TRPC3-interacting triadic proteins in skeletal muscle

Jin Seok Woo, Do Han Kim, Paul D. Allen, Eun Hui Lee

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

The expression of TRPC3 (canonical-type transient receptor potential cation channel type 3) is tightly regulated during skeletal muscle cell differentiation, and a functional interaction between TRPC3 and RyR1 [(ryanodine receptor type 1 ), an SR (sarcoplasmic reticulum) Ca2+-release channel] regulates the gain of SR Ca2+ release during EC (excitation-contraction) coupling. However, it has not been possible to demonstrate direct protein-protein interactions between TRPC3 and RyR1. To identify possible candidate(s) for a linker protein(s) between TRPC3 and RyR1 in skeletal muscle, in the present study we performed MALDITOF (matrix-assisted laser-desorption ionization-time-of-flight) MS analysis of a cross-linked triadic protein complex from rabbit skeletal triad vesicles and co-immunoprecipitation assays using primary mouse skeletal myotubes. From these studies, we found that six triadic proteins, that are known to regulate RyR1 function and/or EC coupling [TRPC1, JP2 (junctophilin 2), homer, mitsugumin 29, calreticulin and calmodulin], interacted directly with TRPC3 in a Ca 2+-independent manner. However we again found no direct interaction between TRPC3 and RyR1. TRPC1 was identified as a potential physical link between TRPC3 and RyR1, as it interacted with both TRPC3 and RyR1, and JPs showed subtype-specific interactions with both RyR1 and TRPC3 (JP1-RyR1 and JP2-TRPC3). These results support the hypothesis that TRPC3 and RyR1 are functionally engaged via linker proteins in skeletal muscle.

Original languageEnglish (US)
Pages (from-to)399-405
Number of pages7
JournalBiochemical Journal
Volume411
Issue number2
DOIs
StatePublished - Apr 15 2008
Externally publishedYes

Fingerprint

Transient Receptor Potential Channels
Ryanodine Receptor Calcium Release Channel
Muscle
Skeletal Muscle
Proteins
Excitation Contraction Coupling
Sarcoplasmic Reticulum
Calreticulin
Skeletal Muscle Fibers
Calmodulin
Immunoprecipitation
Muscle Cells
Ionization
Cell Differentiation
Assays
Desorption
Lasers

Keywords

  • Canonical-type transient receptor potential cation channel 1 (TRPC1)
  • Junctophilin
  • Ryanodine receptor (RyR)
  • TRPC3

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)

Cite this

Woo, J. S., Kim, D. H., Allen, P. D., & Lee, E. H. (2008). TRPC3-interacting triadic proteins in skeletal muscle. Biochemical Journal, 411(2), 399-405. https://doi.org/10.1042/BJ20071504

TRPC3-interacting triadic proteins in skeletal muscle. / Woo, Jin Seok; Kim, Do Han; Allen, Paul D.; Lee, Eun Hui.

In: Biochemical Journal, Vol. 411, No. 2, 15.04.2008, p. 399-405.

Research output: Contribution to journalArticle

Woo, JS, Kim, DH, Allen, PD & Lee, EH 2008, 'TRPC3-interacting triadic proteins in skeletal muscle', Biochemical Journal, vol. 411, no. 2, pp. 399-405. https://doi.org/10.1042/BJ20071504
Woo, Jin Seok ; Kim, Do Han ; Allen, Paul D. ; Lee, Eun Hui. / TRPC3-interacting triadic proteins in skeletal muscle. In: Biochemical Journal. 2008 ; Vol. 411, No. 2. pp. 399-405.
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