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Mol Cell Biochem (2009) 328:25–32
DOI 10.1007/s11010-009-0070-0
Glutamate at position 227 of junctophilin-2 is involved in binding
to TRPC3
Jin Seok Woo Æ Ji-Hye Hwang Æ Jae-Kyun Ko Æ
Do Han Kim Æ Jianjie Ma Æ Eun Hui Lee
Received: 19 November 2008 / Accepted: 24 February 2009 / Published online: 10 March 2009
Springer Science+Business Media, LLC. 2009
Abstract Canonical-type transient receptor potential and/or TRPC3-mediated Ca2? homeostasis in skeletal
cation channel type 3 (TRPC3) allows the entry of extra- muscle.
cellular Ca2? and Na? into various cells. In mouse skeletal
myotubes, functional interaction between TRPC3 and Keywords RyR Excitation–contraction coupling
RyR1 (ryanodine receptor type 1/Ca2?-release channel on Junctional complex
sarcoplasmic reticulum membrane) regulates the gain of
excitation–contraction coupling. Junctophilin-2 (JP2) is a Abbreviations
TRPC3-interacting protein in mouse skeletal myotubes. TRPC3 Canonical-type transient receptor potential
Based on these knowledge from bona-fide TRPC3- cation channel type 3
expressing cells, to identify critical binding region(s) of RyR1 Ryanodine receptor type 1/Ca2?-release
JP2 that participate in binding to TRPC3, various JP2 channel
portions were subjected to co-immunoprecipitation assay JP Junctophilin
with intact TRPC3 from rabbit skeletal muscle. A region EC coupling Excitation–contraction coupling
covering 143 to 234 amino acids of JP2 (F1-2) was the PM Plasma membrane
most efficient portion binding to TRPC3. Through muta- PLC Phospholipase C
tional studies, we found that the binding ability of
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