Evidence map›Paper›PMID 19129194›Full record

ArticleThe Journal of biological chemistry2009

In Vitro and in Vivo Characterization of Molecular Interactions between Calmodulin, Ezrin/Radixin/Moesin, and L-selectin.

David J Killock, Maddy Parsons, Marouan Zarrouk, Simon M Ameer-Beg, Anne J Ridley, Dorian O Haskard, Marketa Zvelebil, Aleksandar Ivetic

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.0field-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

18 citing papers in PubMed, 47 citations in OpenAlex.

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  9. L-selectin shedding is activated specifically within transmigrating pseudopods of monocytes to regulate cell polarity in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2015
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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

8 authors at 5 institutions in 2 countries.

David J KillockCardiovascular Science Unit, National Heart and Lung Institute, Imperial College London, Hammersmith Campus, London W12 0NN.
Maddy Parsons
Marouan Zarrouk
Simon M Ameer-Beg
Anne J Ridley
Dorian O Haskard
Marketa Zvelebil
Aleksandar Ivetic
Lung Institute · USKing's College London · GBBreast Cancer Now · GBImperial College London · GBLondon Cancer · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

L-selectin is a cell adhesion molecule that tethers leukocytes to the luminal walls of venules during inflammation and enables them to roll under the force of blood flow. Clustering of L-selectin during rolling is thought to promote outside-in signals that lead to integrin activation and chemokine receptor expression, ultimately contributing to leukocyte arrest. Several studies have underscored the importance of the L-selectin cytoplasmic tail in functionally regulating adhesion and signaling. Interestingly, the L-selectin tail comprises only 17 amino acids, and yet it is thought to bind simultaneously to several proteins. For example, constitutive association of calmodulin (CaM) and ezrin/radixin/moesin (ERM) to L-selectin confers resistance to proteolysis and microvillar positioning, respectively. In this report we found that recombinant purified CaM and ERM bound non-competitively to the same tail of L-selectin. Furthermore, molecular modeling supported the possibility that CaM, L-selectin, and moesin could form a heterotrimeric complex. Finally, using fluorescence lifetime imaging microscopy to measure fluorescence resonance energy transfer, it was shown that CaM, L-selectin, and ERM could interact simultaneously in vivo. Moreover, L-selectin clustering promoted CaM/ERM interaction in cis (i.e. derived from neighboring L-selectin tails). These results highlight a novel intracellular event that occurs as a consequence of L-selectin clustering, which could participate in transducing signals that promote the transition from rolling to arrest.

Indexed as

AnimalsCalmodulinChlorocebus aethiopsCOS CellsCytoskeletal ProteinsEzrinHumansLeukocyte RollingL-SelectinMembrane ProteinsMicrofilament ProteinsMultiprotein ComplexesProtein BindingRecombinant ProteinsSignal TransductionU937 CellsCalmodulinCytoskeletal ProteinsEzrinL-SelectinMembrane ProteinsMicrofilament ProteinsmoesinMultiprotein ComplexesradixinRecombinant Proteins

Identifiers

PMID19129194
PMCPMC2659241
OpenAlexW2155055442

What OpenQuestion holds

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LicenceCC BY-NC
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.