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[PMID]:28096466
[Au] Autor:Lee H; Min K; Yi JS; Shi H; Chang W; Jackson L; Bennett AM
[Ad] Endereço:From the Department of Pharmacology and.
[Ti] Título:A Phosphoproteomic Screen Identifies a Guanine Nucleotide Exchange Factor for Rab3A Protein as a Mitogen-activated Protein (MAP) Kinase Phosphatase-5-regulated MAP Kinase Target in Interleukin 6 (IL-6) Secretion and Myogenesis.
[So] Source:J Biol Chem;292(9):3581-3590, 2017 Mar 03.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mitogen-activated protein kinases (MAPKs) have been shown to regulate skeletal muscle function. Previously, we showed that MAPK phosphatase-5 (MKP-5) negatively regulates myogenesis and regeneration of skeletal muscle through inhibition of p38 MAPK and c-Jun N-terminal kinase (JNK). However, the identity and contribution of MKP-5-regulated MAPK targets in the control of skeletal muscle function and regenerative myogenesis have not been established. To identify MKP-5-regulated MAPK substrates in skeletal muscle, we performed a global differential phospho-MAPK substrate screen in regenerating skeletal muscles of wild type and MKP-5-deficient mice. We discovered a novel MKP-5-regulated MAPK substrate called guanine nucleotide exchange factor for Rab3A (GRAB) that was hyperphosphorylated on a phospho-MAPK motif in skeletal muscle of MKP-5-deficient mice. GRAB was found to be phosphorylated by JNK on serine 169. Myoblasts overexpressing a phosphorylation-defective mutant of GRAB containing a mutation at Ser-169 to Ala-169 (GRAB-S169A) inhibited the ability of C2C12 myoblasts to differentiate. We found that GRAB phosphorylation at Ser-169 was required for the secretion of the promyogenic cytokine interleukin 6 (IL-6). Consistent with this observation, MKP-5-deficient mice exhibited increased circulating IL-6 expression as compared with wild type mice. Collectively, these data demonstrate a novel mechanism whereby MKP-5-mediated regulation of JNK negatively regulates phosphorylation of GRAB, which subsequently controls secretion of IL-6. These data support the notion that MKP-5 serves as a negative regulator of MAPK-dependent signaling of critical skeletal muscle signaling pathways.
[Mh] Termos MeSH primário: Fosfatases de Especificidade Dupla/metabolismo
Regulação Enzimológica da Expressão Gênica
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Interleucina-6/metabolismo
Desenvolvimento Muscular
Proteína rab3A de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Movimento Celular
Proliferação Celular
Sistema de Sinalização das MAP Quinases
Camundongos
Camundongos Knockout
Músculo Esquelético/metabolismo
Mutação
Mioblastos/metabolismo
Fosforilação
Proteômica
Regeneração
Serina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GRAB protein, mouse); 0 (Guanine Nucleotide Exchange Factors); 0 (Interleukin-6); 0 (interleukin-6, mouse); 452VLY9402 (Serine); EC 3.1.3.16 (Dusp10 protein, mouse); EC 3.1.3.48 (Dual-Specificity Phosphatases); EC 3.6.5.2 (rab3A GTP-Binding Protein)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170119
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.769208


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[PMID]:28057568
[Au] Autor:Tang X; Xie C; Wang Y; Wang X
[Ad] Endereço:Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, PR China.
[Ti] Título:Localization of Rab3A-binding site on C2A domain of synaptotagmin I to reveal its regulatory mechanism.
[So] Source:Int J Biol Macromol;96:736-742, 2017 Mar.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Synaptotagmin I (Syt I) functions in the regulation of neurotransmitter release and multiple other cellular processes through its C2 domain binding to other molecules. Our previous study demonstrated that Rab3A, a small GTP-binding protein, is a new interacting partner of Syt I and could bind to both of the C2 domains; the polylysine motif in C2B is a key site for Rab3A binding, but the binding site on C2A is not clear. In order to localize Rab3-binding site on C2A and reveal the relevant regulatory mechanism, in the present study we investigated the interaction between recombinant Rab3A and various C2A mutants. The results showed that a key Rab3A-binding site on C2A is located at R199K200 in the flexible loop 2 of the domain, and the site does not overlap with most of the known functional sites or residues. It was speculated that the interaction between Rab3A and C2A is not simply based on electrostatic force, and Rab3A regulates C2A-mediated vesicle-presynaptic membrane fusion mainly through affecting the C2A binding to phospholipids in the presynaptic membrane. These results have contributed to the comprehension of action mechanism of Rab3 and synaptotagmin in the regulation of synaptic vesicle exocytosis.
[Mh] Termos MeSH primário: Sinaptotagmina I/química
Sinaptotagmina I/metabolismo
Proteína rab3A de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação
Cálcio/metabolismo
Mutação
Fosfolipídeos/metabolismo
Conformação Proteica em Folha beta
Domínios Proteicos
Ratos
Sinaptotagmina I/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phospholipids); 0 (Synaptotagmin I); EC 3.6.5.2 (rab3A GTP-Binding Protein); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170107
[St] Status:MEDLINE


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[PMID]:27807164
[Au] Autor:Cazares VA; Njus MM; Manly A; Saldate JJ; Subramani A; Ben-Simon Y; Sutton MA; Ashery U; Stuenkel EL
[Ad] Endereço:Neuroscience Graduate Program and.
[Ti] Título:Dynamic Partitioning of Synaptic Vesicle Pools by the SNARE-Binding Protein Tomosyn.
[So] Source:J Neurosci;36(44):11208-11222, 2016 Nov 02.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neural networks engaged in high-frequency activity rely on sustained synaptic vesicle recycling and coordinated recruitment from functionally distinct synaptic vesicle (SV) pools. However, the molecular pathways matching neural activity to SV dynamics and release requirements remain unclear. Here we identify unique roles of SNARE-binding Tomosyn1 (Tomo1) proteins as activity-dependent substrates that regulate dynamics of SV pool partitioning at rat hippocampal synapses. Our analysis is based on monitoring changes in distinct functionally defined SV pools via V-Glut1-pHluorin fluorescence in cultured hippocampal neurons in response to alterations in presynaptic protein expression. Specifically, we find knockdown of Tomo1 facilitates release efficacy from the Readily Releasable Pool (RRP), and regulates SV distribution to the Total Recycling Pool (TRP), which is matched by a decrease in the SV Resting Pool. Notably, these effects were reversed by Tomo1 rescue and overexpression. Further, we identify that these actions of Tomo1 are regulated via activity-dependent phosphorylation by cyclin-dependent kinase 5 (Cdk5). Assessment of molecular interactions that may contribute to these actions identified Tomo1 interaction with the GTP-bound state of Rab3A, an SV GTPase involved in SV targeting and presynaptic membrane tethering. In addition, Tomo1 via Rab3A-GTP was also observed to interact with Synapsin 1a/b cytoskeletal interacting proteins. Finally, our data indicate that Tomo1 regulation of SV pool sizes serves to adapt presynaptic neurotransmitter release to chronic silencing of network activity. Overall, the results establish Tomo1 proteins as central mediators in neural activity-dependent changes in SV distribution among SV pools. SIGNIFICANCE STATEMENT: Although information transfer at central synapses via sustained high-frequency neural activity requires coordinated synaptic vesicle (SV) recycling, the mechanism(s) by which synapses sense and dynamically modify SV pools to match network demands remains poorly defined. To advance understanding, we quantified SV pool sizes and their sensitivity to neural activity while altering Tomo1 expression, a putative regulator of the presynaptic Readily Releasable Pool. Remarkably, we find Tomo1 actions to extend beyond the Readily Releasable Pool to mediate the Total Recycling Pool and SV Resting Pool distribution, and this action is sensitive to neural activity through Cdk5 phosphorylation of Tomo1. Moreover, Tomo1 appears to exert these actions through interaction with Rab3A-GTP and synapsin proteins. Together, our results argue that Tomo1 is a central mediator of SV availability for neurotransmission.
[Mh] Termos MeSH primário: Guanosina Trifosfato/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Terminações Pré-Sinápticas/metabolismo
Proteínas R-SNARE/metabolismo
Proteínas SNARE/metabolismo
Transmissão Sináptica/fisiologia
Vesículas Sinápticas/metabolismo
Proteína rab3A de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Feminino
Hipocampo/metabolismo
Hipocampo/ultraestrutura
Masculino
Ratos
Sinapses
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nerve Tissue Proteins); 0 (R-SNARE Proteins); 0 (SNARE Proteins); 0 (tomosyn-1 protein, rat); 86-01-1 (Guanosine Triphosphate); EC 3.6.5.2 (rab3A GTP-Binding Protein)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161104
[St] Status:MEDLINE


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[PMID]:27613869
[Au] Autor:Quevedo MF; Lucchesi O; Bustos MA; Pocognoni CA; De la Iglesia PX; Tomes CN
[Ad] Endereço:From the IHEM, Universidad Nacional de Cuyo, CONICET, Facultad de Ciencias Médicas, CC56. 5500 Mendoza, Argentina.
[Ti] Título:The Rab3A-22A Chimera Prevents Sperm Exocytosis by Stabilizing Open Fusion Pores.
[So] Source:J Biol Chem;291(44):23101-23111, 2016 10 28.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:At the final stage of exocytotis, a fusion pore opens between the plasma and a secretory vesicle membranes; typically, when the pore dilates the vesicle releases its cargo. Sperm contain a large dense-core secretory granule (the acrosome) whose contents are secreted by regulated exocytosis at fertilization. Minutes after the arrival of the triggering signal, the acrosomal and plasma membranes dock at multiple sites and fusion pores open at the contact points. It is believed that immediately afterward, fusion pores dilate spontaneously. Rab3A is an essential component of human sperm exocytotic machinery. Yet, recombinant, persistently active Rab3A halts calcium-triggered secretion when introduced after docking into streptolysin O-permeabilized cells; so does a Rab3A-22A chimera. Here, we applied functional assays, electron and confocal microscopy to show that the secretion blockage is due to the stabilization of open fusion pores. Other novel findings are that sperm SNAREs engage in α-SNAP/NSF-sensitive complexes at a post-fusion stage. Complexes are disentangled by these chaperons to achieve vesiculation and acrosomal contents release. Thus, post-fusion regulation of the pores determines their expansion and the success of the acrosome reaction.
[Mh] Termos MeSH primário: Exocitose
Espermatozoides/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
Proteína rab3A de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Acrossomo/metabolismo
Cálcio/metabolismo
Membrana Celular/genética
Membrana Celular/metabolismo
Seres Humanos
Masculino
Proteínas rab de Ligação ao GTP/genética
Proteína rab3A de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RAB22A protein, human); EC 3.6.5.2 (rab GTP-Binding Proteins); EC 3.6.5.2 (rab3A GTP-Binding Protein); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160911
[St] Status:MEDLINE


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[PMID]:27559163
[Au] Autor:Hong Y; Zhao T; Li XJ; Li S
[Ad] Endereço:Department of Human Genetics, Emory University School of Medicine, Atlanta, Georgia 30322.
[Ti] Título:Mutant Huntingtin Impairs BDNF Release from Astrocytes by Disrupting Conversion of Rab3a-GTP into Rab3a-GDP.
[So] Source:J Neurosci;36(34):8790-801, 2016 Aug 24.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Brain-derived neurotrophic factor (BDNF) is essential for neuronal differentiation and survival. We know that BDNF levels decline in the brains of patients with Huntington's disease (HD), a neurodegenerative disease caused by the expression of mutant huntingtin protein (mHtt), and furthermore that administration of BDNF in HD mice is protective against HD neuropathology. BDNF is produced in neurons, but astrocytes are also an important source of BDNF in the brain. Nonetheless, whether mHtt affects astrocytic BDNF in the HD brain remains unknown. Here we investigated astrocytes from HD140Q knock-in mice and uncovered evidence that mHtt decreases BDNF secretion from astrocytes, which is mediated by exocytosis in astrocytes. Our results demonstrate that mHtt associates with Rab3a, a small GTPase localized on membranes of dense-core vesicles, and prevents GTP-Rab3a from binding to Rab3-GAP1, disrupting the conversion of GTP-Rab3a into GDP-Rab3a and thus impairing the docking of BDNF vesicles on plasma membranes of astrocytes. Importantly, overexpression of Rab3a rescues impaired BDNF vesicle docking and secretion from HD astrocytes. Moreover, ATP release and the number of ATP-containing dense-core vesicles docking are decreased in HD astrocytes, suggesting that the exocytosis of dense-core vesicles is impaired by mHtt in HD astrocytes. Further, Rab3a overexpression reduces reactive astrocytes in the striatum of HD140Q knock-in mice. Our results indicate that compromised exocytosis of BDNF in HD astrocytes contributes to the decreased BDNF levels in HD brains and underscores the importance of improving glial function in the treatment of HD. SIGNIFICANCE STATEMENT: Huntington's disease (HD) is an inherited neurodegenerative disorder that affects one in every 10,000 Americans. To date, there is no effective treatment for HD, in part because the pathogenic mechanism driving the disease is not fully understood. The dysfunction of astrocytes is known to contribute to the pathogenesis of HD. One important role of astrocytes is to synthesize and release brain-derived neurotrophic factor (BDNF), which is vital for neuronal survival, development, and function. We found that mutant huntingtin protein (mHtt) at the endogenous level decreases BDNF secretion from astrocytes by disrupting the conversion of GTP-Rab3a into GDP-Rab3a and that overexpressing Rab3a can rescue this deficient BDNF release and early neuropathology in HD knock-in mouse brain. Our study suggests that astrocytic Rab3a is a potential therapeutic target for HD treatment.
[Mh] Termos MeSH primário: Fator Neurotrófico Derivado do Encéfalo/metabolismo
Encéfalo/metabolismo
Regulação da Expressão Gênica/genética
Proteína Huntingtina/genética
Mutação/genética
Proteína rab3A de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Animais
Animais Recém-Nascidos
Astrócitos/metabolismo
Células Cultivadas
Feminino
Proteína Glial Fibrilar Ácida/metabolismo
Guanosina Difosfato/metabolismo
Guanosina Trifosfato/metabolismo
Imunoprecipitação
Técnicas In Vitro
Masculino
Camundongos
Camundongos Transgênicos
RNA Mensageiro
Transdução Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Brain-Derived Neurotrophic Factor); 0 (Glial Fibrillary Acidic Protein); 0 (Huntingtin Protein); 0 (RNA, Messenger); 146-91-8 (Guanosine Diphosphate); 86-01-1 (Guanosine Triphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.5.2 (rab3A GTP-Binding Protein)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160826
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.0168-16.2016


  6 / 187 MEDLINE  
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[PMID]:27466341
[Au] Autor:Spencer B; Desplats PA; Overk CR; Valera-Martin E; Rissman RA; Wu C; Mante M; Adame A; Florio J; Rockenstein E; Masliah E
[Ad] Endereço:Department of Neurosciences and.
[Ti] Título:Reducing Endogenous α-Synuclein Mitigates the Degeneration of Selective Neuronal Populations in an Alzheimer's Disease Transgenic Mouse Model.
[So] Source:J Neurosci;36(30):7971-84, 2016 Jul 27.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Alzheimer's disease (AD) is characterized by the progressive accumulation of amyloid ß (Aß) and microtubule associate protein tau, leading to the selective degeneration of neurons in the neocortex, limbic system, and nucleus basalis, among others. Recent studies have shown that α-synuclein (α-syn) also accumulates in the brains of patients with AD and interacts with Aß and tau, forming toxic hetero-oligomers. Although the involvement of α-syn has been investigated extensively in Lewy body disease, less is known about the role of this synaptic protein in AD. Here, we found that reducing endogenous α-syn in an APP transgenic mouse model of AD prevented the degeneration of cholinergic neurons, ameliorated corresponding deficits, and recovered the levels of Rab3a and Rab5 proteins involved in intracellular transport and sorting of nerve growth factor and brain-derived neurotrophic factor. Together, these results suggest that α-syn might participate in mechanisms of vulnerability of selected neuronal populations in AD and that reducing α-syn might be a potential approach to protecting these populations from the toxic effects of Aß. SIGNIFICANCE STATEMENT: Reducing endogenous α-synuclein (α-syn) in an APP transgenic mouse model of Alzheimer's disease (AD) prevented the degeneration of cholinergic neurons, ameliorated corresponding deficits, and recovered the levels of Rab3a and Rab5 proteins involved in intracellular transport and sorting of nerve growth factor and brain-derived neurotrophic factor. These results suggest that α-syn might participate in mechanisms of vulnerability of selected neuronal populations in AD and that reducing α-syn might be a potential approach to protecting these populations from the toxic effects of amyloid ß.
[Mh] Termos MeSH primário: Doença de Alzheimer/metabolismo
Doença de Alzheimer/patologia
Encéfalo/metabolismo
Neurônios/metabolismo
Neurônios/patologia
alfa-Sinucleína/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/patologia
Regulação para Baixo/genética
Feminino
Masculino
Camundongos
Camundongos Knockout
Camundongos Transgênicos
alfa-Sinucleína/genética
Proteína rab3A de Ligação ao GTP/metabolismo
Proteínas rab5 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (alpha-Synuclein); EC 3.6.5.2 (rab3A GTP-Binding Protein); EC 3.6.5.2 (rab5 GTP-Binding Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160729
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.0775-16.2016


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[PMID]:27423421
[Au] Autor:Bello OD; Cappa AI; de Paola M; Zanetti MN; Fukuda M; Fissore RA; Mayorga LS; Michaut MA
[Ad] Endereço:Instituto de Histología y Embriología, CONICET - Universidad Nacional de Cuyo, Av. Libertador 80, 5500 Mendoza, Argentina.
[Ti] Título:Rab3A, a possible marker of cortical granules, participates in cortical granule exocytosis in mouse eggs.
[So] Source:Exp Cell Res;347(1):42-51, 2016 Sep 10.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fusion of cortical granules with the oocyte plasma membrane is the most significant event to prevent polyspermy. This particular exocytosis, also known as cortical reaction, is regulated by calcium and its molecular mechanism is still not known. Rab3A, a member of the small GTP-binding protein superfamily, has been implicated in calcium-dependent exocytosis and is not yet clear whether Rab3A participates in cortical granules exocytosis. Here, we examine the involvement of Rab3A in the physiology of cortical granules, particularly, in their distribution during oocyte maturation and activation, and their participation in membrane fusion during cortical granule exocytosis. Immunofluorescence and Western blot analysis showed that Rab3A and cortical granules have a similar migration pattern during oocyte maturation, and that Rab3A is no longer detected after cortical granule exocytosis. These results suggested that Rab3A might be a marker of cortical granules. Overexpression of EGFP-Rab3A colocalized with cortical granules with a Pearson correlation coefficient of +0.967, indicating that Rab3A and cortical granules have almost a perfect colocalization in the egg cortical region. Using a functional assay, we demonstrated that microinjection of recombinant, prenylated and active GST-Rab3A triggered cortical granule exocytosis, indicating that Rab3A has an active role in this secretory pathway. To confirm this active role, we inhibited the function of endogenous Rab3A by microinjecting a polyclonal antibody raised against Rab3A prior to parthenogenetic activation. Our results showed that Rab3A antibody microinjection abolished cortical granule exocytosis in parthenogenetically activated oocytes. Altogether, our findings confirm that Rab3A might function as a marker of cortical granules and participates in cortical granule exocytosis in mouse eggs.
[Mh] Termos MeSH primário: Grânulos Citoplasmáticos/metabolismo
Exocitose
Oócitos/citologia
Oócitos/metabolismo
Proteína rab3A de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Feminino
Proteínas de Fluorescência Verde/metabolismo
Cavalos
Seres Humanos
Metáfase
Camundongos
Microinjeções
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Fusion Proteins); 0 (enhanced green fluorescent protein); 147336-22-9 (Green Fluorescent Proteins); EC 3.6.5.2 (rab3A GTP-Binding Protein)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160718
[St] Status:MEDLINE


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[PMID]:27325790
[Au] Autor:Encarnação M; Espada L; Escrevente C; Mateus D; Ramalho J; Michelet X; Santarino I; Hsu VW; Brenner MB; Barral DC; Vieira OV
[Ad] Endereço:Centro de Estudos de Doenças Crónicas, NOVA Medical School, Faculdade de Ciências Médicas, Universidade NOVA de Lisboa, 1169-056 Lisboa, Portugal.
[Ti] Título:A Rab3a-dependent complex essential for lysosome positioning and plasma membrane repair.
[So] Source:J Cell Biol;213(6):631-40, 2016 06 20.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysosome exocytosis plays a major role in resealing plasma membrane (PM) disruptions. This process involves two sequential steps. First, lysosomes are recruited to the periphery of the cell and then fuse with the damaged PM. However, the trafficking molecular machinery involved in lysosome exocytosis and PM repair (PMR) is poorly understood. We performed a systematic screen of the human Rab family to identify Rabs required for lysosome exocytosis and PMR. Rab3a, which partially localizes to peripheral lysosomes, was one of the most robust hits. Silencing of Rab3a or its effector, synaptotagmin-like protein 4a (Slp4-a), leads to the collapse of lysosomes to the perinuclear region and inhibition of PMR. Importantly, we have also identified a new Rab3 effector, nonmuscle myosin heavy chain IIA, as part of the complex formed by Rab3a and Slp4-a that is responsible for lysosome positioning at the cell periphery and lysosome exocytosis.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Membrana Celular/fisiologia
Lisossomos/metabolismo
Lisossomos/fisiologia
Proteína rab3A de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Linhagem Celular Tumoral
Exocitose/fisiologia
Células HEK293
Células HeLa
Seres Humanos
Leucócitos Mononucleares
Cadeias Pesadas de Miosina/metabolismo
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (SYTL4 protein, human); 0 (Vesicular Transport Proteins); EC 3.6.4.1 (Myosin Heavy Chains); EC 3.6.5.2 (rab3A GTP-Binding Protein)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160622
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201511093


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[PMID]:27325788
[Au] Autor:Raiborg C; Stenmark H
[Ad] Endereço:Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Montebello, N-0379 Oslo, Norway Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, Montebello, N-0379 Oslo, Norway.
[Ti] Título:Plasma membrane repairs by small GTPase Rab3a.
[So] Source:J Cell Biol;213(6):613-5, 2016 Jun 20.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysosomes fuse with the plasma membrane to help repair membrane lesions, but how they are positioned close to these lesions is not fully understood. Now, Encarnação et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201511093) demonstrate that the lysosomal GTPase Rab3a and its effectors orchestrate lysosome positioning and plasma membrane repair.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Membrana Celular/fisiologia
Proteína rab3A de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Células Eucarióticas/metabolismo
Células Eucarióticas/fisiologia
Seres Humanos
Lisossomos/metabolismo
Lisossomos/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.5.2 (rab3A GTP-Binding Protein); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160622
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201606006


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[PMID]:26791531
[Au] Autor:Wang HH; Cui Q; Zhang T; Wang ZB; Ouyang YC; Shen W; Ma JY; Schatten H; Sun QY
[Ad] Endereço:College of Life Sciences, Qingdao Agricultural University, Qingdao, 266109, China.
[Ti] Título:Rab3A, Rab27A, and Rab35 regulate different events during mouse oocyte meiotic maturation and activation.
[So] Source:Histochem Cell Biol;145(6):647-57, 2016 Jun.
[Is] ISSN:1432-119X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Rab family members play important roles in membrane trafficking, cell growth, and differentiation. Almost all components of the cell endomembrane system, the nucleus, and the plasma membrane are closely related to RAB proteins. In this study, we investigated the distribution and functions of three members of the Rab family, Rab3A, Rab27A, and Rab35, in mouse oocyte meiotic maturation and activation. The three Rab family members showed different localization patterns in oocytes. Microinjection of siRNA, antibody injection, or inhibitor treatment showed that (1) Rab3A regulates peripheral spindle and cortical granule (CG) migration, polarity establishment, and asymmetric division; (2) Rab27A regulates CG exocytosis following MII-stage oocyte activation; and (3) Rab35 plays an important role in spindle organization and morphology maintenance, and thus meiotic nuclear maturation. These results show that Rab proteins play important roles in mouse oocyte meiotic maturation and activation and that different members exert different distinct functions.
[Mh] Termos MeSH primário: Meiose
Oócitos/citologia
Oócitos/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
Proteína rab3A de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Imunofluorescência
Camundongos
Camundongos Endogâmicos ICR
Proteínas rab de Ligação ao GTP/análise
Proteínas rab de Ligação ao GTP/genética
Proteínas rab27 de Ligação ao GTP
Proteína rab3A de Ligação ao GTP/análise
Proteína rab3A de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (rab27 GTP-Binding Proteins); EC 3.6.1.- (Rab35 protein, mouse); EC 3.6.1.-. (Rab27a protein, mouse); EC 3.6.5.2 (rab GTP-Binding Proteins); EC 3.6.5.2 (rab3A GTP-Binding Protein)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160122
[St] Status:MEDLINE
[do] DOI:10.1007/s00418-015-1404-5



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