Evidence map›Paper›PMID 9456321›Full record

ArticleThe Journal of cell biology1998

Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells.

C Lipardi, R Mora, V Colomer, S Paladino, L Nitsch, E Rodriguez-Boulan, C Zurzolo

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.8field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 138 citations in OpenAlex.

  1. Glycosphingolipid and Glycosylphosphatidylinositol Affect Each Other in and on the Cell.Chembiochem : a European journal of chemical biology · 2023
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  14. The effect of membrane domains on the G protein-phospholipase Cbeta signaling pathway.Critical reviews in biochemistry and molecular biology · 2010
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

C LipardiCentro di Endocrinologia ed Oncologia Sperimentale del Consiglio Nazionale delle Ricerche, Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università degli Studi di Napoli Federico II, 80131 Napoli, Italy.
R Mora
V Colomer
S Paladino
L Nitsch
E Rodriguez-Boulan
C Zurzolo
Cornell University · USUniversity of Naples Federico II · IT

Funding

SORTING OF PLASMA MEMBRANE PROTEINS IN EPITHELIAL CELLSR01GM034107 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI RODRIGUEZ-BOULAN, ENRIQUE J · 1985 to 2019
$9.6M
TARGETING AND MEMBRANE DOMAINS IN EPITHELIAL CELLSR01GM041771 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI RODRIGUEZ-BOULAN, ENRIQUE J · 1990 to 1998
–
NIGMS NIH HHS GM41771NIGMS NIH HHS R01 GM034107
6 · The paper itself

Abstract

Most epithelial cells sort glycosylphosphatidylinositol (GPI)-anchored proteins to the apical surface. The "raft" hypothesis, based on data mainly obtained in the prototype cell line MDCK, postulates that apical sorting depends on the incorporation of apical proteins into cholesterol/glycosphingolipid (GSL) rafts, rich in the cholesterol binding protein caveolin/VIP21, in the Golgi apparatus. Fischer rat thyroid (FRT) cells constitute an ideal model to test this hypothesis, since they missort both endogenous and transfected GPI-anchored proteins to the basolateral plasma membrane and fail to incorporate them into cholesterol/glycosphingolipid clusters. Because FRT cells lack caveolin, a major component of the caveolar coat that has been proposed to have a role in apical sorting of GPI-anchored proteins (Zurzolo, C., W. Van't Hoff, G. van Meer, and E. Rodriguez-Boulan. 1994. EMBO [Eur. Mol. Biol. Organ.] J. 13:42-53.), we carried out experiments to determine whether the lack of caveolin accounted for the sorting/clustering defect of GPI-anchored proteins. We report here that FRT cells lack morphological caveolae, but, upon stable transfection of the caveolin1 gene (cav1), form typical flask-shaped caveolae. However, cav1 expression did not redistribute GPI-anchored proteins to the apical surface, nor promote their inclusion into cholesterol/GSL rafts. Our results demonstrate that the absence of caveolin1 and morphologically identifiable caveolae cannot explain the inability of FRT cells to sort GPI-anchored proteins to the apical domain. Thus, FRT cells may lack additional factors required for apical sorting or for the clustering with GSLs of GPI-anchored proteins, or express factors that inhibit these events. Alternatively, cav1 and caveolae may not be directly involved in these processes.

Indexed as

CaveolinsAnimalsCaveolin 1CD55 AntigensCell LineCell MembraneCell PolarityCholesterolEpithelial CellsGlycosphingolipidsGlycosylphosphatidylinositolsGolgi ApparatusMembrane ProteinsMicroscopy, ElectronMicroscopy, ImmunoelectronProteinsCav1 protein, ratCaveolin 1CaveolinsCD55 AntigensCholesterolglycoprotein D, Human herpesvirus 1GlycosphingolipidsGlycosylphosphatidylinositolsMembrane ProteinsProteinsRecombinant Fusion ProteinsViral Envelope Proteins

Identifiers

PMID9456321
PMCPMC2140173
OpenAlexW2060593058

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.