Glutamate at position 227 of junctophilin-在227位谷氨酸junctophilin-227.pdf

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