Docking of Yeast Vacuoles Is Catalyzed by the Ras-like GTPase Ypt7p after Symmetric Priming by Sec18p (NSF)

Vacuole inheritance in yeast involves the formation of tubular and vesicular “segregation structures” which migrate into the bud and fuse there to establish the daughter cell vacuole. Vacuole fusion has been reconstituted in vitro and may be used as a model for an NSF-dependent reaction of priming, docking, and fusion. We have developed biochemical and microscopic assays for the docking step of in vitro vacuole fusion and characterized its requirements. The vacuoles must be primed for docking by the action of Sec17p (α-SNAP) and Sec18p (NSF). Priming is necessary for both fusion partners. It produces a labile state which requires rapid docking in order to lead productively to fusion. In addition to Sec17p/Sec18p, docking requires the activity of the Ras-like GTPase Ypt7p. Unlike Sec17p/Sec18p, which must act before docking, Ypt7p is directly involved in the docking process itself.

[1]  E. Muller,et al.  A Heterodimer of Thioredoxin and IB 2 Cooperates with Sec18p (NSF) to Promote Yeast Vacuole Inheritance , 1997, The Journal of cell biology.

[2]  W. Wickner,et al.  Homotypic vacuole fusion requires Sec17p (yeast alpha‐SNAP) and Sec18p (yeast NSF). , 1996, The EMBO journal.

[3]  A. Mayer,et al.  Sec18p (NSF)-Driven Release of Sec17p (α-SNAP) Can Precede Docking and Fusion of Yeast Vacuoles , 1996, Cell.

[4]  J. H. Chou,et al.  Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras. , 1996, The EMBO journal.

[5]  P. De Camilli,et al.  Phosphoinositides as Regulators in Membrane Traffic , 1996, Science.

[6]  S. Sapperstein,et al.  Assembly of the ER to Golgi SNARE complex requires Uso1p , 1996, The Journal of cell biology.

[7]  Z. Xu,et al.  Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae , 1996, The Journal of cell biology.

[8]  J. Rothman,et al.  A possible docking and fusion particle for synaptic transmission , 1995, Nature.

[9]  M. Zerial,et al.  Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion , 1995, Cell.

[10]  W. Wickner,et al.  The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance. , 1995, The EMBO journal.

[11]  J. Peters,et al.  An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic golgi fragments , 1995, Cell.

[12]  U. Acharya,et al.  The formation of golgi stacks from vesiculated golgi membranes requires two distinct fusion events , 1995, Cell.

[13]  R. Schekman,et al.  Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes , 1995, Cell.

[14]  R. Burgoyne,et al.  Distinct effects of alpha-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis , 1995, The Journal of cell biology.

[15]  P. Hanson,et al.  The N-Ethylmaleimide-sensitive Fusion Protein and α-SNAP Induce a Conformational Change in Syntaxin (*) , 1995, The Journal of Biological Chemistry.

[16]  Thomas C. Südhof,et al.  The synaptic vesicle cycle: a cascade of protein–protein interactions , 1995, Nature.

[17]  E. Ikonen,et al.  Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells , 1995, Cell.

[18]  J. Rothman,et al.  SNAP-mediated protein–protein interactions essential for neurotransmitter release , 1995, Nature.

[19]  W. Neupert,et al.  Mitochondrial protein import: Reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding , 1995, Cell.

[20]  S. Ferro-Novick,et al.  Ypt1p implicated in v-SNARE activation , 1994, Nature.

[21]  J. Rothman,et al.  Mechanisms of intracellular protein transport , 1994, Nature.

[22]  P. Brennwald,et al.  Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis , 1994, Cell.

[23]  T. Südhof,et al.  Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-binding protein, depends on rab3A/3C , 1994, Neuron.

[24]  R. Burgoyne,et al.  SNAP‐25 is present in a SNARE complex in adrenal chromaffin cells , 1994, FEBS letters.

[25]  W. Wickner,et al.  Determination of four biochemically distinct, sequential stages during vacuole inheritance in vitro , 1994, The Journal of cell biology.

[26]  W. Wickner,et al.  G-protein ligands inhibit in vitro reactions of vacuole inheritance , 1994, The Journal of cell biology.

[27]  P. Woodman,et al.  Multiple N-ethylmaleimide-sensitive components are required for endosomal vesicle fusion. , 1994, Molecular biology of the cell.

[28]  P. Novick,et al.  GDI1 encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway. , 1994, EMBO Journal.

[29]  Mark K. Bennett,et al.  A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion , 1993, Cell.

[30]  Paul Tempst,et al.  SNAP receptors implicated in vesicle targeting and fusion , 1993, Nature.

[31]  R. Stuart,et al.  Inhibition of intra-Golgi transport in vitro by mitotic kinase. , 1993, The Journal of biological chemistry.

[32]  M. Colombo,et al.  Control of protein traffic between distinct plasma membrane domains. Requirement for a novel 108,000 protein in the fusion of transcytotic vesicles with the apical plasma membrane. , 1993, The Journal of biological chemistry.

[33]  S. Emr,et al.  In vitro reactions of vacuole inheritance in Saccharomyces cerevisiae , 1992, The Journal of cell biology.

[34]  J. Hay,et al.  Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins , 1992, The Journal of cell biology.

[35]  R. Schekman,et al.  The yeast SEC17 gene product is functionally equivalent to mammalian alpha-SNAP protein. , 1992, The Journal of biological chemistry.

[36]  J. Rothman,et al.  A multisubunit particle implicated in membrane fusion , 1992, The Journal of cell biology.

[37]  P. Cohen,et al.  Cell-free fusion of endocytic vesicles is regulated by phosphorylation , 1992, The Journal of cell biology.

[38]  C. Woldringh,et al.  Vacuolar segregation to the bud of Saccharomyces cerevisiae: an analysis of morphology and timing in the cell cycle. , 1991, Journal of general microbiology.

[39]  R. Schekman,et al.  Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles , 1991, The Journal of cell biology.

[40]  S. Emr,et al.  Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant , 1991, The Journal of cell biology.

[41]  J. Rothman,et al.  SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast , 1990, Cell.

[42]  R. Schekman,et al.  Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway , 1990, Cell.

[43]  M. Dorée,et al.  Inhibition of endocytic vesicle fusion in vitro by the cell-cycle control protein kinase cdc2 , 1989, Nature.

[44]  P. Stahl,et al.  In vitro clustering and multiple fusion among macrophage endosomes. , 1989, The Journal of biological chemistry.

[45]  E. Chen,et al.  A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast , 1989, Nature.

[46]  J. Rothman,et al.  Vesicle fusion following receptor-mediated endocytosis requires a protein active in Golgi transport , 1989, Nature.

[47]  J. Rothman,et al.  Vesicular transport between the endoplasmic reticulum and the Golgi stack requires the NEM-sensitive fusion protein , 1989, Nature.

[48]  D. Eberhard,et al.  MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis. , 1989, The Journal of biological chemistry.

[49]  J. Rothman,et al.  Dissection of a single round of vesicular transport: Sequential intermediates for intercisternal movement in the Golgi stack , 1989, Cell.

[50]  L. Weisman,et al.  Intervacuole exchange in the yeast zygote: a new pathway in organelle communication. , 1988, Science.

[51]  S. Pfeffer.  Transport vesicle docking: SNAREs and associates. , 1996, Annual review of cell and developmental biology.

[52]  W. Balch,et al.  GTPases: multifunctional molecular switches regulating vesicular traffic. , 1994, Annual review of biochemistry.

[53]  C. J. Roberts,et al.  Biogenesis of the vacuole in Saccharomyces cerevisiae. , 1992, International review of cytology.