Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes. - Wikidata - wikimedia - TriplyDB

Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes.

Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes.

http://www.wikidata.org/entity/Q33818978

about

AP-4, a novel protein complex related to clathrin adaptors Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface Rab11 is required for trans-golgi network-to-plasma membrane transport and a preferential target for GDP dissociation inhibitor Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment Rab11 regulates recycling through the pericentriolar recycling endosome The structural features of concanavalin A governing non-proline peptide isomerization MT1-MMP proinvasive activity is regulated by a novel Rab8-dependent exocytic pathway.The function of the intermediate compartment in pre-Golgi trafficking involves its stable connection with the centrosome Recognition of sorting signals by clathrin adaptors.Carbohydrate-mediated Golgi to cell surface transport and apical targeting of membrane proteins.Interactions between the exocytic and endocytic pathways in polarized Madin-Darby canine kidney cells.Role of the endocytic machinery in the sorting of lysosome-associated membrane proteins The subapical compartment and its role in intracellular trafficking and cell polarity.Basolateral sorting of furin in MDCK cells requires a phenylalanine-isoleucine motif together with an acidic amino acid cluster.ARF1.GTP, tyrosine-based signals, and phosphatidylinositol 4,5-bisphosphate constitute a minimal machinery to recruit the AP-1 clathrin adaptor to membranes.Trans-Golgi network sorting.An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting.The tyrosine-based lysosomal targeting signal in lamp-1 mediates sorting into Golgi-derived clathrin-coated vesicles.Differential involvement of endocytic compartments in the biosynthetic traffic of apical proteins.Antibody to AP1B adaptor blocks biosynthetic and recycling routes of basolateral proteins at recycling endosomes.Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells.Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells In polarized MDCK cells basolateral vesicles arise from clathrin-gamma-adaptin-coated domains on endosomal tubules ARF6 targets recycling vesicles to the plasma membrane: insights from an ultrastructural investigation Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells.Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon.Compromised cytoarchitecture and polarized trafficking in autosomal dominant polycystic kidney disease cells.Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway Polarized biosynthetic traffic in renal epithelial cells: sorting, sorting, everywhere.How many ways through the Golgi maze?Morphogenesis of post-Golgi transport carriers Taking the scenic route: biosynthetic traffic to the plasma membrane in polarized epithelial cells In vitro formation of recycling vesicles from endosomes requires adaptor protein-1/clathrin and is regulated by rab4 and the connector rabaptin-5.Clathrin and AP1B: key roles in basolateral trafficking through trans-endosomal routes Emerging roles of recycling endosomes.An intact dilysine-like motif in the carboxyl terminus of MAL is required for normal apical transport of the influenza virus hemagglutinin cargo protein in epithelial Madin-Darby canine kidney cells.Multiple biosynthetic trafficking routes for apically secreted proteins in MDCK cells.

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P2860

Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes.

http://www.wikidata.org/entity/Q33818978

description

1995 nî lūn-bûn

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1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի հոտեմբերին հրատարակված գիտական հոդված

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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name

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PNAS.92.22.10109

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Proceedings of the National Academy of Sciences of the United States of America

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P2093

Hille-Rehfeld A

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Leitinger B

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Spiess M

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P2860

A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains

Lysosomal targeting of Limp II membrane glycoprotein requires a novel Leu-Ile motif at a particular position in its cytoplasmic tail

The residues Leu(Ile)475-Ile(Leu, Val, Ala)476, contained in the extended carboxyl cytoplasmic tail, are critical for targeting of the resident lysosomal membrane protein LIMP II to lysosomes

The biogenesis of lysosomes

Signal-dependent membrane protein trafficking in the endocytic pathway

Endocytosis and recycling of subunit H1 of the asialoglycoprotein receptor is independent of oligomerization with H2.

The two subunits of the human asialoglycoprotein receptor have different fates when expressed alone in fibroblasts.

Membranes of sorting organelles display lateral heterogeneity in receptor distribution.

Membrane and secretory proteins are transported from the Golgi complex to the sinusoidal plasmalemma of hepatocytes by distinct vesicular carriers

Sorting signals in the MHC class II invariant chain cytoplasmic tail and transmembrane region determine trafficking to an endocytic processing compartment.

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10109-10113

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10.1073/PNAS.92.22.10109

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22

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92

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7479735

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40745

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