Asymmetric phospholipid distribution drives
            <i>in vitro</i>
            reconstituted SNARE-dependent membrane fusion

Vicogne, Jérôme; Vollenweider, Daniel; Smith, Jeffery R.; Huang, Ping; Frohman, Michael A.; Pessin, Jeffrey E.

doi:10.1073/pnas.0606881103

Cited by 103 publications

(89 citation statements)

References 32 publications

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“…In the presence of insulin, however, these transport vesicles have increased pausing (tethering) at the plasma membrane with a higher probability of plasma membrane fusion. Kinetic analysis and the development of a novel in vitro plasma membrane fusion assay are consistent with GLUT4 vesicle plasma membrane fusion as the key insulin-regulated step in the translocation process [24,25].…”

Section: Glut4 Intracellular Retention and Exocytosismentioning

confidence: 60%

“…The SNAP isoforms possess 2 coiled-coil domains and are usually link to the plasma membrane by palmitoylation. These t-SNAREs are localized on the acceptor or target compartment [24,43,44]. The assembly of a four helical bundle composed of one helix from the v-SNARE and three helices from the t-SNAREs provide the minimal machinery to drive vesicle fusion both in reconstituted and cellular systems [24,25].…”

Section: Glut4 Vesicle Docking and Plasma Membrane Fusionmentioning

confidence: 99%

“…For example, product of phospholipase D (PLD), phosphatidic acid (PA) appears to play an important role as diminished PA production was found to inhibit GLUT4 plasma membrane fusion without affecting trafficking or docking/tethering [90]. Moreover, in vitro reconstitution studies demonstrated that PA in the syntaxin4/SNAP23 acceptor membrane markedly accelerated the rate of fusion whereas PA in the VAMP2 donor vesicles was inhibitory [24]. As it is well established that insulin alters the lipid composition of various intracellular membranes, further studies are still need to address the specific roles of the donor and acceptor lipid membrane environments as the potential target events responsible for the control of GLUT4 vesicle plasma membrane fusion.…”

Section: Insulin Signaling Leading To Glut4 Translocationmentioning

confidence: 99%

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Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Hou

Pessin

2007

Current Opinion in Cell Biology

132

116

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SummaryGlucose transporter 4 (GLUT4) is the major insulin regulated glucose transporter expressed mainly in muscle and adipose tissue. GLUT4 is stored in a poorly characterized intracellular vesicular compartment and translocates to the cell surface in response to insulin stimulation resulting in increase glucose uptake. This process is essential for the maintenance of normal glucose homeostasis and involves a complex interplay of trafficking events and intracellular signaling cascades. Recent studies have identified sortilin as an essential element for the formation of GLUT4 storage vesicles during adipogenesis and GGA (Golgi-localized γ-ear-containing Arf-binding protein) as a key coat adaptor for the entry of newly synthesized GLUT4 into the specialized compartment. Insulinstimulated GLUT4 translocation from this compartment to the plasma membrane appears to require the Akt/protein kinase B substrate, termed AS160 (Akt Substrate of 160 kDa). In addition, the VPS9 domain-containing protein Gapex-5 in complex with CIP4 appears to function as a Rab31 guanylnucleotide exchange factor that is necessary for insulin-stimulated GLUT4 translocation. Here we attempt to summaries recent advances in GLUT4 vesicle biogenesis, intracellular trafficking and membrane fusion.

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Section: Glut4 Intracellular Retention and Exocytosismentioning

confidence: 60%

Section: Glut4 Vesicle Docking and Plasma Membrane Fusionmentioning

confidence: 99%

Section: Insulin Signaling Leading To Glut4 Translocationmentioning

confidence: 99%

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Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Hou

Pessin

2007

Current Opinion in Cell Biology

132

116

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“…Fusion is regulated by NSF (N-ethylmaleimide-sensitive factor)/ Sec18p, ␣SNAP (soluble NSF attachment protein)/Sec17p, SNAREs (SNAP receptors), Sec1p/Munc18-1p family (SM) proteins, Rab GTPases, and Rab:GTP-binding proteins, termed ''Rab effectors'' (1-3). Lipids, including phosphoinositides, sterols, diacylglycerol (DAG), and phosphatidic acid (PA), have specific roles in fusion (4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14). Proteins and lipids cooperate for their enrichment in membrane fusion microdomains (6,8,15,16).…”

mentioning

confidence: 99%

Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion

Mima

Wickner

2009

Proc. Natl. Acad. Sci. U.S.A.

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Yeast vacuole fusion requires 4 SNAREs, 2 SNARE chaperone systems (Sec17p/Sec18p/ATP and the HOPS complex), and 2 phosphoinositides, phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P 2]. By reconstituting proteoliposomal fusion with purified components, we now show that phosphoinositides have 4 distinct roles: PI(3)P is recognized by the PX domain of the SNARE Vam7p; PI(3)P enhances the capacity of membrane-bound SNAREs to drive fusion in the absence of SNARE chaperones; either PI(3)P or PI(4,5)P 2 can activate SNARE chaperones for the recruitment of Vam7p into fusion-competent SNARE complexes; and either PI(3)P or PI(4,5)P 2 strikingly promotes synergistic SNARE complex remodeling by Sec17p/Sec18p/ATP and HOPS. This ternary synergy of phosphoinositides and 2 SNARE chaperone systems is required for rapid fusion.I ntracellular membrane fusion is a conserved reaction, vital for vesicle trafficking, hormone secretion, and neurotransmission. Fusion is regulated by NSF (N-ethylmaleimide-sensitive factor)/ Sec18p, ␣SNAP (soluble NSF attachment protein)/Sec17p, SNAREs (SNAP receptors), Sec1p/Munc18-1p family (SM) proteins, Rab GTPases, and Rab:GTP-binding proteins, termed ''Rab effectors'' (1-3). Lipids, including phosphoinositides, sterols, diacylglycerol (DAG), and phosphatidic acid (PA), have specific roles in fusion (4-14). Proteins and lipids cooperate for their enrichment in membrane fusion microdomains (6,8,15,16). SNARE proteins are integral or peripheral membrane proteins required for membrane fusion. SNAREs have either a Q or R residue at the center of their SNARE domain and associate in 4-helical QabcR complexes in cis (anchored to one membrane) or in trans (anchored to apposed membranes), where a, b, and c are families of related Q-SNAREs (2, 17, 18). Reconstituted proteoliposomes (RPLs) bearing Q-SNAREs fuse with RPLs bearing an R-SNARE through trans- 20). This fusion has slow kinetics, requires nonphysiologically high SNARE densities, and causes substantial leakage of luminal contents of the RPLs (21-24).We study membrane fusion with yeast vacuoles (lysosomes). Vacuole fusion (25) requires 3 Q-SNAREs (Vam3p, Vti1p, and Vam7p) and 1R-SNARE (Nyv1p) (26, 27), two SNARE chaperone systems, Sec17p/Sec18p/ATP (28), and the HOPS (homotypic fusion and vacuole protein sorting)/Vps Class C complex (29, 30), the Rab-GTPase Ypt7p (31), and chemically minor but functionally vital ''regulatory lipids'': ergosterol (ERG), DAG, PI(3)P, and PI(4,5)P 2 (8). Inactive 4SNARE cis-complexes on isolated organelles are disassembled by Sec17p/Sec18p/ATP (27). The heterohexameric HOPS complex, containing the SM protein Vps33p as a subunit, promotes and proofreads SNAREcomplex assembly (32-34). HOPS can physically interact with the Q-SNAREs [Vam7p (35) and Vam3p (36, 37)], 4SNARE cis-complexes (32), GTP-bound Ypt7p (29), and phosphoinositides (35). PI(3)P supports the membrane association of the Qc-SNARE Vam7p, which has no transmembrane domain, through binding its PX domain (38). SNAREs, ...

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“…Mutations in a mitochondrial-specific phospholipase D fail to generate phosphatidic acid. Phospholipase D is also necessary for SNARE-based fusion reactions (Nakanishi et al, 2006;Vicogne et al, 2006). Importantly, the phospholipase acts Outside of the secretory pathway, organelle fusion is not mediated by the SNARE proteins.…”

Section: Non-snare-based Organelle Fusionmentioning

confidence: 99%

In VivoAnalysis of Membrane Fusion

Palfreyman¹,

Jørgensen²

2009

Encyclopedia of Life Sciences

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Membranes provide a barrier that allows chemical reactions to be isolated from the environment. The plasma membrane, for example, delineates self from nonself, and thus must have played an essential role in the evolution of life. Yet under numerous circumstances it is equally important that membranes be breached. Numerous forces oppose the spontaneous fusion of membranes; thus, specialized proteins have evolved to fuse membranes. The most well-understood fusion proteins are the viral fusion proteins and the SNARE proteins used in the secretory pathway. In addition, recent discoveries have lead to models for the fusion of organelles such as mitochondria and peroxisomes, as well as for cell-cell fusion. Despite the diverse structures of fusion proteins, it is possible that they function to drive membranes through a series of common lipid intermediates. Here we review the mechanisms of fusion for biological membranes, and highlight the similarities and differences in these processes.

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Asymmetric phospholipid distribution drives in vitro reconstituted SNARE-dependent membrane fusion

Cited by 103 publications

References 32 publications

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion

In VivoAnalysis of Membrane Fusion

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