Evidence map›Paper›PMID 34524408›Full record

ArticleThe Biochemical journal2021

Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane.

Daniel Wirth, Ece Özdemir, Christopher King, Lena Ahlswede, Dirk Schneider, Kalina Hristova

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 53% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Review
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 2 institutions in 2 countries.

Daniel WirthDepartment of Materials Science and Engineering and the Institute for NanoBioTechnology, Johns Hopkins University, 3400 Charles Street, Baltimore, MD 21218, U.S.A.
Ece ÖzdemirDepartment of Materials Science and Engineering and the Institute for NanoBioTechnology, Johns Hopkins University, 3400 Charles Street, Baltimore, MD 21218, U.S.A.
Christopher KingDepartment of Materials Science and Engineering and the Institute for NanoBioTechnology, Johns Hopkins University, 3400 Charles Street, Baltimore, MD 21218, U.S.A.
Lena AhlswedeDepartment of Chemistry and Biochemistry, Johannes Gutenberg University, Mainz 55128, Germany.
Dirk SchneiderDepartment of Chemistry and Biochemistry, Johannes Gutenberg University, Mainz 55128, Germany.
Kalina HristovaDepartment of Materials Science and Engineering and the Institute for NanoBioTechnology, Johns Hopkins University, 3400 Charles Street, Baltimore, MD 21218, U.S.A.ORCID 0000-0003-4274-4406
Johns Hopkins University · USJohannes Gutenberg University Mainz · DE

Funding

Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
NIGMS NIH HHS R01 GM068619
6 · The paper itself

Abstract

The spatial distribution of proteins in cell membranes is crucial for signal transduction, cell communication and membrane trafficking. Members of the Tetraspanin family organize functional protein clusters within the plasma membrane into so-called Tetraspanin-enriched microdomains (TEMs). Direct interactions between Tetraspanins are believed to be important for this organization. However, studies thus far have utilized mainly co-immunoprecipitation methods that cannot distinguish between direct and indirect, through common partners, interactions. Here we study Tetraspanin 8 homointeractions in living cells via quantitative fluorescence microscopy. We demonstrate that Tetraspanin 8 exists in a monomer-dimer equilibrium in the plasma membrane. Tetraspanin 8 dimerization is described by a high dissociation constant (Kd = 14 700 ± 1100 Tspan8/µm2), one of the highest dissociation constants measured for membrane proteins in live cells. We propose that this high dissociation constant, and thus the short lifetime of the Tetraspanin 8 dimer, is critical for Tetraspanin 8 functioning as a master regulator of cell signaling.

Indexed as

Fluorescence Resonance Energy TransferHEK293 CellsHumansLipoylationMembrane MicrodomainsMicroscopy, FluorescenceProtein MultimerizationSignal TransductionTetraspaninsThermodynamicsTransfectionTetraspaninsTSPAN8 protein, humanmembrane proteinsprotein-protein interactionstetraspanins

Identifiers

PMID34524408
PMCPMC9171924
OpenAlexW3198934560

What OpenQuestion holds

Textmetadata
LicenceTDM
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.