Activated ADP-ribosylation Factor Assembles Distinct Pools of Actin on Golgi Membranes

Fucini, Raymond V.; Navarrete, Araceli; Vadakkan, Catherine; Lacomis, Lynne; Erdjument‐Bromage, Hediye; Tempst, Paul; Stamnes, Mark

doi:10.1074/jbc.m000024200

Cited by 89 publications

(95 citation statements)

References 45 publications

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“…Recent studies have directly implicated Cdc42 and actin in membrane trafficking through the Golgi. For example, actin has been observed on Golgi-derived membrane vesicles and can assemble on Golgi membranes in vitro (Musch et al, 1997;Godi et al, 1998;Heimann et al, 1999;Fucini et al, 2000;Valderrama et al, 2000). Cdc42 also seems to associate with Golgi-membranes and to induce actin polymerization through the engagement of N-WASP (Fucini et al, 2002;McCallum et al, 1998;Moreau et al, 2000;Wu et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies have suggested that Golgi actin plays a regulatory role in membrane vesicle transport (Godi et al, 1998;Hirschberg et al, 1998;De Matteis and Morrow, 2000;Fucini et al, 2000Fucini et al, , 2002Valderrama et al, 2000Valderrama et al, , 2001. To determine whether perinuclear actin plays a regulatory role in endomembrane trafficking, we took advantage of the temperature-sensitive VSV-G protein mutant ts045.…”

Section: Perinuclear Actin Polymerization Occurs In Golgi Region and mentioning

confidence: 99%

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Small GTP-binding Protein TC10 Differentially Regulates Two Distinct Populations of Filamentous Actin in 3T3L1 Adipocytes

Kanzaki

Watson

Hou

et al. 2002

MBoC

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TC10 is a member of the Rho family of small GTP-binding proteins that has previously been implicated in the regulation of insulin-stimulated GLUT4 translocation in adipocytes. In a manner similar to Cdc42-stimulated actin-based motility, we have observed that constitutively active TC10 (TC10/Q75L) can induce actin comet tails in Xenopus oocyte extracts in vitro and extensive actin polymerization in the perinuclear region when expressed in 3T3L1 adipocytes. In contrast, expression of TC10/Q75L completely disrupted adipocyte cortical actin, which was specific for TC10, because expression of constitutively active Cdc42 was without effect. The effect of TC10/ Q75L to disrupt cortical actin was abrogated after deletion of the amino terminal extension (⌬N-TC10/Q75L), whereas this deletion retained the ability to induce perinuclear actin polymerization. In addition, alteration of perinuclear actin by expression of TC10/Q75L, a dominantinterfering TC10/T31N mutant or a mutant N-WASP protein (N-WASP/⌬VCA) reduced the rate of VSV G protein trafficking to the plasma membrane. Furthermore, TC10 directly bound to Golgi COPI coat proteins through a dilysine motif in the carboxyl terminal domain consistent with a role for TC10 regulating actin polymerization on membrane transport vesicles. Together, these data demonstrate that TC10 can differentially regulate two types of filamentous actin in adipocytes dependent on distinct functional domains and its subcellular compartmentalization. INTRODUCTIONTC10 is a member of the Rho family of GTP-binding proteins and is closely related to Cdc42 (Neudauer et al., 1998). Although TC10 is primarily expressed in adipose and muscle tissue (Neudauer et al., 1998;Imagawa et al., 1999), its function has only been peripherally examined. In vitro binding assays have indicated that active GTP-bound TC10 can bind a number of potential effectors, including mixed lineage kinase 2, myotonic dystrophy-related Cdc42 kinase, p21-activated protein kinases, the Borg family of interacting proteins, the mammalian partition-defective homolog Par6, and the N-WASP isoform of the Wiskott-Aldrich Syndrome Protein (Neudauer et al., 1998;Joberty et al., 1999Joberty et al., , 2000.However, whether TC10 can interact with any of these potential effectors under physiological conditions has yet to be established. Nevertheless, similar to other members of the Rho family, expression of a constitutively active TC10 mutant (TC10/Q75L) in fibroblasts decreased actin stress fibers concomitant with the formation of plasma membrane microspikes (Murphy et al., 1999). However, expression of wildtype TC10 (TC10/WT) was without any effect on fibroblast cell morphology or actin structures. In contrast, expression of wild-type Cdc42 (Cdc42/WT) or a constitutively active Cdc42 mutant (Cdc42/Q61L) in fibroblasts decreased actin stress fibers in parallel with the induction of actin protrusions and lamellipodia (Coghlan et al., 2000). These data indicate that although fibroblasts express the necessary downstream effectors to modulate ac...

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Section: Discussionmentioning

confidence: 99%

Section: Perinuclear Actin Polymerization Occurs In Golgi Region and mentioning

confidence: 99%

Small GTP-binding Protein TC10 Differentially Regulates Two Distinct Populations of Filamentous Actin in 3T3L1 Adipocytes

Kanzaki

Watson

Hou

et al. 2002

MBoC

Self Cite

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“…For example, treatment of cells with cytochalasin decreases the rate of Golgi protein transport [164,165]. Indeed, actin has been observed on Golgi-derived membrane vesicles and assembles on Golgi membranes in vitro [166][167][168][169]. Moreover, actin dynamics at the TGN have been found to be coupled to clathrin-coated vesicle formation [170].…”

Section: (3) Actin Remodeling At the Tgn Plays A Role In Regulatmentioning

confidence: 99%

“…The ARF family is comprised of ARF1-ARF6, which are divided into three classes on the basis of similarity in primary structure: Class I, ARF1-3; Class II, ARF4 and ARF5; and Class III, ARF6 [205]. ARF1 and ARF6 have been shown to be involved in reorganizing the actin cytoskeleton [166,167,173,206]. Like other small G-proteins, ARFs are controlled by ARF-GEFs and ARF-GAPs [205].…”

Section: (4) Actin Dynamics Are Regulated By Both Phosphoinositimentioning

confidence: 99%

Insulin Receptor Signals Regulating GLUT4 Translocation and Actin Dynamics

Kanzaki

2006

Endocr J

131

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Abstract. In skeletal muscle and adipose tissue, insulin-stimulated glucose uptake is dependent upon translocation of the insulin-responsive glucose transporter GLUT4 from intracellular storage compartments to the plasma membrane. This insulin-induced redistribution of GLUT4 protein is achieved through a series of highly organized membrane trafficking events, orchestrated by insulin receptor signals. Recently, several key molecules linking insulin receptor signals and membrane trafficking have been identified, and emerging evidence supports the importance of subcellular compartmentalization of signaling components at the right time and in the right place. In addition, the translocation of GLUT4 in adipocytes requires insulin stimulation of dynamic actin remodeling at the inner surface of the plasma membrane (cortical actin) and in the perinuclear region. This results from at least two independent insulin receptor signals, one leading to the activation of phosphatidylinositol (PI) 3-kinase and the other to the activation of the Rho family small GTP-binding protein TC10. Thus, both spatial and temporal regulations of actin dynamics, both beneath the plasma membrane and around endomembranes, by insulin receptor signals are also involved in the process of GLUT4 translocation.

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“…More recent data demonstrate that ARF1 plays a role in generating clathrin-coated vesicles, by first recruiting adaptor complexes on vesicles at the transGolgi network (TGN) and immature secretory vesicles (14 -17). Additional effects of ARF1 on the cytoskeleton are also described (18).…”

Section: The Nucleotide Sequence(s) Reported In This Paper Has Been Smentioning

confidence: 99%

Toxoplasma gondii ADP-ribosylation Factor 1 Mediates Enhanced Release of Constitutively Secreted Dense Granule Proteins

Liendo

Stedman

Ngô

et al. 2001

Journal of Biological Chemistry

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Toxoplasma gondii dense granules are morphologically similar to dense matrix granules in specialized secretory cells, yet are secreted in a constitutive, calcium-independent fashion. We previously demonstrated that secretion of dense granule proteins in permeabilized parasites was augmented by the non-hydrolyzable GTP analogue guanosine 5-3-O-(thio)triphosphate (GTP␥S) (Chaturvedi, S., Qi, H., Coleman, D. L., Hanson, P., Rodriguez, A., and Joiner, K. A. (1998) J. Biol. Chem. 274, 2424 -2431). As now demonstrated by pharmacological and electron microscopic approaches, GTP␥S enhanced release of dense granule proteins in the permeabilized cell system. To investigate the role of ADPribosylation factor 1 (ARF1) in this process, a cDNA encoding T. gondii ARF1 (TgARF1) was isolated. Endogenous and transgenic TgARF1 localized to the Golgi of T. gondii, but not to dense granules. An epitope-tagged mutant of TgARF1 predicted to be impaired in GTP hydrolysis (Q71L) partially dispersed the Golgi signal, with localization to scattered vesicles, whereas a mutant impaired in nucleotide binding (T31N) was cytosolic in location. Both mutants caused partial dispersion of a Golgi/trans-Golgi network marker. TgARF1 mutants inhibited delivery of the secretory reporter, Escherichia coli alkaline phosphatase, to dense granules, precluding an in vivo assessment of the role of TgARF1 in release of intact dense granules. To circumvent this limitation, recombinant TgARF1 was purified using two separate approaches, and used in the permeabilized cell assay. TgARF1 protein purified on a Cibacron G3 column and able to bind GTP stimulated dense granule secretion in the permeabilized cell secretion assay. These results are the first to show that ARF1 can augment release of constitutively secreted vesicles at the target membrane.Remarkable progress has been made recently in understanding the protein machinery responsible for secretory events in mammalian and yeast cells (1). The components involved in both constitutive secretion as well as regulated release in secretory cells are broadly conserved evolutionarily (2). Although this suggests that the same should be true in protozoan parasites, the presence of unusual secretory organelles in these organisms confounds this simple hypothesis. By the same argument, parasites provide a unique means to explore selected issues in regulation of secretion from preformed organelles (reviewed in Ref.3).We have used this logic to explore the organization of the secretory pathway in the protozoan parasite Toxoplasma gondii. This parasite is an obligate intracellular pathogen that resides in the host cell within a specialized compartment, the parasitophorous vacuole (PV), 1 which is separated from the host cell cytoplasm by the parasitophorous vacuole membrane (PVM). The success of infection depends on the ability of the parasite to modify the PV and the PVM by secreting proteins to the extra-parasite environment (reviewed in Ref. 4). Thus, secretion is a critical feature of parasite survival.T. gondii has a we...

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Activated ADP-ribosylation Factor Assembles Distinct Pools of Actin on Golgi Membranes

Cited by 89 publications

References 45 publications

Small GTP-binding Protein TC10 Differentially Regulates Two Distinct Populations of Filamentous Actin in 3T3L1 Adipocytes

Small GTP-binding Protein TC10 Differentially Regulates Two Distinct Populations of Filamentous Actin in 3T3L1 Adipocytes

Insulin Receptor Signals Regulating GLUT4 Translocation and Actin Dynamics

Toxoplasma gondii ADP-ribosylation Factor 1 Mediates Enhanced Release of Constitutively Secreted Dense Granule Proteins

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