Nonneuronal expression of Rab3A: induction during adipogenesis and association with different intracellular membranes than Rab3D.

Baldini, Giulia; Scherer, Philipp E.; Lodish, Harvey F.

doi:10.1073/pnas.92.10.4284

Cited by 55 publications

(48 citation statements)

References 31 publications

(28 reference statements)

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“…Within the large RabGTPase family, many are involved in cancer progression, both as inhibitory and promoting factors (Ho et al, 2012). Although Rab3A plays a major role in regulating exocytosis in a number of neuronal and endocrine cells (Baldini et al, 1995;Leenders et al, 2001;Pavlos et al, 2010), as well as in sperm (Bustos et al, 2012), it also has a role in cancer cells: Rab3A is upregulated in insulinoma but not in normal islets of pancreatic tissue (Lankat-Buttgereit et al, 1994). Rab3A protein is overexpressed in aggressive breast stem-like tumor cells and in epithelial breast cancer cells in response to Heregulin (Vadlamudi et al, 2000) as well as in myofibroblasts (Ina et al, 2005).…”

Section: Rab3a Interacts With the Spire-1 C-terminal Regionmentioning

confidence: 99%

Spire-1 a novel contributor of invadosome and associated invasive properties

Lagal

Abrivard

Gonzalez

et al. 2013

Journal of Cell Science

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Cancer cells have an increased ability to squeeze through extracellular matrix gaps that they create by promoting proteolysis of its components. Major sites of degradation are specialized microdomains in the plasma membrane collectively named invadosomes where the Arp2/3 complex and formin proteins cooperate to spatiotemporally control actin nucleation and the folding of a dynamic Factin core. At invadosomes, proper coupling of exo-endocytosis allows polarized delivery of proteases that facilitate degradation of ECM and disruption of the cellular barrier. We investigated the contribution of the actin nucleator Spire-1 to invadosome structure and function, using Src-activated cells and cancer cells. We found that Spire-1 is specifically recruited at invadosomes and is part of a multi-molecular complex containing Src kinase, the formin mDia1 and actin. Spire-1 interacts with the Rab3A GTPase, a key player in the regulation of exocytosis that is present at invadosomes. Finally, over-and under-expression of Spire-1 resulted in cells with an increased or decreased potential for matrix degradation, respectively, therefore suggesting a functional interplay of Spire-1 with both actin nucleation and vesicular trafficking that might impact on cell invasive and metastatic behavior.

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Section: Rab3a Interacts With the Spire-1 C-terminal Regionmentioning

confidence: 99%

Spire-1 a novel contributor of invadosome and associated invasive properties

Lagal

Abrivard

Gonzalez

et al. 2013

Journal of Cell Science

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“…In permeabilized adipocytes, nonhydrolyzable GTP analogs induce GLUT4 translocation, suggesting that GTP-binding protein(s) may be involved in insulin-stimulated GLUT4 translocation (9 -12). In this regard, Rab3D has been shown to be predominantly expressed in adipocytes and induced during differentiation of 3T3-L1 cells into adipocytes (13), although it remains to be demonstrated whether the GTPase is involved in the insulin action (14). On the other hand, Cormont et al (15) reported that Rab4 is associated with GLUT4-containing vesicles in rat adipocytes, and insulin stimulation resulted in redistribution of the protein from the vesicle to the cytosol.…”

mentioning

confidence: 99%

Insulin Stimulates Guanine Nucleotide Exchange on Rab4 via a Wortmannin-sensitive Signaling Pathway in Rat Adipocytes

Shibata

Omata

Kojima

1997

Journal of Biological Chemistry

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Rab4, a member of the Rab family of Ras-related small GTP-binding proteins, has been shown to be associated with GLUT4-containing vesicles and implicated in the insulin action on glucose transport in rat adipocytes. In the present study, we investigated the insulin effects on the guanine nucleotide exchange on Rab4. In electrically permeabilized rat adipocytes, the amount of Insulin stimulates glucose transport in muscles and adipose cells by promoting translocation of glucose transporter isoform, GLUT4, from intracellular compartmment(s) to the plasma membrane (1-3), although the molecular mechanisms of the insulin action are still obscure. Recent kinetic and morphological studies have proposed a three-compartment model for the subcellular trafficking of GLUT4 (3, 4). In the model, GLUT4 molecules are associated with at least two intracellular compartments; one is the early endosome in which GLUT4 molecules seem to appear only in the presence of insulin, and the second one is a more specialized compartment where the glucose transporter molecules are sequestrated in the basal state. Although the precise nature of the latter compartment remains indistinct, after insulin stimulation, GLUT4 molecules leave the compartment, are recruited on the plasma membrane, and then enter the endosomal recycling pathway.Over the past decade, it has become apparent that intracellular vesicle traffic is regulated by a variety of GTP-binding proteins, including Rab and Arf families of Ras-related small GTP-binding proteins (5, 6), as well as trimeric GTP-binding proteins (7) and large GTP-binding proteins such as dynamin (8). In permeabilized adipocytes, nonhydrolyzable GTP analogs induce GLUT4 translocation, suggesting that GTP-binding protein(s) may be involved in insulin-stimulated GLUT4 translocation (9 -12). In this regard, Rab3D has been shown to be predominantly expressed in adipocytes and induced during differentiation of 3T3-L1 cells into adipocytes (13), although it remains to be demonstrated whether the GTPase is involved in the insulin action (14). On the other hand, Cormont et al. (15) reported that Rab4 is associated with GLUT4-containing vesicles in rat adipocytes, and insulin stimulation resulted in redistribution of the protein from the vesicle to the cytosol. Rab4, a member of the Rab family, has been demonstrated to be associated with the early endosomes (17, 18) and implicated in regulation of the recycling of cell surface receptors, such as transferrin receptor, from the early endosomes to the cell surface (19).In a previous report, to elucidate the physiological significance of Rab4 in the insulin action, we incorporated into rat adipocytes a synthetic peptide corresponding to the Rab4 hypervariable carboxyl-terminal domain and showed that the peptide specifically inhibited glucose transport and GLUT4 translocation stimulated by insulin or GTP␥S 1 (16), providing evidence that Rab4 plays a critical role in the insulin-induced GLUT4 translocation. It remains to be clarified, however, whether or not Rab4 lies ...

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“…Of all mammalian Rab proteins, it shows the highest degree of simililarity to SEC4, which in yeast is essential for exocytosis. Four Rab3 paralogs (Rab3A, Rab3B, Rab3C, and Rab3D) are expressed in the brain (Touchot et al, 1987;Zahraoui et al, 1989;Baldini et al, 1995;Schluter et al, 2002) and are apparently functionally redundant. Although removal of individual Rab3 isoforms does not affect viability or fertility, genetic deletion of all four rab3 isoforms in mice causes perinatal lethality possibly by respiratory failure (Schluter et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Rab3 Superprimes Synaptic Vesicles for Release: Implications for Short-Term Synaptic Plasticity

Schlüter¹,

Basu²,

Südhof³

et al. 2006

J. Neurosci.

166

158

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Presynaptic vesicle trafficking and priming are important steps in regulating synaptic transmission and plasticity. The four closely related small GTP-binding proteins Rab3A, Rab3B, Rab3C, and Rab3D are believed to be important for these steps. In mice, the complete absence of all Rab3s leads to perinatal lethality accompanied by a 30% reduction of probability of Ca 2ϩ -triggered synaptic release. This study examines the role of Rab3 during Ca 2ϩ -triggered release in more detail and identifies its impact on short-term plasticity. Using patch-clamp electrophysiology of autaptic neuronal cultures from Rab3-deficient mouse hippocampus, we show that excitatory Rab3-deficient neurons display unique time-and frequency-dependent short-term plasticity characteristics in response to spike trains. Analysis of vesicle release and repriming kinetics as well as Ca 2ϩ sensitivity of release indicate that Rab3 acts on a subset of primed, fusion competent vesicles. They lower the amount of Ca 2ϩ required for action potential-triggered release, which leads to a boosting of release probability, but their action also introduces a significant delay in the supply of these modified vesicles. As a result, Rab3-induced modifications to primed vesicles causes a transient increase in the transduction efficacy of synaptic action potential trains and optimizes the encoding of synaptic information at an intermediate spike frequency range.

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Nonneuronal expression of Rab3A: induction during adipogenesis and association with different intracellular membranes than Rab3D.

Abstract: Rab3A is a small GTP-binding

Cited by 55 publications

References 31 publications

Spire-1 a novel contributor of invadosome and associated invasive properties

Spire-1 a novel contributor of invadosome and associated invasive properties

Insulin Stimulates Guanine Nucleotide Exchange on Rab4 via a Wortmannin-sensitive Signaling Pathway in Rat Adipocytes

Rab3 Superprimes Synaptic Vesicles for Release: Implications for Short-Term Synaptic Plasticity

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