Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
about
The SNX-PX-BAR family in macropinocytosis: the regulation of macropinosome formation by SNX-PX-BAR proteinsMyotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated in myotubular myopathy and type 4B Charcot-Marie-Tooth diseaseSNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis.The PX-BAR membrane-remodeling unit of sorting nexin 9The PX-domain protein SNX17 interacts with members of the LDL receptor family and modulates endocytosis of the LDL receptorEvidence for a role of SNX16 in regulating traffic between the early and later endosomal compartmentsThe structural basis of novel endosome anchoring activity of KIF16B kinesinIdentification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motifSorting nexin 12 interacts with BACE1 and regulates BACE1-mediated APP processingRME-8 coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation.Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member.Endosomal localization and function of sorting nexin 1The Phox homology (PX) domain, a new player in phosphoinositide signallingThe beta-appendages of the four adaptor-protein (AP) complexes: structure and binding properties, and identification of sorting nexin 9 as an accessory protein to AP-2Sorting nexin 17 facilitates LRP recycling in the early endosome.Molecular basis for substrate recognition by MTMR2, a myotubularin family phosphoinositide phosphatase.Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagyTCGAP, a multidomain Rho GTPase-activating protein involved in insulin-stimulated glucose transportThe retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domainPhosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activationHow PI3K-derived lipids control cell divisionTrafficking regulation of proteins in Alzheimer's diseaseClass III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane trafficPhosphoinositides: tiny lipids with giant impact on cell regulationStructure and functional interactions of the Tsg101 UEV domain.Structure and Ubiquitin Interactions of the Conserved Zinc Finger Domain of Npl4Structure and ubiquitin binding of the ubiquitin-interacting motifCrystal structure of the yeast Phox homology (PX) domain protein Grd19p complexed to phosphatidylinositol-3-phosphateSolution structure of human sorting nexin 22Molecular characterization of the Ran-binding zinc finger domain of Nup153Structural and membrane binding analysis of the Phox homology domain of Bem1p: basis of phosphatidylinositol 4-phosphate specificityCrystal structures of PI3K-C2α PX domain indicate conformational change associated with ligand bindingMolecular mechanism of membrane docking by the Vam7p PX domain.Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 PtdIns 3-kinase in autophagy.Genome-scale analysis reveals Sst2 as the principal regulator of mating pheromone signaling in the yeast Saccharomyces cerevisiae.Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperonesPhosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusionHOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusionAll phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate.The phox homology (PX) domain protein interaction network in yeast.
P2860
Q21091096-1301B6B4-3545-4F0C-AF22-426AE3BB837BQ24291963-3FA33F53-B1AF-4267-897B-B3892AFD4A41Q24294599-5C3CF60E-0A29-4E5A-A13F-FDC1B9DA582DQ24298249-BBDFFAC4-2FD7-454A-8AC9-48E1EC3CE363Q24304115-DAD407D9-47E4-4597-9738-9BA8D07EDEB3Q24305485-16BB3099-1E77-422B-B3B4-0771CD9ADA76Q24321332-5096C118-C3CA-48DD-A26B-8E5E33B33790Q24338457-EEA72921-35F5-42CB-9E4D-BE0FF082B946Q24338519-AC92586F-7679-4F5A-A366-DABBA88A4E22Q24339406-17458848-1E03-479E-A6FD-01C73291BD0FQ24515262-E426F6E4-92BF-4B5D-BFBB-A612C8AA06CDQ24531264-45E80201-1057-4E66-8941-1EFB2A1E48F3Q24533547-0CF3B1CD-8D40-4F2C-A7C3-A1F0D254F947Q24533882-4A21BFEE-5150-45D1-A361-9F9C8D0EB2CCQ24535575-4093CA15-DFDC-4A28-BA85-339F3C2A47EEQ24538782-26F59A77-E874-4A26-99F4-B92318170B23Q24644121-47314190-2FAB-42A7-881C-71B1FE5FEBCBQ24671095-5608C368-D220-427B-BA1F-0C0580588106Q24673655-1BDBD7E9-EB45-4790-B2B1-E830BC103DDBQ24681540-6922BF39-AC80-4068-81D7-33256B38FEB6Q26781315-E87BBE81-D5A3-4298-9783-79901C89CB2CQ26825722-AB4CA621-47CE-43A1-9A2F-11BB121D5658Q26865657-8F6979E4-56F7-4371-9C80-D0350E1D2E6CQ27012953-8021077E-AC40-482B-9512-7057B01EB095Q27638973-554410C9-43C9-4DA0-A145-D3B350D8EF45Q27640720-1C439064-2EA2-4D8F-BAA4-F474E2AD212EQ27641265-4847A62D-7FC1-44F8-B608-3D48ED434AF3Q27642230-F13E87C7-2079-4A7E-A92C-628AC934D7ABQ27644307-2F9BBCD0-D5A9-4B13-B983-647B0B0F633FQ27644396-A4D339FD-DFB3-4193-B5CD-E435709D5990Q27646147-D96A2074-B472-4CF6-8D51-0B1282C4E9A6Q27649974-B7A533DB-5422-4B26-AEA1-DC60BBC92BAAQ27930182-DB696617-5B9E-482D-A936-86F1A9667BD8Q27930197-11F1F9AF-FC92-44A0-9363-216BDFA2961EQ27931421-1C7BF437-59E4-4F2D-9595-CD65B674172BQ27931637-22436A03-287C-42DB-B672-635027BD433EQ27931924-3BF0E396-F91A-4FB4-A9B2-0A724D095ACDQ27932357-1966ED37-DAAB-45B4-B035-99702FEA00B9Q27932927-61034A17-F08C-44C0-9498-89F6B8C879D4Q27932963-51290501-4DAD-4A7B-8268-6663CC50AE37
P2860
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
@ast
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
@en
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
@nl
type
label
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
@ast
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
@en
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
@nl
prefLabel
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
@ast
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
@en
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.
@nl
P2093
P356
P1433
P1476
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
@en
P2093
P2888
P304
P356
10.1038/35083000
P407
P577
2001-07-01T00:00:00Z
P6179
1051229723