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.