Gaf-1, a γ-SNAP-binding Protein Associated with the Mitochondria

Chen, Dong; Xu, Weidong; He, Ping; Medrano, Estela E.; Whiteheart, Sidney W.

doi:10.1074/jbc.m009424200

Cited by 19 publications

(21 citation statements)

References 57 publications

(24 reference statements)

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“…Interestingly, FIP3 and FIP4, members of the class II Rab11-FIP proteins, interact with Exo70 within the exocyst complex, and this is proposed to couple Rab11-positive vesicles to the cleavage furrow during cytokinesis (Fielding et al, 2005). Furthermore, Rip11 has been reported to interact with ␥SNAP, a component of the SNARE complex (Chen et al, 2001). These observations are of significant interest because Rab proteins are well established to play an important modulatory role in the SNARE-mediated fusion complex that controls several homotypic and heterotypic membrane fusion events (Stamnes et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Rip11 is a Rab11- and AS160-RabGAP-binding protein required for insulin-stimulated glucose uptake in adipocytes

Welsh

Leney

Lloyd-Lewis

et al. 2007

Journal of Cell Science

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The translocation of GLUT4 to the plasma membrane underlies the ability of insulin to stimulate glucose uptake, an event that involves the activation of protein kinase B, several members of the Rab family of GTP-binding proteins and the phosphorylation of the Rab GTPase-activating protein AS160. Here, we explored the regulation by insulin of the class I Rab11-interacting proteins Rip11, RCP and FIP2. We show that Rip11, but not RCP or FIP2, translocates to the plasma membrane of 3T3-L1 adipocytes in response to insulin. This unique response of Rip11 prompted us to explore the role of this protein in more detail. We found that Rip11 partially colocalises with GLUT4 in intracellular compartments. siRNA-mediated knockdown of Rip11 inhibits insulin-stimulated uptake of 2-deoxyglucose, and overexpression of Rip11 blocks insulin-stimulated insertion of translocated GLUT4 vesicles into the plasma membrane. We additionally show that Rip11 forms a complex with AS160 in a Rab11-independent manner and that insulin induces dissociation of AS160 from Rip11. We propose that Rip11 is an AS160- and Rab-binding protein that coordinates the protein kinase signalling and trafficking machinery required to stimulate glucose uptake in response to insulin.

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Section: Discussionmentioning

confidence: 99%

Rip11 is a Rab11- and AS160-RabGAP-binding protein required for insulin-stimulated glucose uptake in adipocytes

Welsh

Leney

Lloyd-Lewis

et al. 2007

Journal of Cell Science

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“…Indeed, the recombinant full-length Rip11 binds poorly to Rab11a in pulldown and yeast two-hybrid assays as compared with full-length endogenous Rip11 from cellular TX-100 extracts (data not shown). Furthermore, it has been previously shown that Rip11 can also interact with ␥SNAP and cytoskeleton (13,24). Thus, the interactions of Rips and Eferin with different factors could be used as a means of differentially regulating Rab11/25 binding.…”

Section: Fig 3 Identification Of the Rbd11 Conserved In Rip Andmentioning

confidence: 99%

Identification of a Novel Rab11/25 Binding Domain Present in Eferin and Rip Proteins

Prekeris¹,

Davies²,

Scheller³

2001

Journal of Biological Chemistry

103

123

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Rab11, a low molecular weight GTP-binding protein, has been shown to play a key role in a variety of cellular processes, including endosomal recycling, phagocytosis, and transport of secretory proteins from the trans-Golgi network. In this study we have described a novel Rab11 effector, EF-hands-containing Rab11-interacting protein (Eferin). In addition, we have identified a 20-amino acid domain that is present at the C terminus of Eferin and other Rab11/25-interacting proteins, such as Rip11 and nRip11. Using biochemical techniques we have demonstrated that this domain is necessary and sufficient for Rab11 binding in vitro and that it is required for localization of Rab11 effector proteins in vivo. The data suggest that various Rab effectors compete with each other for binding to Rab11/25 possibly accounting for the diversity of Rab11 functions.

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“…In addition to NSF, which we have previously reported , several SNARE proteins, SNARE-associated proteins (Sly1/Sec1-family domain containing proteins 1 and 2, SCFD1 and SCFD2, respectively), α-SNAP and other membranetrafficking-related proteins -including clathrin heavy chain and phosphoinositide phosphatase Sac1 -were detected. Among these, we decided to focus on SNAREs because their interactions with γ-SNAP have remained poorly characterized (Chen et al, 2001;Hong, 2005;Tani et al, 2003).…”

Section: γ-Snap Preferentially Binds To Endosomal Snaresmentioning

confidence: 99%

“…In contrast to the considerable contribution of α-SNAP and β-SNAP to SNARE complexes in membrane trafficking events, the biochemical and cellular functions of γ-SNAP remain poorly understood. Yeast twohybrid screening experiments have revealed that γ-SNAP interacts with γ-SNAP-associated factor-1 [Gaf-1; also known as Rab11-interacting protein (Rip11) and Rab11-family interacting protein 5 (FIP5)], γ-tubulin and NSF (Chen et al, 2001;Tani et al, 2003). The two-hybrid assay also revealed that γ-SNAP does not bind to at least to six of the SNAREs tested, including STX4 and STX18, although α-SNAP does bind to them .…”

Section: Introductionmentioning

confidence: 99%

γ-SNAP stimulates disassembly of endosomal SNARE complexes and regulates endocytic trafficking pathways

Inoue

Matsuzaki

Tanaka

et al. 2015

Journal of Cell Science

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Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) that reside in the target membranes and transport vesicles assemble into specific SNARE complexes to drive membrane fusion. N-ethylmaleimide-sensitive factor (NSF) and its attachment protein, α-SNAP (encoded by NAPA), catalyze disassembly of the SNARE complexes in the secretory and endocytic pathways to recycle them for the next round of fusion events. γ-SNAP (encoded by NAPG) is a SNAP isoform, but its function in SNARE-mediated membrane trafficking remains unknown. Here, we show that γ-SNAP regulates the endosomal trafficking of epidermal growth factor (EGF) receptor (EGFR) and transferrin. Immunoprecipitation and mass spectrometry analyses revealed that γ-SNAP interacts with a limited range of SNAREs, including endosomal ones. γ-SNAP, as well as α-SNAP, mediated the disassembly of endosomal syntaxin-7-containing SNARE complexes. Overexpression and small interfering (si)RNA-mediated depletion of γ-SNAP changed the morphologies and intracellular distributions of endosomes. Moreover, the depletion partially suppressed the exit of EGFR and transferrin from EEA1-positive early endosomes to delay their degradation and uptake. Taken together, our findings suggest that γ-SNAP is a unique SNAP that functions in a limited range of organelles -including endosomesand their trafficking pathways.

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Gaf-1, a γ-SNAP-binding Protein Associated with the Mitochondria

Cited by 19 publications

References 57 publications

Rip11 is a Rab11- and AS160-RabGAP-binding protein required for insulin-stimulated glucose uptake in adipocytes

Rip11 is a Rab11- and AS160-RabGAP-binding protein required for insulin-stimulated glucose uptake in adipocytes

Identification of a Novel Rab11/25 Binding Domain Present in Eferin and Rip Proteins

γ-SNAP stimulates disassembly of endosomal SNARE complexes and regulates endocytic trafficking pathways

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