About: N-linked glycosylation and its impact on the electrophoretic mobility and function of the human Proton-Coupled Folate Transporter (HsPCFT)

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About: N-linked glycosylation and its impact on the electrophoretic mobility and function of the human Proton-Coupled Folate Transporter (HsPCFT) Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	N-linked glycosylation and its impact on the electrophoretic mobility and function of the human Proton-Coupled Folate Transporter (HsPCFT)
Creator	Qiu, Andong Selcuk Unal, Ersin Zhao, Rongbao David Goldman, I
source	Elsevier; Medline; PMC
abstract	The human proton-coupled folate transporter (HsPCFT, SLC46A1) mediates intestinal absorption of folates and transport of folates into the liver, brain and other tissues. On Western blot, HsPCFT migrates as a broad band (∼55 kDa), higher than predicted (∼50 kDa) in cell lines. Western blot analysis required that membrane preparations not be incubated in the loading buffer above 50°C to avoid aggregation of the protein. Treatment of membrane fractions from HsPCFT-transfected HeLa cells with peptidyl N-glycanase F, or cells with tunicamycin, resulted in conversion to a ∼35 kDa species. Substitution of asparagine residues of two canonical glycosylation sites to glutamine, individually, yielded a ∼ 47 kDa protein; substitution of both sites gave a smaller (∼35 kDa) protein. Single mutants retained full transport activity; the double mutant retained a majority of activity. Transport function and molecular size were unchanged when the double-mutant was hemagglutinin (HA) tagged at either the NH(2) or COOH terminus and probed with an anti-HA antibody excluding degradation of the deglycosylated protein. Wild-type or deglycosylated HsPCFT HA, tagged at amino or carboxyl termini, could only be visualized on the plasma membrane when HeLa cells were first permeabilized, consistent with the intracellular location of these domains.
has issue date	2008-06-01(xsd:dateTime)
bibo:doi	10.1016/j.bbamem.2008.03.009
bibo:pmid	18405659
has license	green-oa
sha1sum (hex)	33c1ed44e10f518a08b5bfcaa1b75e031daaf6c6
schema:url	https://doi.org/10.1016/j.bbamem.2008.03.009
resource representing a document's title	N-linked glycosylation and its impact on the electrophoretic mobility and function of the human Proton-Coupled Folate Transporter (HsPCFT)
has PubMed Central identifier	PMC2762823
has PubMed identifier	18405659
schema:publication	Biochimica et Biophysica Acta (BBA) - Biomembranes
resource representing a document's body	covid:33c1ed44e10f518a08b5bfcaa1b75e031daaf6c6#body_text
is schema:about of	named entity 'protein' named entity 'cell lines' named entity 'loading' named entity 'WESTERN BLOT ANALYSIS' named entity 'LOADING BUFFER' »more»

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