Evidence map›Paper›PMID 23576432›Full record

ArticleThe Journal of biological chemistry2013

The cation-π box is a specific phosphatidylcholine membrane targeting motif.

Jiongjia Cheng, Rebecca Goldstein, Anne Gershenson, Boguslaw Stec, Mary F Roberts

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

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  5. Duplicate entries in the Protein Data Bank: how to detect and handle them.Acta crystallographica. Section D, Structural biology · 2025
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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

5 authors at 3 institutions in 1 country.

Jiongjia ChengDepartment of Chemistry, Boston College, Chestnut Hill, Massachusetts 02467, USA.
Rebecca Goldstein
Anne Gershenson
Boguslaw Stec
Mary F Roberts
Boston College · USUniversity of Massachusetts Amherst · USSanford Burnham Prebys Medical Discovery Institute · US

Funding

ACTIVATION OF PI-SPECIFIC PHOSPHOLIPASE C ENZYMESR01GM060418 · NIGMS · BOSTON COLLEGE · PI ROBERTS, MARY FEDARKO · 2000 to 2013
$3.1M
NIGMS NIH HHS R01 GM060418NIGMS NIH HHS R01 GM60418
6 · The paper itself

Abstract

Peripheral membrane proteins can be targeted to specific organelles or the plasma membrane by differential recognition of phospholipid headgroups. Although molecular determinants of specificity for several headgroups, including phosphatidylserine and phosphoinositides are well defined, specific recognition of the headgroup of the zwitterionic phosphatidylcholine (PC) is less well understood. In cytosolic proteins the cation-π box provides a suitable receptor for choline recognition and binding through the trimethylammonium moiety. In PC, this moiety might provide a sufficient handle to bind to peripheral proteins via a cation-π cage, where the π systems of two or more aromatic residues are within 4-5 Å of the quaternary amine. We prove this hypothesis by engineering the cation-π box into secreted phosphatidylinositol-specific phospholipase C from Staphylococcus aureus, which lacks specific PC recognition. The N254Y/H258Y variant selectively binds PC-enriched vesicles, and x-ray crystallography reveals N254Y/H258Y binds choline and dibutyroylphosphatidylcholine within the cation-π motif. Such simple PC recognition motifs could be engineered into a wide variety of secondary structures providing a generally applicable method for specific recognition of PC.

Indexed as

Amino Acid MotifsAmino Acid SubstitutionBacterial ProteinsCationsCell MembraneMutation, MissensePhosphatidylcholinesReceptors, Cell SurfaceStaphylococcus aureusBacterial ProteinsCationsPhosphatidylcholinesReceptors, Cell SurfaceMembrane EnzymesNuclear Magnetic ResonancePhosphatidylcholinePhospholipase CX-ray Crystallography

Identifiers

PMID23576432
PMCPMC3663509
OpenAlexW2043363350

What OpenQuestion holds

Textmetadata
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.