Evidence map›Paper›PMID 26067675›Full record

ArticlePLoS computational biology2015

The Physiological Molecular Shape of Spectrin: A Compact Supercoil Resembling a Chinese Finger Trap.

Jeffrey W Brown, Esther Bullitt, Sira Sriswasdi, Sandra Harper, David W Speicher, C James McKnight

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 43 citations in OpenAlex.

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  15. Structural and Functional Refinement of the Axon Initial Segment in Avian Cochlear Nucleus during Development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
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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

6 authors at 3 institutions in 1 country.

Jeffrey W BrownDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts, United States of America; Internal Medicine Residency Program, University of Pittsburgh Medical Center, UPMC Montefiore Hospital, Pittsburgh, Pennsylvania, United States of America.
Esther BullittDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts, United States of America.
Sira SriswasdiCenter for Systems and Computational Biology, and Molecular and Cellular Oncogenesis Program, the Wistar Institute, Philadelphia, Pennsylvania, United States of America; Genomics and Computational Biology Graduate Group, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.
Sandra HarperCenter for Systems and Computational Biology, and Molecular and Cellular Oncogenesis Program, the Wistar Institute, Philadelphia, Pennsylvania, United States of America.
David W SpeicherCenter for Systems and Computational Biology, and Molecular and Cellular Oncogenesis Program, the Wistar Institute, Philadelphia, Pennsylvania, United States of America; Genomics and Computational Biology Graduate Group, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.
C James McKnightDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts, United States of America.
The Wistar Institute · USBoston University · USUniversity of Pittsburgh Medical Center · US

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
Membrane Proteins of Normal and Abnormal Red CellsR01HL038794 · NHLBI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1987 to 2013
$5.1M
STRUCTURE/FUNCTION OF BACTERIAL ADHESION PILIR01GM055722 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI BULLITT, ESTHER · 1998 to 2009
$2.1M
Localizing and Modeling Headpiece Domains on F-ActinR01GM062886 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI MCKNIGHT, CHRISTOPHER JAMES · 2002 to 2006
$1.2M
Improved data collection for FEI TF20 and Philips CM12 electron microscopesS10RR025434 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI BULLITT, ESTHER · 2009 to 2009
$263k
NCI NIH HHS CA010815NCI NIH HHS P30 CA010815NCRR NIH HHS S10 RR025434NCRR NIH HHS S10RR25434NHLBI NIH HHS R01 HL038794NHLBI NIH HHS R01HL038794NIGMS NIH HHS R01 GM055722NIGMS NIH HHS R01GM055722NIGMS NIH HHS R01 GM062886NIGMS NIH HHS R01GM62886
6 · The paper itself

Abstract

The primary, secondary, and tertiary structures of spectrin are reasonably well defined, but the structural basis for the known dramatic molecular shape change, whereby the molecular length can increase three-fold, is not understood. In this study, we combine previously reported biochemical and high-resolution crystallographic data with structural mass spectroscopy and electron microscopic data to derive a detailed, experimentally-supported quaternary structure of the spectrin heterotetramer. In addition to explaining spectrin's physiological resting length of ~55-65 nm, our model provides a mechanism by which spectrin is able to undergo a seamless three-fold extension while remaining a linear filament, an experimentally observed property. According to the proposed model, spectrin's quaternary structure and mechanism of extension is similar to a Chinese Finger Trap: at shorter molecular lengths spectrin is a hollow cylinder that extends by increasing the pitch of each spectrin repeat, which decreases the internal diameter. We validated our model with electron microscopy, which demonstrated that, as predicted, spectrin is hollow at its biological resting length of ~55-65 nm. The model is further supported by zero-length chemical crosslink data indicative of an approximately 90 degree bend between adjacent spectrin repeats. The domain-domain interactions in our model are entirely consistent with those present in the prototypical linear antiparallel heterotetramer as well as recently reported inter-strand chemical crosslinks. The model is consistent with all known physical properties of spectrin, and upon full extension our Chinese Finger Trap Model reduces to the ~180-200 nm molecular model currently in common use.

Indexed as

Crystallography, X-RayHumansModels, MolecularProtein ConformationSpectrinSpectrin

Identifiers

PMID26067675
PMCPMC4466138
OpenAlexW567403462

What OpenQuestion holds

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LicenceCC BY
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.