Evidence map›Paper›PMID 8922391›Full record

ArticleThe Journal of cell biology1996

Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain.

R A Lue, E Brandin, E P Chan, D Branton

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 119 citations in OpenAlex.

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  12. Polarity protein complex Scribble/Lgl/Dlg and epithelial cell barriers.Advances in experimental medicine and biology · 2012
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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

4 authors at 1 institution in 1 country.

R A LueDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
E Brandin
E P Chan
D Branton
Harvard University · US

Funding

GENETIC STUDIES OF NON-ERYTHROID SPECTRINR01GM039686 · NIGMS · HARVARD UNIVERSITY · PI BRANTON, DANIEL · 1988 to 1996
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NIGMS NIH HHS GM39686
6 · The paper itself

Abstract

hDlg, a human homologue of the Drosophila Dig tumor suppressor, contains two binding sites for protein 4.1, one within a domain containing three PSD-95/Dlg/ZO-1 (PDZ) repeats and another within the alternatively spliced I3 domain. Here, we further define the PDZ-protein 4.1 interaction in vitro and show the functional role of both 4.1 binding sites in situ. A single protease-resistant structure formed by the entirety of both PDZ repeats 1 and 2 (PDZ1-2) contains the protein 4.1-binding site. Both this PDZ1-2 site and the I3 domain associate with a 30-kD NH2-terminal domain of protein 4.1 that is conserved in ezrin/radixin/moesin (ERM) proteins. We show that both protein 4.1 and the ezrin ERM protein interact with the murine form of hDlg in a coprecipitating immune complex. In permeabilized cells and tissues, either the PDZ1-2 domain or the I3 domain alone are sufficient for proper subcellular targeting of exogenous hDlg. In situ, PDZ1-2-mediated targeting involves interactions with both 4.1/ERM proteins and proteins containing the COOH-terminal T/SXV motif. I3-mediated targeting depends exclusively on interactions with 4.1/ERM proteins. Our data elucidates the multivalent nature of membrane-associated guanylate kinase homologue (MAGUK) targeting, thus beginning to define those protein interactions that are critical in MAGUK function.

Indexed as

Cytoskeletal ProteinsDrosophila ProteinsNeuropeptidesTumor Suppressor ProteinsAlternative SplicingAnimalsCytoskeletonErythrocyte MembraneEzrinGenes, Tumor SuppressorHumansInsect HormonesMembrane ProteinsMolecular Sequence DataPhosphoproteinsProtein BindingCytoskeletal Proteinsdlg1 protein, DrosophilaDrosophila Proteinserythrocyte membrane band 4.1 proteinerythrocyte membrane protein band 4.1-like 1EzrinInsect HormonesMembrane ProteinsNeuropeptidesPhosphoproteinsProtein Sorting SignalsSerineThreonineTumor Suppressor ProteinsValine

Identifiers

PMID8922391
PMCPMC2133382
OpenAlexW2152331062

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.