Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor.
about
Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surfaceEpithelial cells in fetal intestine produce chemerin to recruit macrophagesAlpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recyclingProtein kinase D regulates basolateral membrane protein exit from trans-Golgi networkInteractions between adaptor protein-1 of the clathrin coat and microtubules via type 1a microtubule-associated proteinsCholesterol-sensitive modulation of transcytosis.Aqueous and micelle-bound structural characterization of the epidermal growth factor receptor juxtamembrane domain containing basolateral sorting motifs.The rat liver Na(+)/bile acid cotransporter. Importance of the cytoplasmic tail to function and plasma membrane targeting.Human cytomegalovirus glycoprotein B contains autonomous determinants for vectorial targeting to apical membranes of polarized epithelial cells.A membrane setting for the sorting motifs present in the adenovirus E3-13.7 protein which down-regulates the epidermal growth factor receptor.Direct interaction between Rab3D and the polymeric immunoglobulin receptor and trafficking through regulated secretory vesicles in lacrimal gland acinar cells.The membrane-proximal intracytoplasmic tyrosine residue of HIV-1 envelope glycoprotein is critical for basolateral targeting of viral budding in MDCK cells.Interactions between the exocytic and endocytic pathways in polarized Madin-Darby canine kidney cells.Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized Madin-Darby canine kidney cellsThe role of syntaxins in the specificity of vesicle targeting in polarized epithelial cells.Polarized sorting and trafficking in epithelial cellsAdaptor proteins involved in polarized sortingSelective alterations in biosynthetic and endocytic protein traffic in Madin-Darby canine kidney epithelial cells expressing mutants of the small GTPase Rac1.Adaptation of core mechanisms to generate cell polarity.Transcytosis: crossing cellular barriers.A unique element in the cytoplasmic tail of the type II transforming growth factor-beta receptor controls basolateral delivery.Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomesStructural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells.Cytoplasmic determinants involved in direct lysosomal sorting, endocytosis, and basolateral targeting of rat lgp120 (lamp-I) in MDCK cells.Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cellsSignal transduction by the polymeric immunoglobulin receptor suggests a role in regulation of receptor transcytosis.Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanismStructural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cellsSorting mechanisms regulating membrane protein traffic in the apical transcytotic pathway of polarized MDCK cellsMutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cellsTranscytosis of NgCAM in epithelial cells reflects differential signal recognition on the endocytic and secretory pathways.Redundant and distinct functions for dynamin-1 and dynamin-2 isoforms.Polarization and myelination in myelinating glia.Transduction of basolateral-to-apical signals across epithelial cells: ligand-stimulated transcytosis of the polymeric immunoglobulin receptor requires two signals.Role of tyrosine phosphorylation in ligand-induced regulation of transcytosis of the polymeric Ig receptor.Hepatocyte polarityRetromer maintains basolateral distribution of the type II TGF-β receptor via the recycling endosome.Mutations in the cytoplasmic domain of the Newcastle disease virus fusion protein confer hyperfusogenic phenotypes modulating viral replication and pathogenicityThe basolateral targeting signal of CD147 (EMMPRIN) consists of a single leucine and is not recognized by retinal pigment epithelium.Clathrin and AP1B: key roles in basolateral trafficking through trans-endosomal routes
P2860
Q22253386-9F01FC56-2BE6-47B6-9803-577AF7D11B52Q24310805-F887F6A0-F0DC-4B1E-A864-11096A202D5FQ24311523-768F65B8-ECBB-48FA-9519-C4A70F36801CQ24605796-63E4ECB9-07D5-495E-AB1B-4043F013F17BQ28202889-6AE804E5-E1D7-4ADC-90C7-A7B5DFCCCA45Q30444599-5FB4D37A-0C4F-478B-A07D-CAA2905D26D1Q30924970-3AF68C44-3DA5-4411-8D32-FD3AA2F09EB0Q31668433-735C2C8C-1F4A-4392-877C-33538C150B7DQ32041819-C32A8B14-670C-4044-B709-23CB6E32E446Q32058445-6ACA248F-BA06-4D10-9E3C-913D800B286AQ33715498-9DB508BF-96E2-4CDB-98AA-F598824D35C2Q33886113-CA61C885-CEDE-4906-97E3-A19D72CA9D90Q33901782-A980BA39-063D-4BD7-B302-29A8607F2A5DQ33944040-71F1A3B2-A382-4789-AFFF-AF1D150A098CQ34148225-1BF259CE-2870-44BC-ACBA-CF4F247C510DQ34270230-925DBE2F-B88B-4C60-B160-C2DC1CD813C2Q34396154-606C20E5-D2C8-4249-A886-C1BDB22F5DC1Q34672405-8A219940-F457-4ABB-82AF-7E632F843ABFQ35109711-23A4670E-045B-4991-9DF4-D045770FC4F6Q35169907-CF641222-9D0D-48AF-9053-94E628BF2720Q36017046-D217D7EE-FC92-4279-B849-E9E3017FDC8AQ36234135-22579E69-1487-4984-8E21-D36772764171Q36234444-53517484-C51C-45A9-9E8C-A4AA2D4A4319Q36235231-6ADC8CE1-6588-4B60-B360-3C9C8AA8379DQ36236769-1E3C56E8-139C-4983-A972-5AAB7A863349Q36236911-683CDE67-03B0-43DF-98F8-61B38E5872DCQ36237485-931FBC18-F3D2-4CF5-A6A4-43AF10E1DD58Q36254744-D988886D-DDB1-4E6F-B96F-C7175A9ED12AQ36255497-22610498-E862-40A6-8A69-E3C6A0F61546Q36256212-0C0BFDED-C3B8-4E91-8B14-B85B5A112F4FQ36320967-5C8F09DF-2799-4BCC-BD9E-F1330EC2F313Q36328593-663FA480-16F4-49E5-B41F-6CF14E6597A6Q36530065-45AA588F-CAC0-4436-9C86-BCCFD03C63D5Q36862472-87FD2699-856B-4526-8963-D9EE7F6244B5Q36888712-DA86AB34-92D9-4E33-B251-BD1537054CE2Q36972087-C9129BA8-6628-42FB-B2B5-205D65D8AC50Q37003924-5618F1B8-C912-4636-86BF-6B126501804DQ37123217-4D0C950A-DE54-48B6-B5CC-E1848760E8F4Q37497050-E6517157-5126-4A8D-A6D2-E62290AB1F5FQ37620955-62C178A2-BF63-4D8D-A20A-74402EF9D41B
P2860
Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Mutational and secondary struc ...... meric immunoglobulin receptor.
@ast
Mutational and secondary struc ...... meric immunoglobulin receptor.
@en
type
label
Mutational and secondary struc ...... meric immunoglobulin receptor.
@ast
Mutational and secondary struc ...... meric immunoglobulin receptor.
@en
prefLabel
Mutational and secondary struc ...... meric immunoglobulin receptor.
@ast
Mutational and secondary struc ...... meric immunoglobulin receptor.
@en
P2093
P2860
P356
P1476
Mutational and secondary struc ...... meric immunoglobulin receptor.
@en
P2093
P2860
P304
P356
10.1083/JCB.123.5.1149
P407
P50
P577
1993-12-01T00:00:00Z