Crystal structures of the TRIC trimeric intracellular cation channel orthologues View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-12

AUTHORS

Go Kasuya, Masahiro Hiraizumi, Andrés D Maturana, Kaoru Kumazaki, Yuichiro Fujiwara, Keihong Liu, Yoshiko Nakada-Nakura, So Iwata, Keisuke Tsukada, Tomotaka Komori, Sotaro Uemura, Yuhei Goto, Takanori Nakane, Mizuki Takemoto, Hideaki E Kato, Keitaro Yamashita, Miki Wada, Koichi Ito, Ryuichiro Ishitani, Motoyuki Hattori, Osamu Nureki

ABSTRACT

Ca2+ release from the sarcoplasmic reticulum (SR) and endoplasmic reticulum (ER) is crucial for muscle contraction, cell growth, apoptosis, learning and memory. The trimeric intracellular cation (TRIC) channels were recently identified as cation channels balancing the SR and ER membrane potentials, and are implicated in Ca2+ signaling and homeostasis. Here we present the crystal structures of prokaryotic TRIC channels in the closed state and structure-based functional analyses of prokaryotic and eukaryotic TRIC channels. Each trimer subunit consists of seven transmembrane (TM) helices with two inverted repeated regions. The electrophysiological, biochemical and biophysical analyses revealed that TRIC channels possess an ion-conducting pore within each subunit, and that the trimer formation contributes to the stability of the protein. The symmetrically related TM2 and TM5 helices are kinked at the conserved glycine clusters, and these kinks are important for the channel activity. Furthermore, the kinks of the TM2 and TM5 helices generate lateral fenestrations at each subunit interface. Unexpectedly, these lateral fenestrations are occupied with lipid molecules. This study provides the structural and functional framework for the molecular mechanism of this ion channel superfamily. More... »

PAGES

1288

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/cr.2016.140

DOI

http://dx.doi.org/10.1038/cr.2016.140

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016102714

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27909292


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