mh] Termos MeSH primário: Adipócitos/enzimologia
Insulina/fisiologia
Interleucina-6/fisiologia
Interleucina-8/fisiologia
Proteínas rab4 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Células 3T3-L1
Animais
Citoplasma/enzimologia
Interleucina-15/fisiologia
Camundongos
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insulin); 0 (Interleukin-15); 0 (Interleukin-6); 0 (Interleukin-8); EC 3.6.5.2 (rab4 GTP-Binding Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170327
[Lr] Data última revisão:
170327
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170214
[St] Status:MEDLINE
[do] DOI:10.1002/cbin.10743


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[PMID]:28031320
[Au] Autor:Schulze U; Brast S; Grabner A; Albiker C; Snieder B; Holle S; Schlatter E; Schröter R; Pavenstädt H; Herrmann E; Lambert C; Spoden GA; Florin L; Saftig P; Ciarimboli G
[Ad] Endereço:Medizinische Klinik D, Experimentelle Nephrologie, and.
[Ti] Título:Tetraspanin CD63 controls basolateral sorting of organic cation transporter 2 in renal proximal tubules.
[So] Source:FASEB J;31(4):1421-1433, 2017 Apr.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CD63 is a ubiquitously expressed member of the tetraspanin superfamily. Using a mating-based split-ubiquitin-yeast 2-hybrid system, pull-down experiments, total internal reflection fluorescence microscopy, Förster resonance energy transfer, and biotinylation assays, we found that CD63 interacts with human organic cation transporter 2 (hOCT2), which transports endogenous and exogenous substrates, such as neurotransmitters and drugs in several epithelial cells. CD63 overexpression affects cellular localization of hOCT2 expressed in human embryonic kidney (HEK)293 cells. Studies with CD63-knockout mice indicate that in renal proximal tubules, CD63 determines the insertion of the mouse ortholog of the transporter into the proper membrane domain and mediates transporter regulation by trafficking processes. In polarized Madin-Darby kidney canine kidney (MDCK) epithelial cells, CD63 and hOCT2 colocalize with the small GTPase Rab4, which controls the rapid recycling from sorting endosomes back to the cell surface. Suitable negative and positive control experiments were performed for each experimental approach. Empty vector transfected cells and wild-type mice were used as control. CD63 seems to play a role in the recycling of hOCT2 from endosomes to the basolateral membrane in polarized epithelia. These data indicate that CD63 has a previously uncharacterized function in regulating trafficking of specific membrane proteins in polarized cells.-Schulze, U., Brast, S., Grabner, A., Albiker, C., Snieder, B., Holle, S., Schlatter, E., Schröter, R., Pavenstädt, H., Herrmann, E., Lambert, C., Spoden, G. A., Florin, L., Saftig, P., Ciarimboli, G. Tetraspanin CD63 controls basolateral sorting of organic cation transporter 2 in renal proximal tubules.
[Mh] Termos MeSH primário: Túbulos Renais Proximais/metabolismo
Proteínas de Transporte de Cátions Orgânicos/metabolismo
Tetraspanina 30/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Cães
Endossomos/metabolismo
Células Epiteliais/metabolismo
Células HEK293
Seres Humanos
Túbulos Renais Proximais/citologia
Células Madin Darby de Rim Canino
Camundongos
Camundongos Endogâmicos C57BL
Transportador 2 de Cátion Orgânico
Ligação Proteica
Transporte Proteico
Tetraspanina 30/genética
Proteínas rab4 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Organic Cation Transport Proteins); 0 (Organic Cation Transporter 2); 0 (SLC22A2 protein, human); 0 (Tetraspanin 30); EC 3.6.5.2 (rab4 GTP-Binding Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161230
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201600901R


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[PMID]:27627840
[Au] Autor:Ho E; Ivanova IA; Dagnino L
[Ad] Endereço:Dept. of Physiology and Pharmacology, Children's Health Research Institute and Lawson Health Research Institute, University of Western Ontario, London, Ontario N6A 5C1, Canada.
[Ti] Título:Integrin-linked kinase and ELMO2 modulate recycling endosomes in keratinocytes.
[So] Source:Biochim Biophys Acta;1863(12):2892-2904, 2016 12.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The formation of tight cell-cell junctions is essential in the epidermis for its barrier properties. In this tissue, keratinocytes follow a differentiation program tightly associated with their movement from the innermost basal to the outer suprabasal layers, and with changes in their cell-cell adhesion profile. Intercellular adhesion in keratinocytes is mediated through cell-cell contacts, including E-cadherin-based adherens junctions. Although the mechanisms that mediate E-cadherin delivery to the plasma membrane have been widely studied in simple epithelia, this process is less well understood in the stratified epidermis. In this study, we have investigated the role of Engulfment and Cell Motility 2 (ELMO2) and integrin-linked kinase (ILK) in the positioning of E-cadherin-containing recycling endosomes during establishment of cell-cell contacts in differentiating keratinocytes. We now show that induction of keratinocyte differentiation by Ca is accompanied by localization of ELMO2 and ILK to Rab4- and Rab11a-containing recycling endosomes. The positioning of long-loop Rab11a-positive endosomes at areas adjacent to cell-cell contacts is disrupted in ELMO2- or ILK-deficient keratinocytes, and is associated with impaired localization of E-cadherin to cell borders. Our studies show a previously unrecognized role for ELMO2 and ILK in modulation of endosomal positioning, which may play key roles in epidermal sheet maintenance and permeability barrier function.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Junções Aderentes/metabolismo
Caderinas/genética
Proteínas do Citoesqueleto/genética
Endossomos/metabolismo
Queratinócitos/metabolismo
Proteínas Serina-Treonina Quinases/genética
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/deficiência
Junções Aderentes/ultraestrutura
Animais
Animais Recém-Nascidos
Caderinas/metabolismo
Cálcio/metabolismo
Adesão Celular
Diferenciação Celular
Membrana Celular/metabolismo
Membrana Celular/ultraestrutura
Proteínas do Citoesqueleto/deficiência
Endossomos/ultraestrutura
Epiderme/citologia
Epiderme/metabolismo
Expressão Gênica
Queratinócitos/citologia
Camundongos
Camundongos Transgênicos
Cultura Primária de Células
Transporte Proteico
Proteínas Serina-Treonina Quinases/deficiência
Transdução de Sinais
Proteínas rab de Ligação ao GTP/genética
Proteínas rab de Ligação ao GTP/metabolismo
Proteínas rab4 de Ligação ao GTP/genética
Proteínas rab4 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Cadherins); 0 (Cytoskeletal Proteins); 0 (E-cadherin protein, mouse); 0 (Elmo2 protein, mouse); EC 2.7.1.- (integrin-linked kinase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.6.1.- (rab11 protein); EC 3.6.5.2 (rab GTP-Binding Proteins); EC 3.6.5.2 (rab4 GTP-Binding Proteins); SY7Q814VUP (Calcium)
[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:160916
[St] Status:MEDLINE


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[PMID]:26716952
[Au] Autor:Yao P; Zhao H; Mo W; He P
[Ad] Endereço:1 ICU of the Affiliated Nanhua Hospital of University of South China , Hengyang, China .
[Ti] Título:Laminar Shear Stress Promotes Vascular Endothelial Cell Autophagy Through Upregulation with Rab4.
[So] Source:DNA Cell Biol;35(3):118-23, 2016 Mar.
[Is] ISSN:1557-7430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Laminar shear stress is considered to improve endothelial cell (EC) function. However, the underlying mechanism is unclear. Autophagy has been found to protect cell survival under stress. In this study, the effect of laminar shear stress on EC autophagy and its potential mechanism were explored. The autophagic markers, Beclin 1 and LC3 II, in human umbilical vascular endothelial cells increased after laminar shear stress treatment. Meanwhile, the autophagic substrate, p62, decreased. The protein level of Rab4 increased under laminar shear stress. When pretreated with Rab4 siRNA, the increased levels of Beclin 1 and LC3 II were attenuated and p62 levels significantly increased. In addition, the MCP level and the adhesion of monocytes were also obviously increased by Rab4 siRNA. Laminar shear stress upregulated Rab4 expression, which contributed to improved EC autophagy and function.
[Mh] Termos MeSH primário: Autofagia/fisiologia
Endotélio Vascular/fisiologia
Proteínas rab4 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Proteínas Reguladoras de Apoptose/metabolismo
Beclina-1
Quimiocina CCL2/metabolismo
Endotélio Vascular/citologia
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Proteínas de Membrana/metabolismo
Proteínas Associadas aos Microtúbulos/metabolismo
Regulação para Cima
Proteínas rab4 de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoptosis Regulatory Proteins); 0 (BECN1 protein, human); 0 (Beclin-1); 0 (CCL2 protein, human); 0 (Chemokine CCL2); 0 (Membrane Proteins); 0 (Microtubule-Associated Proteins); 0 (light chain 3, human); EC 3.6.5.2 (rab4 GTP-Binding Proteins)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151231
[St] Status:MEDLINE
[do] DOI:10.1089/dna.2015.3041


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[PMID]:26617273
[Au] Autor:Takeuchi H; Takada A; Kuboniwa M; Amano A
[Ad] Endereço:Department of Preventive Dentistry, Osaka University Graduate School of Dentistry, Suita-Osaka, 565-0871, Japan.
[Ti] Título:Intracellular periodontal pathogen exploits recycling pathway to exit from infected cells.
[So] Source:Cell Microbiol;18(7):928-48, 2016 07.
[Is] ISSN:1462-5822
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Although human gingival epithelium prevents intrusions by periodontal bacteria, Porphyromonas gingivalis, the most well-known periodontal pathogen, is able to invade gingival epithelial cells and pass through the epithelial barrier into deeper tissues. We previously reported that intracellular P. gingivalis exits from gingival epithelial cells via a recycling pathway. However, the underlying molecular process remains unknown. In the present study, we found that the pathogen localized in early endosomes recruits VAMP2 and Rab4A. VAMP2 was found to be specifically localized in early endosomes, although its localization remained unclear in mammalian cells. A single transmembrane domain of VAMP2 was found to be necessary and sufficient for localizing in early endosomes containing P. gingivalis in gingival epithelial cells. VAMP2 forms a complex with EXOC2/Sec5 and EXOC3/Sec6, whereas Rab4A mediates dissociation of the EXOC complex followed by recruitment of RUFY1/Rabip4, Rab4A effector, and Rab14. Depletion of VAMP2 or Rab4A resulted in accumulation of bacteria in early endosomes and disturbed bacterial exit from infected cells. It is suggested that these novel dynamics allow P. gingivalis to exploit fast recycling pathways promoting further bacterial penetration of gingival tissues.
[Mh] Termos MeSH primário: Gengiva/microbiologia
Interações Hospedeiro-Patógeno/fisiologia
Porphyromonas gingivalis/patogenicidade
Proteína 2 Associada à Membrana da Vesícula/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Infecções por Bacteroidaceae/metabolismo
Infecções por Bacteroidaceae/microbiologia
Transporte Biológico
Endossomos/metabolismo
Células Epiteliais/metabolismo
Células Epiteliais/microbiologia
Gengiva/metabolismo
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Fosforilação
Domínios Proteicos
Proteína 2 Associada à Membrana da Vesícula/genética
Proteínas de Transporte Vesicular/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
Proteínas rab4 de Ligação ao GTP/genética
Proteínas rab4 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (EXOC3 protein, human); 0 (Intracellular Signaling Peptides and Proteins); 0 (RUFY1 protein, human); 0 (Rabip4 protein, human); 0 (VAMP2 protein, human); 0 (Vesicle-Associated Membrane Protein 2); 0 (Vesicular Transport Proteins); EC 3.6.1.- (Rab14 protein, human); EC 3.6.5.2 (rab GTP-Binding Proteins); EC 3.6.5.2 (rab4 GTP-Binding Proteins)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170215
[Lr] Data última revisão:
170215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151201
[St] Status:MEDLINE
[do] DOI:10.1111/cmi.12551


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[PMID]:26484934
[Au] Autor:Stone R; Hayashi T; Bajimaya S; Hodges E; Takimoto T
[Ad] Endereço:Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Box 672 Rochester, NY 14642, USA.
[Ti] Título:Critical role of Rab11a-mediated recycling endosomes in the assembly of type I parainfluenza viruses.
[So] Source:Virology;487:11-8, 2016 Jan.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Paramyxoviruses replicate in the cytoplasm of infected cells and newly synthesized viral nucleocapsids (vRNPs) are transported to the plasma membrane to be incorporated into progeny virions. In this study, we analyzed the impact of the Rab11-mediated recycling pathway in Sendai virus (SeV) and human parainfluenza virus type 1 (hPIV1) vRNP transport. We found that suppression of Rab11 expression caused vRNP aggregation in the cytoplasm and reduced progeny virion formation. Overexpression of constitutively active Rab11Q70L, but not dominant negative Rab11S25N co-localized with vRNP, showing that vRNP specifically recognizes the GTP-bound active form of Rab11. Moreover, Rab11Q70L co-localized with the dominant negative tails of all three subtypes of myosins, Va, Vb, and Vc, while SeV and hPIV1 vRNPs co-localized with only myosin Vb and Vc. These results highlight the critical role of Rab11 in vRNP trafficking, and suggest a specificity in the recycling endosomes parainfluenza viruses utilize for virus assembly.
[Mh] Termos MeSH primário: Miosina Tipo V/metabolismo
Vírus da Parainfluenza 1 Humana/metabolismo
Vírus Sendai/metabolismo
Montagem de Vírus/genética
Proteínas rab de Ligação ao GTP/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Endossomos/metabolismo
Células HeLa
Seres Humanos
Macaca mulatta
Nucleocapsídeo/metabolismo
Vírus da Parainfluenza 1 Humana/genética
Infecções por Paramyxoviridae
Transporte Proteico/genética
Transporte Proteico/fisiologia
Interferência de RNA
RNA Interferente Pequeno
Vírus Sendai/genética
Proteínas rab de Ligação ao GTP/biossíntese
Proteínas rab4 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (RNA, Small Interfering); EC 3.6.1.- (Myosin Type V); EC 3.6.1.- (rab11 protein); EC 3.6.5.2 (rab GTP-Binding Proteins); EC 3.6.5.2 (rab4 GTP-Binding Proteins)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170101
[Lr] Data última revisão:
170101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151021
[St] Status:MEDLINE


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[PMID]:26430212
[Au] Autor:Kälin S; Hirschmann DT; Buser DP; Spiess M
[Ad] Endereço:Biozentrum, University of Basel, Klingelbergstrasse 70, Basel CH-4056, Switzerland.
[Ti] Título:Rabaptin5 is recruited to endosomes by Rab4 and Rabex5 to regulate endosome maturation.
[So] Source:J Cell Sci;128(22):4126-37, 2015 Nov 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Rab GTPases control membrane identity, fusion and transport by interaction with effector proteins. Effectors that influence the activation-inactivation cycle of their own or other Rab proteins contribute to the timely conversion of Rab membrane identities. Rab5 and its effector rabaptin5 (Rbpt5, also known as RABEP1) are generally considered the prime example for a positive-feedback loop in which Rab5-GTP recruits Rbpt5 in complex with Rabex5 (also known as RABGEF1), the GDP/GTP exchange factor of Rab5, to early endosomes, thus maintaining the Rab5 membrane identity. By deletion analysis, we found that the membrane recruitment of Rabaptin5 required binding to Rab4 and Rabex5, but not Rab5. Deletion of either one of the two Rab5-binding domains or silencing of Rab5 expression did not affect Rabaptin5 recruitment, but produced giant endosomes with early and late endosomal characteristics. The results contradict the model of feedback activation of Rab5 and instead indicate that Rbpt5 is recruited by both Rabex5 recognizing ubiquitylated cargo and by Rab4 to activate Rab5 in a feed-forward manner.
[Mh] Termos MeSH primário: Endossomos/metabolismo
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Proteínas de Transporte Vesicular/metabolismo
Proteínas rab4 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Endossomos/enzimologia
Células HeLa
Seres Humanos
Estrutura Terciária de Proteína
Ubiquitina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Guanine Nucleotide Exchange Factors); 0 (RABEP1 protein, human); 0 (RABGEF1 protein, human); 0 (Ubiquitin); 0 (Vesicular Transport Proteins); EC 3.6.5.2 (rab4 GTP-Binding Proteins)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151117
[Lr] Data última revisão:
151117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151003
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.174664


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[PMID]:26254426
[Au] Autor:Chichger H; Braza J; Duong H; Stark M; Harrington EO
[Ad] Endereço:Vascular Research Laboratory, Providence Veterans Affairs Medical Center, and Department of Medicine, Alpert Medical School of Brown University, Providence, Rhode Island havovi.chichger@anglia.ac.uk.
[Ti] Título:Neovascularization in the pulmonary endothelium is regulated by the endosome: Rab4-mediated trafficking and p18-dependent signaling.
[So] Source:Am J Physiol Lung Cell Mol Physiol;309(7):L700-9, 2015 Oct 01.
[Is] ISSN:1522-1504
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neovascularization, the formation of new blood vessels, requires multiple processes including vascular leak, migration, and adhesion. Endosomal proteins, such as Rabs, regulate trafficking of key signaling proteins involved in neovascularization. The novel endosome protein, p18, enhances vascular endothelial (VE)-cadherin recycling from early endosome to cell junction to improve pulmonary endothelial barrier function. Since endothelial barrier integrity is vital in neovascularization, we sought to elucidate the role for endosome proteins p18 and Rab4, Rab7, and Rab9 in the process of vessel formation within the pulmonary vasculature. Overexpression of wild-type p18 (p18(wt)), but not the nonendosomal-binding mutant (p18(N39)), significantly increased lung microvascular endothelial cell migration, adhesion, and both in vitro and in vivo tube formation. Chemical inhibition of mTOR or p38 attenuated the proneovascularization role of p18(wt). Similar to the effect of p18(wt), overexpression of prorecycling wild-type (Rab4(WT)) and endosome-anchored (Rab4(Q67L)) Rab4 enhanced neovascularization processes, whereas molecular inhibition of Rab4, by using the nonendosomal-binding mutant (Rab4(S22N)) attenuated VEGF-induced neovascularization. Unlike p18, Rab4-induced neovascularization was independent of mTOR or p38 inhibition but was dependent on p18 expression. This study shows for the first time that neovascularization within the pulmonary vasculature is dependent on the prorecycling endocytic proteins Rab4 and p18.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Endossomos/metabolismo
Endotélio/metabolismo
Pulmão/metabolismo
Neovascularização Fisiológica/fisiologia
Proteínas rab4 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/genética
Endossomos/genética
Endotélio/citologia
Mutação
Ratos
Serina-Treonina Quinases TOR/genética
Serina-Treonina Quinases TOR/metabolismo
Proteínas Quinases p38 Ativadas por Mitógeno/genética
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
Proteínas rab4 de Ligação ao GTP/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 (Carrier Proteins); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.1.1 (mTOR protein, rat); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.6.5.2 (rab4 GTP-Binding Proteins)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150809
[St] Status:MEDLINE
[do] DOI:10.1152/ajplung.00235.2015


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[PMID]:26249342
[Au] Autor:Touw WG; Joosten RP; Vriend G
[Ad] Endereço:Centre for Molecular and Biomolecular Informatics, Radboud University Medical Center, Geert Grooteplein-Zuid 26-28, 6525 GA Nijmegen, The Netherlands.
[Ti] Título:Detection of trans-cis flips and peptide-plane flips in protein structures.
[So] Source:Acta Crystallogr D Biol Crystallogr;71(Pt 8):1604-14, 2015 Aug.
[Is] ISSN:1399-0047
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A coordinate-based method is presented to detect peptide bonds that need correction either by a peptide-plane flip or by a trans-cis inversion of the peptide bond. When applied to the whole Protein Data Bank, the method predicts 4617 trans-cis flips and many thousands of hitherto unknown peptide-plane flips. A few examples are highlighted for which a correction of the peptide-plane geometry leads to a correction of the understanding of the structure-function relation. All data, including 1088 manually validated cases, are freely available and the method is available from a web server, a web-service interface and through WHAT_CHECK.
[Mh] Termos MeSH primário: Peptídeos/química
Proteínas/química
[Mh] Termos MeSH secundário: Animais
Cristalografia por Raios X
Bases de Dados de Proteínas
Seres Humanos
IMP Desidrogenase/química
Modelos Moleculares
Conformação Proteica
Proteínas rab4 de Ligação ao GTP/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptides); 0 (Proteins); EC 1.1.1.205 (IMP Dehydrogenase); EC 1.1.1.205 (IMPDH2 protein, human); EC 3.6.5.2 (rab4 GTP-Binding Proteins)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150808
[St] Status:MEDLINE
[do] DOI:10.1107/S1399004715008263



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