Evidence map›Paper›PMID 25049274›Full record

ArticleThe Journal of cell biology2014

Ankyrin-G palmitoylation and βII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly.

Meng He, Khadar M Abdi, Vann Bennett

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.6field-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

60 citing papers in PubMed, 85 citations in OpenAlex.

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  12. Live imaging of excitable axonal microdomains in ankyrin-G-GFP mice.bioRxiv : the preprint server for biology · 2024
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  19. Ankyrin-B is lipid-modified byFrontiers in physiology · 2023
    Article
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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

3 authors at 2 institutions in 3 countries.

Meng HeDepartment of Pharmacology and Cancer Biology, Department of Cell Biology, Department of Biochemistry, and Department of Neurobiology, Duke University Medical Center, Durham, NC 27710.
Khadar M AbdiDepartment of Pharmacology and Cancer Biology, Department of Cell Biology, Department of Biochemistry, and Department of Neurobiology, Duke University Medical Center, Durham, NC 27710.
Vann BennettDepartment of Pharmacology and Cancer Biology, Department of Cell Biology, Department of Biochemistry, and Department of Neurobiology, Duke University Medical Center, Durham, NC 27710Department of Pharmacology and Cancer Biology, Department of Cell Biology, Department of Biochemistry, and Department of Neurobiology, Duke University Medical Center, Durham, NC 27710 Howard Hughes Medical Institute, Durham, NC 27710 vann.bennett@duke.edu.
Duke University Hospital · USCentre for Cancer Biology · AU

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Ankyrin-G and βII-spectrin colocalize at sites of cell-cell contact in columnar epithelial cells and promote lateral membrane assembly. This study identifies two critical inputs from lipids that together provide a rationale for how ankyrin-G and βII-spectrin selectively localize to Madin-Darby canine kidney (MDCK) cell lateral membranes. We identify aspartate-histidine-histidine-cysteine 5/8 (DHHC5/8) as ankyrin-G palmitoyltransferases required for ankyrin-G lateral membrane localization and for assembly of lateral membranes. We also find that βII-spectrin functions as a coincidence detector that requires recognition of both ankyrin-G and phosphoinositide lipids for its lateral membrane localization. DHHC5/8 and βII-spectrin colocalize with ankyrin-G in micrometer-scale subdomains within the lateral membrane that are likely sites for palmitoylation of ankyrin-G. Loss of either DHHC5/8 or ankyrin-G-βII-spectrin interaction or βII-spectrin-phosphoinositide recognition through its pleckstrin homology domain all result in failure to build the lateral membrane. In summary, we identify a functional network connecting palmitoyltransferases DHHC5/8 with ankyrin-G, ankyrin-G with βII-spectrin, and βII-spectrin with phosphoinositides that is required for the columnar morphology of MDCK epithelial cells.

Indexed as

AnimalsAnkyrinsCell MembraneCell PolarityDogsEpithelial CellsGene Knockdown TechniquesLipoylationMembrane ProteinsModels, BiologicalPhosphatidylinositolsSpectrinAnkyrinsMembrane ProteinsPhosphatidylinositolsSpectrin

Identifiers

PMID25049274
PMCPMC4107783
OpenAlexW2161349075

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.