Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion.
about
Phosphorylation of SNAP-23 by the novel kinase SNAK regulates t-SNARE complex assemblyThe DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8.Convergence and divergence in the mechanism of SNARE binding by Sec1/Munc18-like proteinsThe R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomesThe yeast mutant vps5Delta affected in the recycling of Golgi membrane proteins displays an enhanced vacuolar Mg2+/H+ exchange activityGS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREsCell-free reconstitution of microautophagic vacuole invagination and vesicle formationThe Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery.Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late GolgiThree v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.Permease recycling and ubiquitination status reveal a particular role for Bro1 in the multivesicular body pathway.Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage.Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast.Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6.The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion.The yeast ATP-binding cassette (ABC) transporter Ycf1p enhances the recruitment of the soluble SNARE Vam7p to vacuoles for efficient membrane fusion.The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain.Fusion of docked membranes requires the armadillo repeat protein Vac8p.A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusionPositive and negative regulation of a SNARE protein by control of intracellular localization.Disassembly of all SNARE complexes by N-ethylmaleimide-sensitive factor (NSF) is initiated by a conserved 1:1 interaction between α-soluble NSF attachment protein (SNAP) and SNARE complexSNAP-23 participates in SNARE complex assembly in rat adipose cellsDual acylation accounts for the localization of {alpha}19-giardin in the ventral flagellum pair of Giardia lamblia.Phylogeny of the SNARE vesicle fusion machinery yields insights into the conservation of the secretory pathway in fungiInteractions between syntaxins identify at least five SNARE complexes within the Golgi/prevacuolar system of the Arabidopsis cell.Yeast vacuoles and membrane fusion pathwaysMembrane tethering and fusion in the secretory and endocytic pathways.Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly.Vibrio effector protein VopQ inhibits fusion of V-ATPase-containing membranes.A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.Vacuole acidification is required for trans-SNARE pairing, LMA1 release, and homotypic fusionRapid mapping of insertional mutations to probe cell wall regulation in Cryptococcus neoformans.Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles.Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusionA cycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusionThe docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt proteinProteins needed for vesicle budding from the Golgi complex are also required for the docking step of homotypic vacuole fusion.
P2860
Q22010905-BCBA7ECD-19BD-41F8-8B1A-8AC4256FA7BEQ24536275-79C0EC5E-2C61-44AF-9FF7-7F693C55CA0BQ24541277-7D59E305-1FF7-402A-A017-9AAB180218B7Q24550767-BC7150C3-F8D1-4A63-842A-5C1778620F46Q24555771-9F90F480-A0BA-4361-B218-7E757A4BB5EFQ24644645-61C6EDDD-C1D0-43F3-94B5-40108E24CFE0Q24656954-53922979-3519-4C4E-8295-866A017377EFQ24683797-8907D58F-580C-4A9D-8063-B3E08DCFA276Q27931175-C9A14606-6610-4382-A7F1-1FA4C7217413Q27932636-DEEE1B20-AB84-4CBC-9751-A0C8BB4D80B2Q27932817-8215E843-4F45-437F-9EBC-8AFD13D6843EQ27933496-AA4354C9-00B4-441B-BA80-EE527AE57960Q27934032-4092280F-B82D-4AA9-B11C-F13D9D5B59A5Q27934041-A557ED05-C9EB-4355-8E8B-36C7F7A8A22FQ27934382-0529E2DE-A541-4D32-906D-6E190CC4B8B3Q27934671-F2931F83-A920-42A7-92EB-484A9782652CQ27936291-2C2015AB-F1A2-4EE0-933D-CAEF3F360D02Q27936803-C478B537-874C-4725-AD79-2E2A30D0CCCEQ27937772-3FBC6745-634A-46E8-B067-7DB834E076B9Q27939110-2840747E-DDC0-46B6-9836-7E3904A47B58Q27940373-EE2F4844-4C91-4972-97E8-A2A080AED89CQ28565327-065D20E5-AABA-4658-8FF1-A876D5A0166DQ28581582-CD9119DB-3C19-4030-B9EF-FDEAF9F3BE75Q30490764-4FC9DD8F-0914-476A-9405-588D8D5D29BFQ33402655-F6B0E6DB-B2BA-49AC-9ADF-8C5404B2BE67Q33948745-E7BD0C64-DF41-4562-BA3A-7FDF40482BACQ34086175-DA0C7697-7002-4B55-9C24-FEEFB2FAD8A3Q34156712-92753D04-786F-48B6-8AAF-74137CE4F610Q34386086-6A3EE3C2-C37F-4B04-9050-626BB63B9A2FQ34926211-065EBBC8-9174-4EFF-8E7B-EB68FD814D0CQ35189942-ACF1ED88-2AF7-468F-A261-67B8AF37DB02Q35608147-C1EB67A6-E344-4D2B-AA6E-18A98C6DF74BQ35642673-3FADE3FC-73AB-470D-972C-8AC5E34A3B88Q35674956-2841A846-8B0E-4F57-878C-84F57328AE77Q36322360-BFE4CA5B-FB31-4DC5-BFD2-08A7AE19D924Q36322803-18050716-3F27-4AAC-BC39-B11C24312B77Q36322950-981DA556-44E5-4ED4-B389-3FE70050767CQ36324115-8995B8DF-8E74-4110-8C3F-942CC42BFE1BQ36326304-BB343BD1-2840-4648-B8D8-4401E6578C83Q36326324-B19FC566-53E2-4076-8BAB-05AA8E40072F
P2860
Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@ast
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@en
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@nl
type
label
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@ast
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@en
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@nl
prefLabel
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@ast
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@en
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@nl
P2860
P356
P1433
P1476
Vam7p, a vacuolar SNAP-25 homo ...... nd vacuole docking and fusion.
@en
P2093
Ungermann C
P2860
P304
P356
10.1093/EMBOJ/17.12.3269
P407
P577
1998-06-01T00:00:00Z