↓ Skip to main content

Regions of ryanodine receptors that influence activation by the dihydropyridine receptor β1a subunit

Overview of attention for article published in Skeletal Muscle, July 2015
Altmetric Badge

About this Attention Score

  • Good Attention Score compared to outputs of the same age (67th percentile)
  • Average Attention Score compared to outputs of the same age and source

Mentioned by

twitter
5 tweeters

Citations

dimensions_citation
6 Dimensions

Readers on

mendeley
12 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Regions of ryanodine receptors that influence activation by the dihydropyridine receptor β1a subunit
Published in
Skeletal Muscle, July 2015
DOI 10.1186/s13395-015-0049-3
Pubmed ID
Authors

Robyn T. Rebbeck, Hermia Willemse, Linda Groom, Marco G. Casarotto, Philip G. Board, Nicole A. Beard, Robert T. Dirksen, Angela F. Dulhunty

Abstract

Although excitation-contraction (EC) coupling in skeletal muscle relies on physical activation of the skeletal ryanodine receptor (RyR1) Ca(2+) release channel by dihydropyridine receptors (DHPRs), the activation pathway between the DHPR and RyR1 remains unknown. However, the pathway includes the DHPR β1a subunit which is integral to EC coupling and activates RyR1. In this manuscript, we explore the isoform specificity of β1a activation of RyRs and the β1a binding site on RyR1. We used lipid bilayers to measure single channel currents and whole cell patch clamp to measure L-type Ca(2+) currents and Ca(2+) transients in myotubes. We demonstrate that both skeletal RyR1 and cardiac RyR2 channels in phospholipid bilayers are activated by 10-100 nM of the β1a subunit. Activation of RyR2 by 10 nM β1a was less than that of RyR1, suggesting a reduced affinity of RyR2 for β1a. A reduction in activation was also observed when 10 nM β1a was added to the alternatively spliced (ASI(-)) isoform of RyR1, which lacks ASI residues (A3481-Q3485). It is notable that the equivalent region of RyR2 also lacks four of five ASI residues, suggesting that the absence of these residues may contribute to the reduced 10 nM β1a activation observed for both RyR2 and ASI(-)RyR1 compared to ASI(+)RyR1. We also investigated the influence of a polybasic motif (PBM) of RyR1 (K3495KKRRDGR3502) that is located immediately downstream from the ASI residues and has been implicated in EC coupling. We confirmed that neutralizing the basic residues in the PBM (RyR1 K-Q) results in an ~50 % reduction in Ca(2+) transient amplitude following expression in RyR1-null (dyspedic) myotubes and that the PBM is also required for β1a subunit activation of RyR1 channels in lipid bilayers. These results suggest that the removal of β1a subunit interaction with the PBM in RyR1 could contribute directly to ~50 % of the Ca(2+) release generated during skeletal EC coupling. We conclude that the β1a subunit likely binds to a region that is largely conserved in RyR1 and RyR2 and that this region is influenced by the presence of the ASI residues and the PBM in RyR1.

Twitter Demographics

The data shown below were collected from the profiles of 5 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 12 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Japan 1 8%
Ireland 1 8%
Unknown 10 83%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 2 17%
Other 2 17%
Professor 1 8%
Student > Bachelor 1 8%
Student > Doctoral Student 1 8%
Other 3 25%
Unknown 2 17%
Readers by discipline Count As %
Agricultural and Biological Sciences 4 33%
Biochemistry, Genetics and Molecular Biology 3 25%
Business, Management and Accounting 1 8%
Pharmacology, Toxicology and Pharmaceutical Science 1 8%
Medicine and Dentistry 1 8%
Other 0 0%
Unknown 2 17%

Attention Score in Context

This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 18 August 2015.
All research outputs
#1,393,546
of 5,558,092 outputs
Outputs from Skeletal Muscle
#76
of 148 outputs
Outputs of similar age
#60,510
of 193,139 outputs
Outputs of similar age from Skeletal Muscle
#6
of 11 outputs
Altmetric has tracked 5,558,092 research outputs across all sources so far. This one has received more attention than most of these and is in the 63rd percentile.
So far Altmetric has tracked 148 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.6. This one is in the 45th percentile – i.e., 45% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 193,139 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 67% of its contemporaries.
We're also able to compare this research output to 11 others from the same source and published within six weeks on either side of this one. This one is in the 36th percentile – i.e., 36% of its contemporaries scored the same or lower than it.