Evidence map›Paper›PMID 9362511›Full record

ArticleThe Journal of cell biology1997

The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells.

C Yeaman, A H Le Gall, A N Baldwin, L Monlauzeur, A Le Bivic, E Rodriguez-Boulan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

99 citing papers in PubMed, 279 citations in OpenAlex.

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  13. Spatial control of membrane traffic in neuronal dendrites.Molecular and cellular neurosciences · 2020
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  20. Article

39 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 2 countries.

C YeamanDyson Vision Research Institute, Department of Ophthalmology, and Department of Cell Biology, Cornell University Medical College, New York 10021, USA.
A H Le Gall
A N Baldwin
L Monlauzeur
A Le Bivic
E Rodriguez-Boulan
Cornell University · USInstitut de Biologie du Développement Marseille · FRStanford University · US

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 GM 34107NIGMS NIH HHS GM 41771NIGMS NIH HHS R01 GM034107
6 · The paper itself

Abstract

Delivery of newly synthesized membrane-spanning proteins to the apical plasma membrane domain of polarized MDCK epithelial cells is dependent on yet unidentified sorting signals present in the luminal domains of these proteins. In this report we show that structural information for apical sorting of transmembrane neurotrophin receptors (p75(NTR)) is localized to a juxtamembrane region of the extracellular domain that is rich in O-glycosylated serine/threonine residues. An internal deletion of 50 amino acids that removes this stalk domain from p75(NTR) causes the protein to be sorted exclusively of the basolateral plasma membrane. Basolateral sorting stalk-minus p75(NTR) does not occur by default, but requires sequences present in the cytoplasmic domain. The stalk domain is also required for apical secretion of a soluble form of p75(NTR), providing the first demonstration that the same domain can mediate apical sorting of both a membrane-anchored as well as secreted protein. However, the single N-glycan present on p75(NTR) is not required for apical sorting of either transmembrane or secreted forms.

Indexed as

AnimalsAsparagineCell LineCell PolarityCytoplasmDogsGlycosylationHumansPolysaccharidesReceptor, Nerve Growth FactorReceptors, Nerve Growth FactorRecombinant ProteinsSerineSolubilityStructure-Activity RelationshipThreonineAsparaginePolysaccharidesReceptor, Nerve Growth FactorReceptors, Nerve Growth FactorRecombinant ProteinsSerineThreonine

Identifiers

PMID9362511
PMCPMC2139957
OpenAlexW2030662833

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.