The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study.

C. Franzini-Armstrong, L. J. Kenney, E. Varriano-Marston

Research output: Contribution to journalArticle

158 Scopus citations

Abstract

We have examined the structure of calsequestrin in three-dimensional images from deep-etched rotary-replicated freeze fractures of skeletal muscle fibers. We selected a fast-acting muscle because the sarcoplasmic reticulum has an orderly disposition and is rich in internal membranes. Calsequestrin forms a network in the center of the terminal cisternae and is anchored to the sarcoplasmic reticulum membrane, with preference for the junctional portion. The anchorage is responsible for maintaining calsequestrin in the region of the sarcoplasmic reticulum close to the calcium-release channels, and it corroborates the finding that calsequestrin and the spanning protein of the junctional feet may interact with each other in the junctional membrane. Anchoring filaments may be composed of a protein other than calsequestrin.

Original languageEnglish (US)
Pages (from-to)49-56
Number of pages8
JournalThe Journal of cell biology
Volume105
Issue number1
DOIs
StatePublished - Jul 1987

ASJC Scopus subject areas

  • Cell Biology

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