Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells - Wikidata - wikimedia - TriplyDB

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

http://www.wikidata.org/entity/Q28260778

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Phosphorylation of SNAP-23 by the novel kinase SNAK regulates t-SNARE complex assembly Syntaxins 3 and 4 are concentrated in separate clusters on the plasma membrane before the establishment of cell polarity CFTR chloride channels are regulated by a SNAP-23/syntaxin 1A complex.Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery Syntaxin 3 and SNAP-25 pairing, regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments Cep164 mediates vesicular docking to the mother centriole during early steps of ciliogenesis Protein kinase A acts at the basal body of the primary cilium to prevent Gli2 activation and ventralization of the mouse neural tube SNAP-23 participates in SNARE complex assembly in rat adipose cells D53 is a novel endosomal SNARE-binding protein that enhances interaction of syntaxin 1 with the synaptobrevin 2 complex in vitro The zebrafish foxj1a transcription factor regulates cilia function in response to injury and epithelial stretch Distribution of synaptic vesicle proteins in the mammalian retina identifies obligatory and facultative components of ribbon synapses.The cytoplasmic tail of fibrocystin contains a ciliary targeting sequence Basolateral sorting of syntaxin 4 is dependent on its N-terminal domain and the AP1B clathrin adaptor, and required for the epithelial cell polarity.Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells Tight junction, a platform for trafficking and signaling protein complexes.Membrane traffic in myelinating oligodendrocytes.Soluble levels of cytosolic tubulin regulate ciliary length control Intracellular redirection of plasma membrane trafficking after loss of epithelial cell polarity Drosophila SNAP-29 is an essential SNARE that binds multiple proteins involved in membrane traffic.Vesicle-associated membrane protein-2 (VAMP2) mediates cAMP-stimulated renin release in mouse juxtaglomerular cells.Transcytosis: crossing cellular barriers.The human submandibular gland: immunohistochemical analysis of SNAREs and cytoskeletal proteins.Apical targeting of syntaxin 3 is essential for epithelial cell polarity.SNAP23 is selectively expressed in airway secretory cells and mediates baseline and stimulated mucin secretion.The SNARE machinery is involved in apical plasma membrane trafficking in MDCK cells.Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells.Mast cells possess distinct secretory granule subsets whose exocytosis is regulated by different SNARE isoforms.Hepatocyte polarity Regulation of flagellar length in Chlamydomonas.The ubiquitin conjugation system is involved in the disassembly of cilia and flagella.Primary cilia and dendritic spines: different but similar signaling compartments.VAMP7 modulates ciliary biogenesis in kidney cells.Phosphorylation of SNAP-23 regulates exocytosis from mast cells.SNARE expression and localization in renal epithelial cells suggest mechanism for variability of trafficking phenotypes.SNAP-25 traffics to the plasma membrane by a syntaxin-independent mechanism.The last exon of SNAP-23 regulates granule exocytosis from mast cells.SNARE protein trafficking in polarized MDCK cells.SNAP-23 requirement for transferrin recycling in Streptolysin-O-permeabilized Madin-Darby canine kidney cells.Identification of signaling pathways regulating primary cilium length and flow-mediated adaptation.Alteration of microRNA expressions in the pons and medulla in rats after 3,3'-iminodipropionitrile administration

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P2860

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

http://www.wikidata.org/entity/Q28260778

description

1998 nî lūn-bûn

@nan

1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

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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

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@ast

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@en

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@nl

type

label

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@ast

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@en

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@nl

prefLabel

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@ast

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@en

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@nl

P1433

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P1433

Journal of Biological Chemistry

P1476

Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells

@en

P2093

H A Anderson

http://www.w3.org/2001/XMLSchema#string

K E Mostov

http://www.w3.org/2001/XMLSchema#string

M Zhang

http://www.w3.org/2001/XMLSchema#string

P A Roche

http://www.w3.org/2001/XMLSchema#string

S C van Ijzendoorn

http://www.w3.org/2001/XMLSchema#string

S H Low

http://www.w3.org/2001/XMLSchema#string

P2860

The syntaxin family of vesicular transport receptors

Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues

n-Sec1: a neural-specific syntaxin-binding protein

Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses

rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin

Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis.

A conserved domain is present in different families of vesicular fusion proteins: a new superfamily

Mechanisms of intracellular protein transport

A new syntaxin family member implicated in targeting of intracellular transport vesicles

A novel isoform of syntaxin-binding protein homologous to yeast Sec1 expressed ubiquitously in mammalian cells

P304

3422-3430

http://www.w3.org/2001/XMLSchema#string

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scholarly article

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4795904

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P356

10.1074/JBC.273.6.3422

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P433

6

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P478

273

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P577

1998-02-01T00:00:00Z

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P5875

238316198

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P698

9452464

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