Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle

Barbara A Block; Toshiaki Imagawa; Kevin P Campbell; Clara Franzini-Armstrong

doi:10.1083/jcb.107.6.2587

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Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle

Journal article

Open access

Peer reviewed

Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle

Barbara A Block, Toshiaki Imagawa, Kevin P Campbell and Clara Franzini-Armstrong

The Journal of cell biology, Vol.107(6 Pt 2), pp.2587-2600

12/1988

DOI: 10.1083/jcb.107.6.2587

PMID: 2849609

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Abstract

The architecture of the junctional sarcoplasmic reticulum (SR) and transverse tubule (T tubule) membranes and the morphology of the two major proteins isolated from these membranes, the ryanodine receptor (or foot protein) and the dihydropyridine receptor, have been examined in detail. Evidence for a direct interaction between the foot protein and a protein component of the junctional T tubule membrane is presented. Comparisons between freeze-fracture images of the junctional SR and rotary-shadowed images of isolated triads and of the isolated foot protein, show that the foot protein has two domains. One is the large hydrophilic foot which spans the junctional gap and is composed of four subunits. The other is a hydrophobic domain which presumably forms the SR Ca2+-release channel and which also has a fourfold symmetry. Freeze-fracture images of the junctional T tubule membranes demonstrate the presence of diamond-shaped clusters of particles that correspond exactly in position to the subunits of the feet protein. These results suggest the presence of a large junctional complex spanning the two junctional membranes and intervening gap. This junctional complex is an ideal candidate for a mechanical coupling hypothesis of excitation-contraction coupling at the triadic junction.

Rabbits

Calcium

Calcium Channels

Muscles - ultrastructure

Ryanodine Receptor Calcium Release Channel

Freeze Drying

Calcium Channel Blockers - analysis

Microscopy, Electron

Freeze Fracturing

Animals

Fishes

Receptors, Cholinergic - analysis

Receptors, Nicotinic - analysis

Microtubules - ultrastructure

Sarcoplasmic Reticulum - ultrastructure

Intercellular Junctions - ultrastructure

Details

Title: Subtitle: Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
Creators: Barbara A Block - Department of Biology, University of Pennsylvania, Philadelphia 19104
Toshiaki Imagawa
Kevin P Campbell
Clara Franzini-Armstrong
Resource Type: Journal article
Publication Details: The Journal of cell biology, Vol.107(6 Pt 2), pp.2587-2600
Publisher: United States
DOI: 10.1083/jcb.107.6.2587
PMID: 2849609
ISSN: 0021-9525
eISSN: 1540-8140
Grant note: HL-39265 / NHLBI NIH HHS HL-37187 / NHLBI NIH HHS HL-15838 / NHLBI NIH HHS
Language: English
Date published: 12/1988
Academic Unit: Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
Record Identifier: 9984020757502771

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