PT  - JOURNAL ARTICLE
AU  - Numaga, Takuro
AU  - Nishida, Motohiro
AU  - Kiyonaka, Shigeki
AU  - Kato, Kenta
AU  - Katano, Masahiro
AU  - Mori, Emiko
AU  - Kurosaki, Tomohiro
AU  - Inoue, Ryuji
AU  - Hikida, Masaki
AU  - Putney, James W.
AU  - Mori, Yasuo
TI  - Ca<sup>2+</sup> influx and protein scaffolding via TRPC3 sustain PKCβ and ERK activation in B cells
AID  - 10.1242/jcs.061051
DP  - 2010 Mar 15
TA  - Journal of Cell Science
PG  - 927--938
VI  - 123
IP  - 6
4099  - http://jcs.biologists.org/content/123/6/927.short
4100  - http://jcs.biologists.org/content/123/6/927.full
SO  - J. Cell Sci.2010 Mar 15; 123
AB  - Ca2+ signaling mediated by phospholipase C that produces inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] and diacylglycerol (DAG) controls lymphocyte activation. In contrast to store-operated Ca2+ entry activated by Ins(1,4,5)P3-induced Ca2+ release from endoplasmic reticulum, the importance of DAG-activated Ca2+ entry remains elusive. Here, we describe the physiological role of DAG-activated Ca2+ entry channels in B-cell receptor (BCR) signaling. In avian DT40 B cells, deficiency of transient receptor potential TRPC3 at the plasma membrane (PM) impaired DAG-activated cation currents and, upon BCR stimulation, the sustained translocation to the PM of protein kinase Cβ (PKCβ) that activated extracellular signal-regulated kinase (ERK). Notably, TRPC3 showed direct association with PKCβ that maintained localization of PKCβ at the PM. Thus, TRPC3 functions as both a Ca2+-permeable channel and a protein scaffold at the PM for downstream PKCβ activation in B cells.