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Journal of Molecular Biology
Article . 2004 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
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The Relative Position of RyR Feet and DHPR Tetrads in Skeletal Muscle

Authors: PAOLINI, CECILIA; PROTASI, Feliciano; FRANZINI ARMSTRONG C.;

The Relative Position of RyR Feet and DHPR Tetrads in Skeletal Muscle

Abstract

In skeletal muscle, L-type calcium channels (or dihydropyridine receptors, DHPRs) are coupled functionally to the calcium release channels of the sarcoplasmic reticulum (or ryanodine receptors, RyRs) within specialized structures called calcium release units (CRUs). The functional linkage requires a specific positioning of four DHPRs in correspondence of the four identical subunits of a single RyR type 1. Four DHPRs linked to the four binding sites of the RyR1 cytoplasmic domain (or foot), define the corners of a square, constituting a tetrad. RyRs self-assemble into ordered arrays and by associating with them, DHPRs also assemble into ordered arrays. The approximate location of the four DHPRs relative to the four identical subunits of a RyR-foot can be predicted on the basis of the relative position of tetrads and feet within the arrays. However, until recently one vital piece of information has been lacking: the orientation of the two arrays relative to one another. In this work we have defined the relative orientation of the RyR and DHPR arrays by directly superimposing replicas of rotary shadowed images of rows of feet, obtained from isolated SR vesicles, and replicas of tetrad arrays obtained by freeze-fracture. If the orientation for the two sets of images is carefully maintained, the superimposition provides specific constraints on the DHPR-RyR relative position.

Related Organizations
Keywords

Calcium Channels, L-Type, Macromolecular Substances, CALCIUM-RELEASE CHANNEL; II-III LOOP; RYANODINE RECEPTOR; DIHYDROPYRIDINE RECEPTOR; 3-DIMENSIONAL RECONSTRUCTION; ELECTRON CRYOMICROSCOPY; SARCOPLASMIC-RETICULUM; CA2+ CHANNEL; CELL-LINE; LOCALIZATION, Ryanodine Receptor Calcium Release Channel, Mice, Protein Subunits, Sarcoplasmic Reticulum, Animals, Freeze Fracturing, Muscle, Skeletal, Protein Structure, Quaternary

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
74
Top 10%
Top 10%
Top 10%
Green