Evidence map›Paper›PMID 27166806›Full record

ArticleBiophysical journal2016

Determinants of Curvature-Sensing Behavior for MARCKS-Fragment Peptides.

Armando J de Jesus, Ormacinda R White, Aaron D Flynn, Hang Yin

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Armando J de JesusDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado; BioFrontiers Institute, University of Colorado, Boulder, Colorado.
Ormacinda R WhiteDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado; BioFrontiers Institute, University of Colorado, Boulder, Colorado.
Aaron D FlynnDepartment of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, Colorado; BioFrontiers Institute, University of Colorado, Boulder, Colorado.
Hang YinDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado; BioFrontiers Institute, University of Colorado, Boulder, Colorado. Electronic address: hubert.yin@colorado.edu.
University of Colorado Boulder · US

Funding

TRAINING IN SIGNAL TRANSDUCTION &CELL CYCLE REGULATIONT32GM008759 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI AHN, NATALIE G. · 2000 to 2020
$5.9M
Predoctoral Training Program in Signaling and Cellular Regulation INCLUDE Down Syndrome SupplementT32GM142607 · NIGMS · UNIVERSITY OF COLORADO · PI Sabrina Leigh Spencer, Tin Tin Su · 2021 to 2026
$3.6M
Dissecting Cell Signaling Mediated by Protein-Protein Interactions in MembranesR01GM103843 · NIGMS · UNIVERSITY OF COLORADO · PI YIN, HANG HUBERT · 2013 to 2016
$1.3M
NIGMS NIH HHS R01 GM103843NIGMS NIH HHS T32 GM008759NIGMS NIH HHS T32 GM142607
6 · The paper itself

Abstract

It is increasingly recognized that membrane curvature plays an important role in various cellular activities such as signaling and trafficking, as well as key issues involving health and disease development. Thus, curvature-sensing peptides are essential to the study and detection of highly curved bilayer structures. The effector domain of myristoylated alanine-rich C-kinase substrate (MARCKS-ED) has been demonstrated to have curvature-sensing ability. Research of the MARCKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers. MARCKS-ED has the added property of being a lower-molecular-weight curvature sensor, which offers advantages in production. With that in mind, this work investigates peptide-sequence-related factors that influence curvature sensing and explores whether peptide fragments of even shorter length can function as curvature sensors. Using both experimental and computational methods, we studied the curvature-sensing capabilities of seven fragments of MARCKS-ED. Two of the longer fragments were designed from approximately the two halves of the full-length peptide whereas the five shorter fragments were taken from the central stretch of MARCKS-ED. Fully atomistic molecular dynamics simulations show that the fragments that remain bound to the bilayer exhibit interactions with the bilayer similar to that of the full-length MARCKS-ED peptide. Fluorescence enhancement and anisotropy assays, meanwhile, reveal that five of the MARCKS fragments possess the ability to sense membrane curvature. Based on the sequences of the curvature-sensing fragments, it appears that the ability to sense curvature involves a balance between the numbers of positively charged residues and hydrophobic anchoring residues. Together, these findings help crystallize our understanding of the molecular mechanisms underpinning the curvature-sensing behaviors of peptides, which will prove useful in the design of future curvature sensors.

Indexed as

Amino Acid SequenceIntracellular Signaling Peptides and ProteinsLipid BilayersLysineMembrane ProteinsMolecular Dynamics SimulationMyristoylated Alanine-Rich C Kinase SubstratePeptide FragmentsProtein ConformationIntracellular Signaling Peptides and ProteinsLipid BilayersLysineMembrane ProteinsMyristoylated Alanine-Rich C Kinase SubstratePeptide Fragments

Identifiers

PMID27166806
PMCPMC4939528
OpenAlexW2352886595

What OpenQuestion holds

Textmetadata
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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.