Ypt and Rab GTPases: insight into functions through novel interactions

Segev, Nava

doi:10.1016/s0955-0674(00)00242-8

Cited by 267 publications

(196 citation statements)

References 90 publications

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“…A current model of the mode of actions of Rab proteins is that Rab proteins recruit the tethering, docking, and fusion factors and the actin-and microtubule-based motor proteins, most of which are their target proteins themselves or are proteins that interact with their target proteins, resulting in the assembly of a protein complex that facilitates vesicle traffic (Pfeffer, 1999(Pfeffer, , 2001Segev, 2001;Takai et al, 2001;Zerial and McBride, 2001;Hammer and Wu, 2002). Our data are consistent with this model.…”

Section: Discussionsupporting

confidence: 85%

“…The Rab family small G proteins appear to be a key regulator of intracellular vesicle traffic, including exocytosis and endocytosis (Novick and Zerial, 1997;Olkkonen and Stenmark, 1997;Martinez and Goud, 1998;Segev 2001;Pfeffer, 2001;Takai et al, 2001;Zerial and McBride, 2001). In mammalian cells, more than 60 members have been identified and each Rab protein localizes at the surface of a distinct intracellular compartment.…”

Section: Introductionmentioning

confidence: 99%

“…In mammalian cells, more than 60 members have been identified and each Rab protein localizes at the surface of a distinct intracellular compartment. Evidence is accumulating that Rab proteins regulate one (or more) specific steps of vesicle traffic by the recruitment of the tethering, docking and fusion factors and the actin-and microtubule-based motor proteins to facilitate vesicle traffic (Pfeffer, 1999(Pfeffer, , 2001Segev, 2001;Takai et al, 2001;Zerial and McBride, 2001;Hammer and Wu, 2002). Rab proteins cycle between the GDP-bound inactive and GTPbound active forms and between the cytosol and the membrane.…”

Section: Introductionmentioning

confidence: 99%

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Rabring7, a Novel Rab7 Target Protein with a RING Finger Motif

Mizuno

Kitamura

Sasaki

2003

MBoC

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Rab7, a member of the Rab family small G proteins, has been shown to regulate intracellular vesicle traffic to late endosome/lysosome and lysosome biogenesis, but the exact roles of Rab7 are still undetermined. Accumulating evidence suggests that each Rab protein has multiple target proteins that function in the exocytic/endocytic pathway. We have isolated a new Rab7 target protein, Rabring7 (Rab7-interacting RING finger protein), using a CytoTrap system. It contains an H2 type RING finger motif at the C termini. Rabring7 shows no homology with RILP, which has been reported as another Rab7 target protein. GST pull-down and coimmunoprecipitation assays demonstrate that Rabring7 specifically binds the GTP-bound form of Rab7 at the N-terminal portion. Rabring7 is found mainly in the cytosol and is recruited efficiently to late endosomes/lysosomes by the GTP-bound form of Rab7 in BHK cells. Overexpression of Rabring7 not only affects epidermal growth factor degradation but also causes the perinuclear aggregation of lysosomes, in which the accumulation of the acidotropic probe LysoTracker is remarkably enhanced. These results suggest that Rabring7 plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis

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Section: Discussionsupporting

confidence: 85%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Rabring7, a Novel Rab7 Target Protein with a RING Finger Motif

Mizuno

Kitamura

Sasaki

2003

MBoC

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“…To de-activate Ypt/Rab GTPases, GTP-hydrolysis activation proteins, GAPs, stimulate GTP hydrolysis and the GTPases can then be extracted from membranes by GDI. 10 Bacterial SVFs change the activity and membrane localization of Rab1 in two completely different ways: nucleotide-membrane cycling and post-translational modification. One multifunctional SVF, SidM, can do both.…”

Section: Svfs As Regulators Of Rab Gtpase Functionmentioning

confidence: 99%

Bringing host-cell takeover by pathogenic bacteria to center stage

Dubreuil

Segev

2011

Cellular Logistics

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“…Sin embargo, a diferencia de la REP, el GDI no puede mediar la modificación lipídica de Rab descrita anteriormente. Para la activación de Rab, los factores de desplazamiento de GDI o REP median la disociación de Rab de estos complejos y permiten su interacción con la membrana respectiva (34,37 Rab puede regular múltiples eventos moleculares en una sola región de la membrana. Sin embargo, aún se desconoce mucho de las proteínas efectoras de Rab en los mamíferos y de los mecanismos que éstas desencadenan.…”

Section: Rab Gtpasasunclassified

Alteraciones en el reclutamiento y activación de proteínas Rab durante la infección micobacteriana

Castaño

Rojas

2010

biomedica

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En el fagosoma, Mycobacterium spp. altera la activación y reclutamiento de diferentes proteínas "del gen Ras de cerebro de rata", comúnmente conocidas como Rab. En este manuscrito se revisa una serie de reportes que han demostrado que los fagosomas que contienen micobacterias tienen una expresión mayor y sostenida de Rab5, Rab11, Rab14 y Rab22a, y menor o ninguna expresión de Rab7, Rab9 y Rab6. Esto se correlaciona con aumento de la fusión de estos fagosomas con endosomas tempranos y de reciclaje, lo que les permite mantener ciertas características de compartimentos tempranos, permite que las bacterias obtengan acceso a nutrientes y previene la activación de mecanismos contra la micobacteria. La expresión de mutantes constitutivamente activos de las Rab de endosomas tempranos impide la maduración de fagosomas que contienen esferas de látex o micobacterias inactivadas por calor. Mientras que su silenciamiento, mediante ARN de interferencia o mediante dominantes negativos, induce la maduración de fagosomas micobacterianos. Los mecanismos exactos por los que las micobacterias alteran la dinámica de expresión de estas GTPasas, afectando la maduración fagolisosómica, no se han establecido. El problema podría explicarse por defectos en el reclutamiento de las proteínas que interactúan con Rab, como la cinasa-3 del fosfatidilinositol y el antígeno endosómico temprano 1. La identificación de los mecanismos empleados por Mycobacterium spp. para interrumpir el ciclo de activación de las Rab, será esencial para comprender la fisiopatología de la infección micobacteriana y útil como posibles blancos farmacológicos.Palabras clave: tuberculosis, Mycobacterium tuberculosis, proteínas de unión a GTP rab, proteínas SNARE, fagosomas, endosomas. Alterations in recruitment and activation of Rab proteins during mycobacterial infectionAt the phagosome level, Mycobacterium spp. alters activation and recruitment of several "Ras gene from rat brain" proteins, commonly known as Rab. Mycobacterial phagosomes have a greater and sustained expression of Rab5, Rab11, Rab14 and Rab22a, and lowered or no expression of Rab7, Rab9 and Rab6. This correlates with increased fusion of the phagosomes with early and recycling endosomes acquiring some features of early phogosomes, allowing the bacteria to gain access to nutrients and preventing the activation of anti-mycobacterial mechanisms. The expression of constitutively active mutants of Rab from the early stage endosomes prevents the maturation of phagosomes containing latex beads or heat-inactivated mycobacteria. Silencing of these mutants by interference RNA or dominant negative forms induces the maturation of mycobacterial phagosomes. The mechanisms have not been established by which mycobacteria alter the expression of these GTPases and thereby shift the phagolysosomal maturation. The problem can be explained by alterations in the recruitment of proteins that interact with Rab, such as phosphoinositide 3-kinases and early endosomal antigen 1. Identifying the mechanisms used by Mycobacterium sp...

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Ypt and Rab GTPases: insight into functions through novel interactions

Cited by 267 publications

References 90 publications

Rabring7, a Novel Rab7 Target Protein with a RING Finger Motif

Rabring7, a Novel Rab7 Target Protein with a RING Finger Motif

Bringing host-cell takeover by pathogenic bacteria to center stage

Alteraciones en el reclutamiento y activación de proteínas Rab durante la infección micobacteriana

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