The role of N-glycosylation in transport to the plasma membrane and sorting of the neuronal glycine transporter GLYT2. (Q31468942)

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1 November 2019

title

The role of N-glycosylation in transport to the plasma membrane and sorting of the neuronal glycine transporter GLYT2 (English)

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5

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Francisco Zafra

6

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author name string

Martínez-Maza R

1

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Poyatos I

2

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López-Corcuera B

3

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N úñez E

4

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Aragón C

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language of work or name

English

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publication date

17 October 2000

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Journal of Biological Chemistry

1 November 2019

published in

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volume

276

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issue

3

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page(s)

2168-2173

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Role of transmitter uptake mechanisms in synaptic neurotransmission

1 November 2019

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Cloning and expression of a glycine transporter reveal colocalization with NMDA receptors

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Characterization of the 5' region of the rat brain glycine transporter GLYT2 gene: identification of a novel isoform

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Cellular expression of glycine transporter 2 messenger RNA exclusively in rat hindbrain and spinal cord

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Regional distribution and developmental variation of the glycine transporters GLYT1 and GLYT2 in the rat CNS.

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Two glycine transporter variants with distinct localization in the CNS and peripheral tissues are encoded by a common gene

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Modulation of N-methyl-D-aspartate receptor function by glycine transport

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Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture

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Protein and lipid sorting from thetrans–Golgi network to the plasma membrane in polarized cells

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The role of N-glycosylation in the targeting and activity of the GLYT1 glycine transporter

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Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface

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The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells

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Why mammalian cell surface proteins are glycoproteins

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Polarized distribution of glycine transporter isoforms in epithelial and neuronal cells

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Glycans in post-Golgi apical targeting: sorting signals or structural props?

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N-glycans as apical sorting signals in epithelial cells

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Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain

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Multiple Sorting Signals Determine Apical Localization of a Nonglycosylated Integral Membrane Protein

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Identification of Sorting Determinants in the C-terminal Cytoplasmic Tails of the γ-Aminobutyric Acid Transporters GAT-2 and GAT-3

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Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes.

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VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles

21 January 2018

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Apical sorting of bovine enteropeptidase does not involve detergent-resistant association with sphingolipid-cholesterol rafts.

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Identifiers

DOI

10.1074/JBC.M006774200

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11036075 AND SRC:MED&resulttype=core&format=json

1 November 2019

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