Calsequestrin (CASQ) is the major component of the sarcoplasmic reticulum (SR) lumen in skeletal and cardiac muscles. This calcium-binding protein localizes to the junctional SR (jSR) cisternae, where it is responsible for the storage of large amounts of Ca2+, whereas it is usually absent, at least in its polymerized form, in the free SR. The retention of CASQ inside the jSR is due partly to its association with other jSR proteins, such as junctin and triadin, and partly to its ability to polymerize, in a high Ca2+ environment, into an intricate gel that holds the protein in place. In this work, we shed some light on the still poorly described in situ structure of polymerized CASQ using detailed EM images from thin sections, with and without tilting, and from deep-etched rotary-shadowed replicas. The latter directly illustrate the fundamental network nature of polymerized CASQ, revealing repeated nodal points connecting short segments of the linear polymer. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.

Perni, S., Close, M., Franzini-Armstrong, C. (2013). Novel Details of Calsequestrin Gel Conformation in Situ. JOURNAL OF BIOLOGICAL CHEMISTRY, 288(43), 31358-31362 [10.1074/jbc.M113.507749].

Novel Details of Calsequestrin Gel Conformation in Situ

Perni, S.
;
2013

Abstract

Calsequestrin (CASQ) is the major component of the sarcoplasmic reticulum (SR) lumen in skeletal and cardiac muscles. This calcium-binding protein localizes to the junctional SR (jSR) cisternae, where it is responsible for the storage of large amounts of Ca2+, whereas it is usually absent, at least in its polymerized form, in the free SR. The retention of CASQ inside the jSR is due partly to its association with other jSR proteins, such as junctin and triadin, and partly to its ability to polymerize, in a high Ca2+ environment, into an intricate gel that holds the protein in place. In this work, we shed some light on the still poorly described in situ structure of polymerized CASQ using detailed EM images from thin sections, with and without tilting, and from deep-etched rotary-shadowed replicas. The latter directly illustrate the fundamental network nature of polymerized CASQ, revealing repeated nodal points connecting short segments of the linear polymer. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.
Perni, S., Close, M., Franzini-Armstrong, C. (2013). Novel Details of Calsequestrin Gel Conformation in Situ. JOURNAL OF BIOLOGICAL CHEMISTRY, 288(43), 31358-31362 [10.1074/jbc.M113.507749].
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/1216056