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Beard NA, Dulhunty AF. C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibition. Skelet Muscle. 2015;5:6doi: 10.1186/s13395-015-0029-7.
Beard, N. A., & Dulhunty, A. F. (2015). C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibition. Skeletal muscle, 56. https://doi.org/10.1186/s13395-015-0029-7
Beard, Nicole A, and Dulhunty, Angela F. "C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibition." Skeletal muscle vol. 5 (2015): 6. doi: https://doi.org/10.1186/s13395-015-0029-7
Beard NA, Dulhunty AF. C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibition. Skelet Muscle. 2015 Feb 22;5:6. doi: 10.1186/s13395-015-0029-7. eCollection 2015. PMID: 25861445; PMCID: PMC4389316.
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Skelet Muscle. 2015 Feb 22;5:6. doi: 10.1186/s13395-015-0029-7. eCollection 2015.

C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibition.

Skeletal muscle

Nicole A Beard, Angela F Dulhunty

Affiliations

  1. John Curtin School of Medical Research, Australian National University, Garran Road, Canberra, ACT 2601 Australia ; Discipline of Biomedical Sciences, Centre for Research in Therapeutic Solutions, Faculty of Education Science, Technology and Maths, University of Canberra, Kirinari Street, Bruce, ACT 2601 Australia.
  2. John Curtin School of Medical Research, Australian National University, Garran Road, Canberra, ACT 2601 Australia.

PMID: 25861445 PMCID: PMC4389316 DOI: 10.1186/s13395-015-0029-7

Abstract

BACKGROUND: Skeletal muscle function depends on calcium signaling proteins in the sarcoplasmic reticulum (SR), including the calcium-binding protein calsequestrin (CSQ), the ryanodine receptor (RyR) calcium release channel, and skeletal triadin 95 kDa (trisk95) and junctin, proteins that bind to calsequestrin type 1 (CSQ1) and ryanodine receptor type 1 (RyR1). CSQ1 inhibits RyR1 and communicates store calcium load to RyR1 channels via trisk95 and/or junctin.

METHODS: In this manuscript, we test predictions that CSQ1's acidic C-terminus contains binding sites for trisk95 and junctin, the major calcium binding domain, and that it determines CSQ1's ability to regulate RyR1 activity.

RESULTS: Progressive alanine substitution of C-terminal acidic residues of CSQ1 caused a parallel reduction in the calcium binding capacity but did not significantly alter CSQ1's association with trisk95/junctin or influence its inhibition of RyR1 activity. Deletion of the final seven residues in the C-terminus significantly hampered calcium binding, significantly reduced CSQ's association with trisk95/junctin and decreased its inhibition of RyR1. Deletion of the full C-terminus further reduced calcium binding to CSQ1 altered its association with trisk95 and junctin and abolished its inhibition of RyR1.

CONCLUSIONS: The correlation between the number of residues mutated/deleted and binding of calcium, trisk95, and junctin suggests that binding of each depends on diffuse ionic interactions with several C-terminal residues and that these interactions may be required for CSQ1 to maintain normal muscle function.

Keywords: Ca2+ binding protein; Calsequestrin; Ryanodine receptor; Sarcoplasmic reticulum; Skeletal muscle

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