Evidence map›Paper›PMID 11927608›Full record

ArticleThe Journal of cell biology2002

The Maguk protein, Pals1, functions as an adapter, linking mammalian homologues of Crumbs and Discs Lost.

Michael H Roh, Olga Makarova, Chia-Jen Liu, KunYoo Shin, Seonok Lee, Stephanie Laurinec, Meera Goyal, Roger Wiggins, Ben Margolis

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.

0numbers the graph read from it
0cells of the map it votes in
141citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

141 citing papers in PubMed, 349 citations in OpenAlex.

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  17. Structural biology of SARS-CoV-2: open the door for novel therapies.Signal transduction and targeted therapy · 2022
    Review
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81 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

9 authors at 2 institutions in 1 country.

Michael H RohDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Olga Makarova
Chia-Jen Liu
KunYoo Shin
Seonok Lee
Stephanie Laurinec
Meera Goyal
Roger Wiggins
Ben Margolis
University of Michigan–Ann Arbor · USHoward Hughes Medical Institute · US

Funding

MICHIGAN MEDICAL SCIENTIST TRAINING PROGRAMT32GM007863 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI COLLINS, KATHLEEN L. · 1985 to 2024
$38.3M
PUBLIC HEALTH DEMONSTRATIONP60DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 1985 to 2012
$26.5M
Tight Junction Proteins and Epithelial PolarityR01DK058208 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARGOLIS, BENJAMIN L · 2001 to 2009
$2.2M
NIDDK NIH HHS 5-P60-DK20572NIDDK NIH HHS DK58208NIDDK NIH HHS P60 DK020572NIDDK NIH HHS R01 DK058208NIGMS NIH HHS T32 GM007863NIGMS NIH HHS T32 GM07863
6 · The paper itself

Abstract

Membrane-associated guanylate kinase (Maguk) proteins are scaffold proteins that contain PSD-95-Discs Large-zona occludens-1 (PDZ), Src homology 3, and guanylate kinase domains. A subset of Maguk proteins, such as mLin-2 and protein associated with Lin-7 (Pals)1, also contain two L27 domains: an L27C domain that binds mLin-7 and an L27N domain of unknown function. Here, we demonstrate that the L27N domain targets Pals1 to tight junctions by binding to a PDZ domain protein, Pals1-associated tight junction (PATJ) protein, via a unique Maguk recruitment domain. PATJ is a homologue of Drosophila Discs Lost, a protein that is crucial for epithelial polarity and that exists in a complex with the apical polarity determinant, Crumbs. PATJ and a human Crumbs homologue, CRB1, colocalize with Pals1 to tight junctions, and CRB1 interacts with PATJ albeit indirectly via binding the Pals1 PDZ domain. In agreement, we find that a Drosophila homologue of Pals1 participates in identical interactions with Drosophila Crumbs and Discs Lost. This Drosophila Pals1 homologue has been demonstrated recently to represent Stardust, a crucial polarity gene in Drosophila. Thus, our data identifies a new multiprotein complex that appears to be evolutionarily conserved and likely plays an important role in protein targeting and cell polarity.

Indexed as

Membrane Transport ProteinsNerve Tissue ProteinsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCarrier ProteinsCells, CulturedConserved SequenceDrosophilaDrosophila ProteinsEye ProteinsGuanylate KinasesHumansInsect ProteinsKidneyMembrane ProteinsAdaptor Proteins, Signal TransducingCarrier ProteinsCRB1 protein, humancrb protein, Drosophiladlt protein, DrosophilaDrosophila ProteinsEye ProteinsGuanylate KinasesInsect ProteinsLIN7A protein, humanLIN7C protein, humanLIN-7 protein, mammalianMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsNucleoside-Phosphate KinasePATJ protein, humanPatj protein, ratsdt protein, DrosophilaTight Junction ProteinsVesicular Transport Proteins

Identifiers

PMID11927608
PMCPMC2173254
OpenAlexW2133862855

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.