Evidence map›Paper›PMID 21737843›Full record

ArticleThe Journal of biological chemistry2011

Oligomeric interactions of sarcolipin and the Ca-ATPase.

Joseph M Autry, John E Rubin, Sean D Pietrini, Deborah L Winters, Seth L Robia, David D Thomas

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
2.1field-weighted citation impact, top 11% 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, 49 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

6 authors at 2 institutions in 1 country.

Joseph M AutryDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA.
John E Rubin
Sean D Pietrini
Deborah L Winters
Seth L Robia
David D Thomas
University of Minnesota · USLoyola University Chicago · US

Funding

Structural Determinants of Calcium Pump RegulationR01HL092321 · NHLBI · LOYOLA UNIVERSITY CHICAGO · PI Seth L Robia · 2008 to 2026
$8.9M
Structural Dynamics of Muscle Calcium ATPase RegulationR01GM027906 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1985 to 2016
$8.6M
NHLBI NIH HHS R01 HL092321NIGMS NIH HHS GM27906NIGMS NIH HHS R01 GM027906
6 · The paper itself

Abstract

We have detected directly the interactions of sarcolipin (SLN) and the sarcoplasmic reticulum Ca-ATPase (SERCA) by measuring fluorescence resonance energy transfer (FRET) between fusion proteins labeled with cyan fluorescent protein (donor) and yellow fluorescent protein (acceptor). SLN is a membrane protein that helps control contractility by regulating SERCA activity in fast-twitch and atrial muscle. Here we used FRET microscopy and spectroscopy with baculovirus expression in insect cells to provide direct evidence for: 1) oligomerization of SLN and 2) regulatory complex formation between SLN and the fast-twitch muscle Ca-ATPase (SERCA1a isoform). FRET experiments demonstrated that SLN monomers self-associate into dimers and higher order oligomers in the absence of SERCA, and that SLN monomers also bind to SERCA monomers in a 1:1 binary complex when the two proteins are coexpressed. FRET experiments further demonstrated that the binding affinity of SLN for itself is similar to that for SERCA. Mutating SLN residue isoleucine-17 to alanine (I17A) decreased the binding affinity of SLN self-association and converted higher order oligomers into monomers and dimers. The I17A mutation also decreased SLN binding affinity for SERCA but maintained 1:1 stoichiometry in the regulatory complex. Thus, isoleucine-17 plays dual roles in determining the distribution of SLN homo-oligomers and stabilizing the formation of SERCA-SLN heterodimers. FRET results for SLN self-association were supported by the effects of SLN expression in bacterial cells. We propose that SLN exists as multiple molecular species in muscle, including SERCA-free (monomer, dimer, oligomer) and SERCA-bound (heterodimer), with transmembrane zipper residues of SLN serving to stabilize oligomeric interactions.

Indexed as

Protein MultimerizationAnimalsBacterial ProteinsBaculoviridaeCloning, MolecularDogsFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHeart AtriaInsectaLuminescent ProteinsMuscle Fibers, Fast-TwitchMuscle ProteinsMutagenesis, Site-DirectedProtein BindingProteolipidsBacterial ProteinsCyan Fluorescent ProteinGreen Fluorescent ProteinsLuminescent ProteinsMuscle ProteinsProteolipidssarcolipinSarcoplasmic Reticulum Calcium-Transporting ATPasesyellow fluorescent protein, Bacteria

Identifiers

PMID21737843
PMCPMC3173058
OpenAlexW2103522217

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.