Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells.
about
Vacuolar protein sorting mechanisms in plantsThe ER-Membrane Transport System Is Critical for Intercellular Trafficking of the NSm Movement Protein and Tomato Spotted Wilt TospovirusTales of tethers and tentacles: golgins in plants.New putative chloroplast vesicle transport components and cargo proteins revealed using a bioinformatics approach: an Arabidopsis modelThe B7-1 cytoplasmic tail enhances intracellular transport and mammalian cell surface display of chimeric proteins in the absence of a linear ER export motif.Dual-targeting of Arabidopsis DMP1 isoforms to the tonoplast and the plasma membraneStacks off tracks: a role for the golgin AtCASP in plant endoplasmic reticulum-Golgi apparatus tethering.A membrane-tethered transcription factor defines a branch of the heat stress response in Arabidopsis thaliana.Advances in fluorescent protein-based imaging for the analysis of plant endomembranes.What is moving in the secretory pathway of plants?ER and vacuoles: never been closer.The plant Golgi apparatus: last 10 years of answered and open questions.The YXXΦ motif within the severe acute respiratory syndrome coronavirus (SARS-CoV) 3a protein is crucial for its intracellular transport.Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plantsThe secreted plant N-glycoproteome and associated secretory pathwaysTrafficking of plant plasma membrane aquaporins: multiple regulation levels and complex sorting signals.Is the 6 kDa tobacco etch viral protein a bona fide ERES marker?Evidence for the localization of the Arabidopsis cytokinin receptors AHK3 and AHK4 in the endoplasmic reticulum.Multiple cytosolic and transmembrane determinants are required for the trafficking of SCAMP1 via an ER-Golgi-TGN-PM pathway.Diacidic motif is required for efficient transport of the K+ channel KAT1 to the plasma membrane.Protein composition of 6K2-induced membrane structures formed during Potato virus A infection.Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes.Salt stress triggers enhanced cycling of Arabidopsis root plasma-membrane aquaporins.A novel di-acidic motif facilitates ER export of the syntaxin SYP31.Arabidopsis synaptotagmin SYT1, a type I signal-anchor protein, requires tandem C2 domains for delivery to the plasma membrane.Golgi membrane dynamics after induction of a dominant-negative mutant Sar1 GTPase in tobacco.Localization and trafficking of an isoform of the AtPRA1 family to the Golgi apparatus depend on both N- and C-terminal sequence motifs.Trans-Golgi network-located AP1 gamma adaptins mediate dileucine motif-directed vacuolar targeting in Arabidopsis.Golgi-dependent transport of vacuolar sorting receptors is regulated by COPII, AP1, and AP4 protein complexes in tobacco.An Arabidopsis prenylated Rab acceptor 1 isoform, AtPRA1.B6, displays differential inhibitory effects on anterograde trafficking of proteins at the endoplasmic reticulum.Routes to the tonoplast: the sorting of tonoplast transporters in Arabidopsis mesophyll protoplasts.Putative glycosyltransferases and other plant Golgi apparatus proteins are revealed by LOPIT proteomics.The endoplasmic reticulum is a hub to sort proteins toward unconventional traffic pathways and endosymbiotic organelles.Molecular and biochemical characterizations of the monoacylglycerol lipase gene family of Arabidopsis thaliana.A new LxxxA motif in the transmembrane Helix3 of maize aquaporins belonging to the plasma membrane intrinsic protein PIP2 group is required for their trafficking to the plasma membrane.The Golgi-localized Arabidopsis endomembrane protein12 contains both endoplasmic reticulum export and Golgi retention signals at its C terminus.Identification of sorting motifs of AtβFruct4 for trafficking from the ER to the vacuole through the Golgi and PVC.Assembly and sorting of the tonoplast potassium channel AtTPK1 and its turnover by internalization into the vacuole.Mechanisms and effects of retention of over-expressed aquaporin AtPIP2;1 in the endoplasmic reticulum.Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway.
P2860
Q27026111-5F29C793-F87B-478E-A5CD-4483C9252F3FQ27315865-6FCD2B14-70B6-4504-BF9A-07C2FBD08222Q34275325-2739C380-421D-4178-9B4A-ABF7C5B46AB0Q34661772-549FDE20-C3A4-4D57-B736-887970198258Q35000777-ED27E1E4-897B-43FC-AF6B-41B496F6134FQ36337942-E212A49F-00A1-45B5-8A6D-9DE7C72623D5Q36399391-D208AC03-3F3F-4591-BBA8-67B6F588D56CQ36945136-8F1639A2-7D6C-4500-B7AC-94AD80EB8B46Q37234773-51DD6D39-6C70-462C-9BC2-45014B91C0C0Q37234781-319FE343-ADF6-4BF1-B41A-3CA4CFDCAA23Q37552224-56788EB4-196B-48EF-9847-0C3DF2833C3DQ37607551-E07B235E-D3A2-42D3-9B91-A0DDD59D4118Q37732056-E28D2CE3-DE68-4AD9-AE25-F205772B2F81Q37838613-C48C341D-48E6-4ECA-BEDF-E82CAFE22B72Q38017660-81E7A579-363F-4DE0-A5E4-E8D825170B5CQ38292541-18746762-C5B3-4470-B36C-8944AB2B427BQ38699836-DAA8AA3B-3B51-482D-94FA-DF0751F71EE4Q39337421-4048D1AF-11E3-400B-A2E3-851F13AD4F58Q39605257-149EC0C0-AC1D-4873-BC3C-D403CABB2FD6Q40236569-2FE3B146-2E99-4A08-91E0-C1876C2F97E0Q40314991-DBE6FADA-8553-4E14-A603-6ED89B2B09EBQ41590118-648F4590-42FC-4AE2-8FE8-E19F2A93EB76Q41906039-BBAC9E9E-FF20-4D6D-B58B-0FA86F9F0A2DQ42631402-85F17EDA-8F71-4606-A7F4-C2608BCC5E32Q42724452-4394C08F-6DA7-40DF-8988-768B9C06838BQ43253811-F48E3CDB-48BC-4E4F-963D-3F5BD5E75C2FQ44879164-A727529B-65E2-4167-BFB7-69B2B0E1E46FQ44994308-819719D8-40E0-40E3-9A46-52C9F3A3A6D9Q45170524-69CB966E-0969-4180-B51E-4122C808A72AQ46141858-9A2ED63C-E540-4826-936F-3D97363389CCQ46779068-95375430-4D59-45F4-BA99-2AE36D381388Q47220653-3465138F-FA81-43AA-8853-1DB5BB92B5BCQ47676453-09CD499A-CC5A-4D0F-BF72-D38FD846B661Q47881776-FEE9D2C0-D5AC-4780-BEC3-BA250B395CC8Q47994777-F5BFFB90-A311-486F-A844-F1ABF6DDEB04Q50497324-D8962E53-FA6F-4AC8-BBBE-B58F706DA3D1Q50512873-B7ABE0E9-2C64-4E25-8477-89C5D4C7F481Q50518139-BF7709C1-4B2F-421C-A5FE-671409390A24Q50530442-71E54236-481B-4C69-BC94-693C3303019AQ50706444-8CA8545C-1C0B-4F45-8EDB-777661A4A217
P2860
Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Diacidic motifs influence the ...... smic reticulum in plant cells.
@en
Diacidic motifs influence the ...... smic reticulum in plant cells.
@nl
type
label
Diacidic motifs influence the ...... smic reticulum in plant cells.
@en
Diacidic motifs influence the ...... smic reticulum in plant cells.
@nl
prefLabel
Diacidic motifs influence the ...... smic reticulum in plant cells.
@en
Diacidic motifs influence the ...... smic reticulum in plant cells.
@nl
P2860
P50
P356
P1433
P1476
Diacidic motifs influence the ...... smic reticulum in plant cells.
@en
P2093
Sally L Hanton
P2860
P304
P356
10.1105/TPC.105.034900
P577
2005-10-07T00:00:00Z